|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
436-1153 |
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: 1326.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRRKHITGARIS 595
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKHLTGARIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 596 TYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEHSLNKERLAALKHALNVIGF 675
Cdd:cd14878 161 TYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSLNREKLAVLKQALNVVGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 676 STLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQMAA 755
Cdd:cd14878 241 SSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 756 FYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQE 835
Cdd:cd14878 321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 836 QTECVQEGVAMETACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESSNTNAVYSPVKDGNGNVA 915
Cdd:cd14878 401 QTECVQEGVTMETAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYSPMKDGNGNVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 916 FKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLsqtgslissypsfkfgghkstlls 995
Cdd:cd14878 481 LKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL------------------------ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 996 krtassmvgvnknylelskllkkkgtstflqrlergepATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDH 1075
Cdd:cd14878 537 --------------------------------------VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDN 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953283 1076 FYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQAAEERCRLVLQRCKLQGWQIGVHKVFLK 1153
Cdd:cd14878 579 FYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
437-1153 |
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: 608.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSptGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRG--KGRSADLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCTMFDS-------RLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCqRRKHI 589
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSSKSSSsassieqQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD-PTGRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 590 TGARISTYMLEKSRVVAQPPGQGTFLIFSWLM----DGLSSEEKCGLHLNNFCAHRYVSQGmreDVSTAEHSLNKERLAA 665
Cdd:cd00124 159 VGASIETYLLEKSRVVSQAPGERNFHIFYQLLaglsDGAREELKLELLLSYYYLNDYLNSS---GCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 666 LKHALNVIGFSTLEVENLFVILSAILHIGDIQFT--ALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEedEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 744 VIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDeyKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKM 823
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTD--AAESTSFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 824 HHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESSNTNav 903
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDFPDNQD-CLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRF-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 904 YSPVKDGNGnvafkgqgaAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSenvvishlfqsklsqtgslissyps 983
Cdd:cd00124 471 FSKKRKAKL---------EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 984 fkfgghkstllskrtassmvgvnknylelskllkkkgtstflqrlergepataaSQLTKSLADITAKLQRGSPHFILCIK 1063
Cdd:cd00124 517 ------------------------------------------------------SQFRSQLDALMDTLNSTQPHFVRCIK 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1064 PNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA-SVLLGETKGQAAEERCRLVLQRCKLQG 1142
Cdd:cd00124 543 PNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILApGATEKASDSKKAAVLALLLLLKLDSSG 622
|
730
....*....|.
gi 568953283 1143 WQIGVHKVFLK 1153
Cdd:cd00124 623 YQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
424-1163 |
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: 570.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 424 SDDLATLSELNDSSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFH 503
Cdd:smart00242 8 VEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKY---RGKSRGELPPHVFAIADNAYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 504 RLFQERKPQNIILSGERGSGKTQASKQIMKYLTSRASSSCTmfDSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWE 579
Cdd:smart00242 85 NMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE--VGSVEDQILesnpILEAFGNAKTLRNNNSSRFGKFIE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 580 LQCCQRRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHL---NNFcahRYVSQGMREDVSTAEh 656
Cdd:smart00242 163 IHFDAKGK-IIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLkspEDY---RYLNQGGCLTVDGID- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 657 slNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSA-FVSDLQLLEQVAGMLQVSTDELASALTT 735
Cdd:smart00242 238 --DAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEKALTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 736 DIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEykslQTLDIGILDIFGFEEFQKNEFEQLC 815
Cdd:smart00242 316 RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG----STYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 816 VNLTNEKMHHYIQEVLFLQEQTECVQEGVAMeTACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLL 895
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDW-TFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 896 EssNTNAVYSPVKDGNgnvafkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTG 975
Cdd:smart00242 471 K--KHPHFSKPKKKGR---------TEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 976 SLISsypsfkfgghkstllskrtassmvgvnknylelskllkkkgtstflqrlergePATAASQLTKSLADITAKLQRGS 1055
Cdd:smart00242 540 SKKR-----------------------------------------------------FQTVGSQFKEQLNELMDTLNSTN 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1056 PHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLgETKGQAAEERCRLVL 1135
Cdd:smart00242 567 PHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTW-PPWGGDAKKACEALL 645
|
730 740 750
....*....|....*....|....*....|
gi 568953283 1136 QRCKL--QGWQIGVHKVFLKYWHVDQLSDL 1163
Cdd:smart00242 646 QSLGLdeDEYQLGKTKVFLRPGQLAELEEL 675
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
437-1153 |
8.83e-157 |
|
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: 496.80 E-value: 8.83e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLY---RGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcQRRKHITGARIST 596
Cdd:cd01379 79 SGESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKF-TSTGAVTGARISE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 597 YMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCG---LHLNNFCAHRYVSQGMREDVSTAEHslNKERLAALKHALNVI 673
Cdd:cd01379 158 YLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSG--NREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 674 GFSTLEVENLFVILSAILHIGDIQFTALTEAD----SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRH 749
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGDIEFTEVESNHqtdkSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 750 TIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQtLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQE 829
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEP-LSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 830 VLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESSNtnaVYSPvkd 909
Cdd:cd01379 395 HIFAWEQQEYLNEGIDVDLIEYEDNRP-LLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKY---YWRP--- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 910 gngnvafKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVIshlfqsklSQTgslISSYpsFKFggh 989
Cdd:cd01379 468 -------KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV--------RQT---VATY--FRY--- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 990 kstllskrtassmvgvnknylelskllkkkgtstflqrlergepataasqltkSLADITAKLQRGSPHFILCIKPNTSQL 1069
Cdd:cd01379 525 -----------------------------------------------------SLMDLLSKMVVGQPHFVRCIKPNDSRQ 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1070 PGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLlgETKGQAAEERCRLVLQRCKLQGWQIGVHK 1149
Cdd:cd01379 552 AGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDNWALGKTK 629
|
....
gi 568953283 1150 VFLK 1153
Cdd:cd01379 630 VFLK 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
425-1153 |
5.26e-153 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 487.94 E-value: 5.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 425 DDLATLSELNDSSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHR 504
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAY---RGKRRGELPPHIFAIADEAYRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 505 LFQERKPQNIILSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWEL 580
Cdd:pfam00063 79 MLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILqsnpILEAFGNAKTVRNNNSSRFGKYIEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 581 QCCQRRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEHSlnk 660
Cdd:pfam00063 159 QFDAKGD-IVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 661 ERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 741 KGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclQNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTN 820
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRIN---KSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 821 EKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESqviwsgepNLPRK-----LQGLL 895
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQP-CIDLIEKKPLGILSLLDEEC--------LFPKAtdqtfLDKLY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 896 ESSNTNAVYSPVKdgngnvaFKGQgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSklsqtG 975
Cdd:pfam00063 463 STFSKHPHFQKPR-------LQGE-THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD-----Y 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 976 SLISSYPSFKFGGHKstllSKRTASSMvgvnknylelskllkkkgtstflqrlergePATAASQLTKSLADITAKLQRGS 1055
Cdd:pfam00063 530 ETAESAAANESGKST----PKRTKKKR------------------------------FITVGSQFKESLGELMKTLNSTN 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1056 PHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGqAAEERCRLVL 1135
Cdd:pfam00063 576 PHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-DAKKGCEAIL 654
|
730 740
....*....|....*....|
gi 568953283 1136 QRCKLQG--WQIGVHKVFLK 1153
Cdd:pfam00063 655 QSLNLDKeeYQFGKTKIFFR 674
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
437-1153 |
2.47e-140 |
|
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: 451.45 E-value: 2.47e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQRSPslPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQR--PPHLFWIADQAYRRLLETGRNQCILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRrKHITGARIST 596
Cdd:cd14897 80 SGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTEN-GQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 597 YMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHR-----YVSQGMREDVSTAEHSLNK--ERLAALKHa 669
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRilrddNRNRPVFNDSEELEYYRQMfhDLTNIMKL- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 670 lnvIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRH 749
Cdd:cd14897 238 ---IGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 750 TIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQ-NQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQ 828
Cdd:cd14897 315 SLRQANDSRDALAKDLYSRLFGWIVGQINRNLWpDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 829 EVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESSNTnavYSPVK 908
Cdd:cd14897 395 DYVFPRERSEYEIEGIEWRDIEYHDNDD-VLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR---YVASP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 909 DGNgnvafkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFqsklsqtgslissypsfkfgg 988
Cdd:cd14897 471 GNR---------VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 989 hkstllskrtassmvgvnknylelskllkkkgtstflqrlergepataASQLTKSLADITAKLQRGSPHFILCIKPNTSQ 1068
Cdd:cd14897 521 ------------------------------------------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFL 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1069 LPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLasVLLGETKGQAAEERCRLVLQRCKLQGWQIGVH 1148
Cdd:cd14897 553 RPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEI--CDFSNKVRSDDLGKCQKILKTAGIKGYQFGKT 630
|
....*
gi 568953283 1149 KVFLK 1153
Cdd:cd14897 631 KVFLK 635
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
425-1230 |
7.79e-139 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 471.10 E-value: 7.79e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 425 DDLATLSELNDSSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHR 504
Cdd:COG5022 69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY---SGKNRLELEPHVFAIAEEAYRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 505 LFQERKPQNIILSGERGSGKTQASKQIMKYLTSRASSSCTM---FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQ 581
Cdd:COG5022 146 LLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEissIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 582 CCQRRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEhslNKE 661
Cdd:COG5022 226 FDENGE-ICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGID---DAK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 662 RLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTAlTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 741
Cdd:COG5022 302 EFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 742 GDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNE 821
Cdd:COG5022 381 GEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNF----IGVLDIYGFEIFEKNSFEQLCINYTNE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 822 KMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLeSSNTN 901
Cdd:COG5022 457 KLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQRL-NKNSN 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 902 AVYSPVKdgngnvaFKGQGaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQsklsqtgslissy 981
Cdd:COG5022 536 PKFKKSR-------FRDNK--FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFD------------- 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 982 psfkfgghkstllskrtassmVGVNKNylelskllkkkgtstflqrlERGEPATAASQLTKSLADITAKLQRGSPHFILC 1061
Cdd:COG5022 594 ---------------------DEENIE--------------------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRC 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1062 IKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYE---PLASVLLGETKGQAAEERCRLVLQRC 1138
Cdd:COG5022 633 IKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRilsPSKSWTGEYTWKEDTKNAVKSILEEL 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1139 KL--QGWQIGVHKVFLK-------------YWH--VDQLSDLW---------LQLQRKIVTCQKVIRGFLARQHLlqRMS 1192
Cdd:COG5022 713 VIdsSKYQIGNTKVFFKagvlaaledmrdaKLDniATRIQRAIrgrylrrryLQALKRIKKIQVIQHGFRLRRLV--DYE 790
|
810 820 830
....*....|....*....|....*....|....*....
gi 568953283 1193 IKQQEVTSIKSFLQSTEDMA-LKTYDALVIQNASDIARE 1230
Cdd:COG5022 791 LKWRLFIKLQPLLSLLGSRKeYRSYLACIIKLQKTIKRE 829
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
1235-1605 |
3.77e-133 |
|
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: 421.11 E-value: 3.77e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1235 RKEVHTAyhRNRQEEGTKRAEDQG---------GCRHVHSNSVPVPMVVDSL-AQALTGPSTRPPSLHSVFSMDDSTGLP 1304
Cdd:pfam15439 3 RKEKLEK--RRRQEEGIKRSGEEVagkvrdissEGRHFRMGFMTMPASQDRLpHPCAAGMSIRSQSLHSVGSGDEDGSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1305 SPRKQPPPKPKRDPNTRLSASYEAVSACLS-AAKDAAG--EALTRPRPHSDDYStmKKIPPRKPKRSPHTKLSGSYEEIW 1381
Cdd:pfam15439 81 SSRKQPPPKPKRDPSTKLSMSSEAVSAGLSaGAKETPSetEALSKPRPHSDEYS--RKIPPPKPKRSPNTQLSGSFDEIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1382 GP-PRPSGTMgqggrhqapgtlsvQWARPDSVPQCTpqlplhlplpqGDYDDDAEPVYIEMVGNAARAGG--SETDSPDQ 1458
Cdd:pfam15439 159 APyIRPHGLL--------------QRASSSDGPSPA-----------PLPDEEEEPVYIEMVGNVLRDFSptTPDDDPDQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1459 GESVYEEMKYILPEEGCGLGMLTFLpASPPLFLETRKAIILEAAEGNC------QPSKDTCDIPPPFPNLLPHRPPLLVF 1532
Cdd:pfam15439 214 SEAVYEEMKYPLPEDSGAANGPPPL-ASSPLLADPHSPISPESDSALPssqcatPTKKDLCDIPAPFPNLLPHRPPLLVF 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568953283 1533 PPTPVTRSPASDESPLTPLEVKKLPVLEtNLKYPVQSEgSSPLSPQYSKAQKGDNDQLASPGFPVFNGPSRIS 1605
Cdd:pfam15439 293 PPAPVTCSPASDESPLTPLEVKKLPVLE-NVSYSKQPA-SSPLSPQESKHQREDKDRPSSPGLAVLTPSGRAR 363
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
438-1153 |
1.35e-132 |
|
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: 430.87 E-value: 1.35e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 438 LLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSptgQRSPSLPPHLFSCAERAFH----RLFQERKPQN 513
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKC---EKKSSLPPHIFAVADRAYQsmlgRLARGPKNQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 514 IILSGERGSGKTQASKQIMKYLTSRASSScTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcqRRKHITGAR 593
Cdd:cd14889 80 IVISGESGAGKTESTKLLLRQIMELCRGN-SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF--RNGHVKGAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 594 ISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQ--GMREDVSTAehslnKERLAALKHALN 671
Cdd:cd14889 157 INEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREVQYW-----KKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 672 VIGFSTLEVENLFVILSAILHIGDIQFTaLTEADSAFVSDLQ--LLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRH 749
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFE-MDDDEALKVENDSngWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 750 TIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYkSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQE 829
Cdd:cd14889 311 TKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDS-SVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 830 VLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESsntNAVYSPVKD 909
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITYKDNKP-ILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG---NSYYGKSRS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 910 gngnvafkgQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSLISSYPSFKFGGH 989
Cdd:cd14889 466 ---------KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 990 KstllskrtassmvgvnknylelskllkkkGTSTFLQrlergepaTAASQLTKSLADITAKLQRGSPHFILCIKPNTSQL 1069
Cdd:cd14889 537 N-----------------------------FNSTRKQ--------SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKV 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1070 PGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYeplaSVLLGETKGQAAEERCRLVLQRCKLQGWQIGVHK 1149
Cdd:cd14889 580 PGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERY----KILLCEPALPGTKQSCLRILKATKLVGWKCGKTR 655
|
....
gi 568953283 1150 VFLK 1153
Cdd:cd14889 656 LFFK 659
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
436-1153 |
1.22e-128 |
|
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: 419.81 E-value: 1.22e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQY---FGKRMGALPPHIFALAEAAYTNMQEDGKNQSVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSScTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELqCCQRRKHITGARIS 595
Cdd:cd14883 78 ISGESGAGKTETTKLILQYLCAVTNNH-SWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEV-CFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 596 TYMLEKSRVVAQPPGQGTFLIFSWLMDG--LSSEEKCGLHLNNFCAHRYVSQgmrEDVSTAEHSLNKERLAALKHALNVI 673
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQ---SGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 674 GFSTLEVENLFVILSAILHIGDIQFTALTEADSAF-VSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQ 752
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 753 MAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLF 832
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF----IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 833 LQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESsntNAVYspVKDgng 912
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFTDNQE-CLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEK---HPYY--EKP--- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 913 nvAFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFqsklsqtgslisSYPSFKFGGHKST 992
Cdd:cd14883 460 --DRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELF------------TYPDLLALTGLSI 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 993 LLSKRTASSMVGVNKnylelskllkkkgtstflqrlergepATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGV 1072
Cdd:cd14883 526 SLGGDTTSRGTSKGK--------------------------PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNV 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1073 FDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEplasVLLGETKGQAAEERCRLVLQRCKLQG-----WQIGV 1147
Cdd:cd14883 580 FDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL----CLDPRARSADHKETCGAVRALMGLGGlpedeWQVGK 655
|
....*.
gi 568953283 1148 HKVFLK 1153
Cdd:cd14883 656 TKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
442-1153 |
1.21e-125 |
|
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: 410.78 E-value: 1.21e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 442 IQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIILSGERG 521
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESY---RGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 522 SGKTQASKQIMKYLTSrASSSCTMFDSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWELQ-------Ccqrrkhit 590
Cdd:cd01378 84 AGKTEASKRIMQYIAA-VSGGSESEVERVKDMLLasnpLLEAFGNAKTLRNDNSSRFGKYMEIQfdfkgepV-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 591 GARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEhslNKERLAALKHAL 670
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGID---DAADFKEVLNAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 671 NVIGFSTLEVENLFVILSAILHIGDIQFTAlTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD---VIIR 747
Cdd:cd01378 232 KVIGFTEEEQDSIFRILAAILHLGNIQFAE-DEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 748 RHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQdeyKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHH-Y 826
Cdd:cd01378 311 PLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAK---SGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQiF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 827 IQEVLfLQEQTECVQEGVAMETacspgnqagvLDFFF---------QKPSGFFSLLDEEsqVIWSGEPNLPRKLQGLLES 897
Cdd:cd01378 388 IELTL-KAEQEEYVREGIEWTP----------IKYFNnkiicdlieEKPPGIFAILDDA--CLTAGDATDQTFLQKLNQL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 898 SNTNAVYSPVKDgngnvAFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTgsl 977
Cdd:cd01378 455 FSNHPHFECPSG-----HFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD--- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 978 issypsfkfgghkstllSKRtassmvgvnknylelskllkkkgtstflqrlergEPATAASQLTKSLADITAKLQRGSPH 1057
Cdd:cd01378 527 -----------------SKK----------------------------------RPPTAGTKFKNSANALVETLMKKQPS 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1058 FILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPL---------------ASVLLGET 1122
Cdd:cd01378 556 YIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLspktwpawdgtwqggVESILKDL 635
|
730 740 750
....*....|....*....|....*....|.
gi 568953283 1123 KGQAAEercrlvlqrcklqgWQIGVHKVFLK 1153
Cdd:cd01378 636 NIPPEE--------------YQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
436-1153 |
9.57e-124 |
|
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: 405.48 E-value: 9.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLY---RNKKIGELPPHIFAIADNAYTNMKRNKRDQCVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSrASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRRKhITGARIS 595
Cdd:cd01381 78 ISGESGAGKTESTKLILQYLAA-ISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV-IEGAKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 596 TYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGmreDVSTAEHSLNKERLAALKHALNVIGF 675
Cdd:cd01381 156 QYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQG---NCLTCEGRDDAAEFADIRSAMKVLMF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 676 STLEVENLFVILSAILHIGDIQFTALTEA--DSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQM 753
Cdd:cd01381 233 TDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 754 AAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEyKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFL 833
Cdd:cd01381 313 ALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRG-TDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 834 QEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGlLESSNTNAVySPVKDGNgn 913
Cdd:cd01381 392 LEQEEYDKEGINWQHIEFVDNQD-VLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHS-THGNNKNYL-KPKSDLN-- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 914 vafkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQtgslissypsfkfgghkstl 993
Cdd:cd01381 467 -------TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM-------------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 994 lskrtassmvgvnknylelskllkkkGTSTflqrleRGEPATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVF 1073
Cdd:cd01381 520 --------------------------GSET------RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLF 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1074 DHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKG---QAAEERCRLVLQRCKLqgWQIGVHKV 1150
Cdd:cd01381 568 DRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTdcrAATRKICCAVLGGDAD--YQLGKTKI 645
|
...
gi 568953283 1151 FLK 1153
Cdd:cd01381 646 FLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
437-1153 |
2.13e-122 |
|
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: 401.31 E-value: 2.13e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlsptGQRSpSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY----RQKL-LDSPHVYAVADTAYREMMRDEINQSIII 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCTMfDSRLRHAIYIVEAFGHAKTTLNNVSS---CLIQYwelqCCQRRKHITGAR 593
Cdd:cd01383 77 SGESGAGKTETAKIAMQYLAALGGGSSGI-ENEILQTNPILEAFGNAKTLRNDNSSrfgKLIDI----HFDAAGKICGAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 594 ISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGmreDVSTAEHSLNKERLAALKHALNVI 673
Cdd:cd01383 152 IQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQS---NCLTIDGVDDAKKFHELKEALDTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 674 GFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQM 753
Cdd:cd01383 229 GISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 754 AAFYRDLLAKSLYSRLFGFLINTVNCCLQ--NQDEYKSlqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVL 831
Cdd:cd01383 309 AIDARDALAKAIYASLFDWLVEQINKSLEvgKRRTGRS-----ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 832 FLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLessntnavyspvkdgN 911
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDFEDNQE-CLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHL---------------K 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 912 GNVAFKG-QGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENvVISHLFQSKLSQTG-SLISSYPSFKFGGH 989
Cdd:cd01383 448 SNSCFKGeRGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSC-QLPQLFASKMLDASrKALPLTKASGSDSQ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 990 KSTLLSKrtassmvgvnknylelskllkkkgtstFlqrlergepataASQLTKSLaditAKLQRGSPHFILCIKPNTSQL 1069
Cdd:cd01383 527 KQSVATK---------------------------F------------KGQLFKLM----QRLENTTPHFIRCIKPNNKQL 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1070 PGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEplasVLLGETKG--QAAEERCRLVLQRCKLQG--WQI 1145
Cdd:cd01383 564 PGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYG----FLLPEDVSasQDPLSTSVAILQQFNILPemYQV 639
|
....*...
gi 568953283 1146 GVHKVFLK 1153
Cdd:cd01383 640 GYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
439-1153 |
2.27e-120 |
|
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: 395.51 E-value: 2.27e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 439 LYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIILS 517
Cdd:cd01384 4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQY---KGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 518 GERGSGKTQASKQIMKYLT---SRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcQRRKHITGARI 594
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAymgGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQF-DDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 595 STYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQG---MREDVSTAEhslnkERLAALKhALN 671
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSkcfELDGVDDAE-----EYRATRR-AMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 672 VIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSD---LQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRR 748
Cdd:cd01384 234 VVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 749 HTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKM-HHYI 827
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL----IGVLDIYGFESFKTNSFEQFCINLANEKLqQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 828 QEVlFLQEQTECVQEGVAMETACSPGNQaGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLqgllessntnavYSPV 907
Cdd:cd01384 390 QHV-FKMEQEEYTKEEIDWSYIEFVDNQ-DVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKL------------YQTL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 908 KDGNGNVAFKGQGAAFTVMHYAGRVMYEMGGAVERNKD---SLSQNLLfvmKTSENVVISHLFQSKLSQTGSlissyPSF 984
Cdd:cd01384 456 KDHKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDyvvAEHQALL---NASKCPFVAGLFPPLPREGTS-----SSS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 985 KFgghkstllskrtasSMVGvnknylelskllkkkgtstflqrlergepataaSQLTKSLADITAKLQRGSPHFILCIKP 1064
Cdd:cd01384 528 KF--------------SSIG---------------------------------SRFKQQLQELMETLNTTEPHYIRCIKP 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1065 NTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLAS-VLLGETKGQAAeerCRLVLQRCKLQGW 1143
Cdd:cd01384 561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPeVLKGSDDEKAA---CKKILEKAGLKGY 637
|
730
....*....|
gi 568953283 1144 QIGVHKVFLK 1153
Cdd:cd01384 638 QIGKTKVFLR 647
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
437-1153 |
2.44e-119 |
|
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: 394.44 E-value: 2.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMY---QNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRassSCTMFDSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWELQCcQRRKHITGA 592
Cdd:cd01385 79 SGESGSGKTESTNFLLHHLTAL---SQKGYGSGVEQTILgagpVLEAFGNAKTAHNNNSSRFGKFIQVNY-RENGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 593 RISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQgmrEDVSTAEHSLNKERLAALKHALNV 672
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQ---SDCYTLEGEDEKYEFERLKQAMEM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 673 IGFSTLEVENLFVILSAILHIGDIQFT--ALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHT 750
Cdd:cd01385 232 VGFLPETQRQIFSVLSAVLHLGNIEYKkkAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 751 IQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEV 830
Cdd:cd01385 312 LPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 831 LFLQEQTECVQEGVAM-------ETACspgnqagvLDFFFQKPSGFFSLLDEESqviwsgepNLPRKL-QGLLE------ 896
Cdd:cd01385 392 IFKLEQEEYKKEGISWhnieytdNTGC--------LQLISKKPTGLLCLLDEES--------NFPGATnQTLLAkfkqqh 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 897 SSNTNAVYSPVKDgngnvafkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHL--------FQ 968
Cdd:cd01385 456 KDNKYYEKPQVME-----------PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavFR 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 969 SKLSQTgsLISSYPSFKFGGhkstllsKRTASSMVGVNKNYlelskllKKKGTSTFLQRLERGEPATAASQLTKSLADIT 1048
Cdd:cd01385 525 WAVLRA--FFRAMAAFREAG-------RRRAQRTAGHSLTL-------HDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLM 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1049 AKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYeplaSVLLGETKGQAAE 1128
Cdd:cd01385 589 ETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQF----QVLLPKGLISSKE 664
|
730 740
....*....|....*....|....*..
gi 568953283 1129 ERCrLVLQRCKLQ--GWQIGVHKVFLK 1153
Cdd:cd01385 665 DIK-DFLEKLNLDrdNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
437-1153 |
1.45e-116 |
|
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: 384.92 E-value: 1.45e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQY---SRRHLGELPPHIFAIANECYRCLWKRHDNQCIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTS----RASSSCTMFDSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWELQCCQRrK 587
Cdd:cd14873 79 ISGESGAGKTESTKLILKFLSVisqqSLELSLKEKTSCVEQAILesspIMEAFGNAKTVYNNNSSRFGKFVQLNICQK-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 588 HITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQgmrEDVSTAEHSLNKERLAALK 667
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQ---SGCVEDKTISDQESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 668 HALNVIGFSTLEVENLFVILSAILHIGDIQFTAlteADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIR 747
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 748 RHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSlqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYI 827
Cdd:cd14873 312 PLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS-----IGILDIFGFENFEVNHFEQFNINYANEKLQEYF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 828 QEVLFLQEQTECVQEGVAMEtACSPGNQAGVLDfFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGlLESSNTNAVYSPV 907
Cdd:cd14873 387 NKHIFSLEQLEYSREGLVWE-DIDWIDNGECLD-LIEKKLGLLALINEESHFPQATDSTLLEKLHS-QHANNHFYVKPRV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 908 KDGNgnvafkgqgaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGslissypsfkfg 987
Cdd:cd14873 464 AVNN-----------FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNN------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 988 ghKSTLlskRTASsmvgvnknylelskllkkkgtstflqrlERGEPaTAASQLTKSLADITAKLQRGSPHFILCIKPNTS 1067
Cdd:cd14873 521 --QDTL---KCGS----------------------------KHRRP-TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQ 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1068 QLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASvllGETKGQAAEERCRLVLQRCKLQG--WQI 1145
Cdd:cd14873 567 KMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMR---NLALPEDVRGKCTSLLQLYDASNseWQL 643
|
....*...
gi 568953283 1146 GVHKVFLK 1153
Cdd:cd14873 644 GKTKVFLR 651
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
436-1153 |
1.19e-115 |
|
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: 382.56 E-value: 1.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQY---SGRALGELPPHLFAIANLAFAKMLDAKQNQCVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcqRRKHITGARIS 595
Cdd:cd01387 78 ISGESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF--EGGVIVGAITS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 596 TYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEHSLNKERLAAlkhALNVIGF 675
Cdd:cd01387 156 QYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLA---AMQVLGF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 676 STLEVENLFVILSAILHIGDIQFTALTEADS----AFVSDLQlLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTI 751
Cdd:cd01387 233 SSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegvSVGSDAE-IQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 752 QMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEykslQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVL 831
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQ----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 832 FLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESqviwsgepNLPRK-----LQGLLESSNTNAVYSP 906
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAFADNQP-VINLISKKPVGILHILDDEC--------NFPQAtdhsfLEKCHYHHALNELYSK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 907 VKDGngnvafkgqGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQtgslissypsfkf 986
Cdd:cd01387 459 PRMP---------LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 987 ggHKSTLLSKrtassmvgvnknylelskllkkkGTSTFLQRLERGEpaTAASQLTKSLADITAKLQRGSPHFILCIKPNT 1066
Cdd:cd01387 517 --TDKAPPRL-----------------------GKGRFVTMKPRTP--TVAARFQDSLLQLLEKMERCNPWFVRCLKPNH 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1067 SQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPL-ASVLLGETKGQAAEERCRLVLQRCKLQGWQI 1145
Cdd:cd01387 570 KKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLvALKLPRPAPGDMCVSLLSRLCTVTPKDMYRL 649
|
....*...
gi 568953283 1146 GVHKVFLK 1153
Cdd:cd01387 650 GATKVFLR 657
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
437-1153 |
3.63e-115 |
|
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: 381.43 E-value: 3.63e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGdIFLL-VNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSG-LFCVaVNPYKRLPIYTEEVIDKY---KGKRREEMPPHIFAIADNAYRNMLQDRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRH---------AIYIVEAFGHAKTTLNNVSScliqywelqccqR- 585
Cdd:cd01377 78 ITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledqilqANPILEAFGNAKTVRNNNSS------------Rf 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 586 ----RKH------ITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHR-YVSQGmredVSTA 654
Cdd:cd01377 146 gkfiRIHfgstgkIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQG----ELTI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 655 EHSLNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALT 734
Cdd:cd01377 222 DGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 735 TDIqyFK-GDVIIRRH-TIQMAAFYRDLLAKSLYSRLFGFLINTVNcclqnqdeykslQTLD--------IGILDIFGFE 804
Cdd:cd01377 302 KPR--IKvGREWVTKGqNKEQVVFSVGALAKALYERLFLWLVKRIN------------KTLDtkskrqyfIGVLDIAGFE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 805 EFQKNEFEQLCVNLTNEKM-----HHyiqevLFLQEQTECVQEGVAMEtacspgnqagVLDF---------FFQKPS-GF 869
Cdd:cd01377 368 IFEFNSFEQLCINYTNEKLqqffnHH-----MFVLEQEEYKKEGIEWT----------FIDFgldlqptidLIEKPNmGI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 870 FSLLDEESQViwsgePN-----LPRKLQGLLESSNTNAVYSPVKDGNgnvafkgqgAAFTVMHYAGRVMYEMGGAVERNK 944
Cdd:cd01377 433 LSILDEECVF-----PKatdktFVEKLYSNHLGKSKNFKKPKPKKSE---------AHFILKHYAGDVEYNIDGWLEKNK 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 945 DSLSQNLLFVMKTSENVVISHLFqsklsqtgsliSSYPSFKFGGHKstllsKRTASSMvgvnknylelskllkkkgtstF 1024
Cdd:cd01377 499 DPLNENVVALLKKSSDPLVASLF-----------KDYEESGGGGGK-----KKKKGGS---------------------F 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1025 LqrlergepaTAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSF 1104
Cdd:cd01377 542 R---------TVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIF 612
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 568953283 1105 EDFLSRYEPLA--SVLLGETKGQAAeerCRLVLQRCKL--QGWQIGVHKVFLK 1153
Cdd:cd01377 613 AEFKQRYSILApnAIPKGFDDGKAA---CEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
437-1135 |
3.65e-115 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 380.66 E-value: 3.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQRspsLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKE---MPPHTYNIADDAYRAMIVDAMNQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCTMfDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRrKHITGARIST 596
Cdd:cd14872 79 SGESGAGKTEATKQCLSFFAEVAGSTNGV-EQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNR-GRICGASTEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 597 YMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLhlNNFCAHRYVSQGMREDVSTAEHSLNKERLaalKHALNVIGFS 676
Cdd:cd14872 157 YLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSLSGCIEVEGVDDVADFEEV---VLAMEQLGFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 677 TLEVENLFVILSAILHIGDIQFTAL---TEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG--DVIIRRHTI 751
Cdd:cd14872 232 DADINNVMSLIAAILKLGNIEFASGggkSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPTRIPLTPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 752 QmAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQdeyKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVL 831
Cdd:cd14872 312 Q-ATDACDALAKAAYSRLFDWLVKKINESMRPQ---KGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 832 FLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQgllessNTNAVYSPVKDGN 911
Cdd:cd14872 388 FKLEEALYQSEGVKFEHIDFIDNQP-VLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN------QTHAAKSTFVYAE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 912 gnvaFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFqsklsqtgslissyPSFkfgghks 991
Cdd:cd14872 461 ----VRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------PPS------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 992 tLLSKRTASsmvgvnknylelskllkkkgtstflqrlergepATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPG 1071
Cdd:cd14872 516 -EGDQKTSK---------------------------------VTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRAR 561
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568953283 1072 VFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVlLGETKGQAAEERCRLVL 1135
Cdd:cd14872 562 LFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKT-IAKRVGPDDRQRCDLLL 624
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
437-1153 |
3.35e-114 |
|
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: 377.27 E-value: 3.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQ-IHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd01380 2 AVLHNLKVRFCQRNaIYTYCGIVLVAINPYEDLPIYGEDIIQAY---SGQNMGELDPHIFAIAEEAYRQMARDEKNQSII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMfdSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWELQCCQrRKHITG 591
Cdd:cd01380 79 VSGESGAGKTVSAKYAMRYFATVGGSSSGE--TQVEEKVLasnpIMEAFGNAKTTRNDNSSRFGKYIEILFDK-NYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 592 ARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEhslNKERLAALKHALN 671
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVD---DAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 672 VIGFSTLEVENLFVILSAILHIGDIQFTAlTEADSAFVS-DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHT 750
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKA-TRNDSASISpDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 751 IQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKslQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKM-HHYIQE 829
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEK--QHSFIGVLDIYGFETFEVNSFEQFCINYANEKLqQQFNQH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 830 VlFLQEQTECVQEGVAMETACSPGNQAgVLDfFFQKPSGFFSLLDEESQVIWSGEPNLPRKL-QGLLESSntNAVYSPVK 908
Cdd:cd01380 390 V-FKLEQEEYVKEEIEWSFIDFYDNQP-CID-LIEGKLGILDLLDEECRLPKGSDENWAQKLyNQHLKKP--NKHFKKPR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 909 DGNGnvafkgqgaAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENvvishlfqsklsqtgslissypsfkfgg 988
Cdd:cd01380 465 FSNT---------AFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 989 HKSTLlskrtassmvgvnknylelskllkkkgtstflqrlergepataASQLTKSLADITAKLQRGSPHFILCIKPNTSQ 1068
Cdd:cd01380 508 RKKTV-------------------------------------------GSQFRDSLILLMETLNSTTPHYVRCIKPNDEK 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1069 LPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASvlLGETKGQAAEERCRLVLQRCKL--QGWQIG 1146
Cdd:cd01380 545 LPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLP--SKEWLRDDKKKTCENILENLILdpDKYQFG 622
|
....*..
gi 568953283 1147 VHKVFLK 1153
Cdd:cd01380 623 KTKIFFR 629
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
436-1123 |
5.62e-111 |
|
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: 369.75 E-value: 5.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSPTGQRSP-----SLPPHLFSCAERAFHRLFQER 509
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQNGEyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 510 KPQNIILSGERGSGKTQASKQIMKYLTS-----RASSSCTMFDSRLRHAIY--------------IVEAFGHAKTTLNNV 570
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQlsqqeQNSEEVLTLTSSIRATSKstksieqkilscnpILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 571 SSCLIQYWELQCCQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNN---FCAHRYVSQGM 647
Cdd:cd14907 161 SSRFGKYVSILVDKKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 648 REDVSTaehsLNKERL-AALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAF--VSDLQLLEQVAGMLQV 724
Cdd:cd14907 241 CYEVDT----INDEKLfKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPccVKNKETLQIIAKLLGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 725 STDELASALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCL----QNQDEYKSLQTLDIGILDI 800
Cdd:cd14907 317 DEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdEKDQQLFQNKYLSIGLLDI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 801 FGFEEFQKNEFEQLCVNLTNEKMHH-YIQEVlFLQEQTECVQEGVA--METACSPGNQaGVLDFFFQKPSGFFSLLDEES 877
Cdd:cd14907 397 FGFEVFQNNSFEQLCINYTNEKLQQlYISYV-FKAEEQEFKEEGLEdyLNQLSYTDNQ-DVIDLLDKPPIGIFNLLDDSC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 878 QVIWSGEPNLPRKLQgllESSNTNAVYSPVKdgngnvafKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKT 957
Cdd:cd14907 475 KLATGTDEKLLNKIK---KQHKNNSKLIFPN--------KINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 958 SENVVISHLF----QSKLSQTGSLISSYPSFKFGGHKstllskrtassmvgvnknylelskllkkkgtstFLQRLergep 1033
Cdd:cd14907 544 SKNRIISSIFsgedGSQQQNQSKQKKSQKKDKFLGSK---------------------------------FRNQM----- 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1034 ataasqltKSLADitaKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEP 1113
Cdd:cd14907 586 --------KQLMN---ELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSL 654
|
730
....*....|.
gi 568953283 1114 L-ASVLLGETK 1123
Cdd:cd14907 655 LkKNVLFGKTK 665
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
436-1153 |
6.51e-110 |
|
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: 365.64 E-value: 6.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFhRLFQERKP-QNI 514
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASY---HPRKALNTTPHIFAIAASAY-RLSQSTGQdQCI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 515 ILSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYweLQCCQRRKHITGARI 594
Cdd:cd14896 77 LLSGHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQV--LRLHLQHGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 595 STYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEhslNKERLAALKHALNVIG 674
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKE---DAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 675 FSTLEVENLFVILSAILHIGDIQFTAlTEADS---AFVSDLQLLEQVAGMLQVSTDELASALT---TDIQYfkgDVIIRR 748
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSS-SERESqevAAVSSWAEIHTAARLLQVPPERLEGAVThrvTETPY---GRVSRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 749 HTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQ 828
Cdd:cd14896 308 LPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAT--IGVVDAYGFEALRVNGLEQLCINLASERLQLFSS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 829 EVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLprkLQGLLESSNTNAVYS--- 905
Cdd:cd14896 386 QTLLAQEEEECQRELLPWVPIPQPPRES-CLDLLVDQPHSLLSILDDQTWLSQATDHTF---LQKCHYHHGDHPSYAkpq 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 906 ---PVkdgngnvafkgqgaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGslissyp 982
Cdd:cd14896 462 lplPV---------------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYG------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 983 sfkfgghkstllskrtassmvgvnknylelskllkkkgtstflqrLERGEPaTAASQLTKSLADITAKLQRGSPHFILCI 1062
Cdd:cd14896 520 ---------------------------------------------LGQGKP-TLASRFQQSLGDLTARLGRSHVYFIHCL 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1063 KPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASvllGETKGQAAEERCRLVLQrcKLQG 1142
Cdd:cd14896 554 NPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS---ERQEALSDRERCGAILS--QVLG 628
|
730
....*....|....*.
gi 568953283 1143 -----WQIGVHKVFLK 1153
Cdd:cd14896 629 aesplYHLGATKVLLK 644
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
437-1153 |
4.44e-107 |
|
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: 358.24 E-value: 4.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSPTGQRSPslppHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISKSP----HVFSTASSAYQGMCNNKKSQTIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFD---SRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQ--CCQRRKH-- 588
Cdd:cd14888 78 ISGESGAGKTESTKYVMKFLACAGSEDIKKRSlveAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQfsKLKSKRMsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 589 ----ITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHL--NNFCAHR-YVSQGMREDVS--------- 652
Cdd:cd14888 158 drgrLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYeeNDEKLAKgADAKPISIDMSsfephlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 653 ----TAEHSLNK----ERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQF-TALTEADSAFVSDLQL--LEQVAGM 721
Cdd:cd14888 238 yltkSSCHELPDvddlEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFeNNEACSEGAVVSASCTddLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 722 LQVSTDELASALTTDiqyfkgdVIIRRH-------TIQMAAFYRDLLAKSLYSRLFGFLINTVNcclQNQDEYKSLQTLD 794
Cdd:cd14888 318 LGVDAEDLLNALCYR-------TIKTAHefytkplRVDEAEDVRDALARALYSCLFDKVVERTN---ESIGYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 795 IGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVlDFFFQKPSGFFSLLD 874
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCV-DLLQEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 875 EESQVIWSGEPNLPRKlqgLLESSNTNAVYSPVK-DGNgnvafkgqgaAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLF 953
Cdd:cd14888 467 EECFVPGGKDQGLCNK---LCQKHKGHKRFDVVKtDPN----------SFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 954 VMKTSENVVISHLFQSKLSQtgslissypsfkfGGHKSTLLSKRtassmvgvnknylelskllkkkgtstflqrlergep 1033
Cdd:cd14888 534 VIKNSKNPFISNLFSAYLRR-------------GTDGNTKKKKF------------------------------------ 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1034 ATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEP 1113
Cdd:cd14888 565 VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRI 644
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 568953283 1114 LASvllGETKGQaaeercrlvlqrckLQGWQIGVHKVFLK 1153
Cdd:cd14888 645 LLN---GEGKKQ--------------LSIWAVGKTLCFFK 667
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
436-1153 |
3.31e-105 |
|
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: 352.54 E-value: 3.31e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTmvSQMyLSPTGQRSPSLPPHLFSCAERAFHRLFQERKP--- 511
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSE--ERM-LLYHGTTAGELPPHVFAIADHAYTQLIQSGVLdps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 512 -QNIILSGERGSGKTQASKQIMKYLTsRASS-------------------SCTMFDSRLRHAIYIVEAFGHAKTTLNNVS 571
Cdd:cd14890 78 nQSIIISGESGAGKTEATKIIMQYLA-RITSgfaqgasgegeaaseaieqTLGSLEDRVLSSNPLLESFGNAKTLRNDNS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 572 SCLIQYWELQCcQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYvsqgMREDV 651
Cdd:cd14890 157 SRFGKFIEIQF-DHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFY----LRGEC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 652 STAEHSLNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEAD-SAFVSDLQLLEQVAGMLQVSTDELA 730
Cdd:cd14890 232 SSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvLEDATTLQSLKLAAELLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 731 SALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNqdeyKSLQTLDIGILDIFGFEEFQKNE 810
Cdd:cd14890 312 KALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISS----PDDKWGFIGVLDIYGFEKFEWNT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 811 FEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPS---GFFSLLDEesqvIWSGEPNL 887
Cdd:cd14890 388 FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQA-CLELIEGKVNgkpGIFITLDD----CWRFKGEE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 888 P-RKLQGLLESSntnavYSPVKDGNGNVAFKGQGA-----------AFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVM 955
Cdd:cd14890 463 AnKKFVSQLHAS-----FGRKSGSGGTRRGSSQHPhfvhpkfdadkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 956 KTSEnvvishlfqsklsqtgslissypsfkfgghkstllskrtaSSMVGVnknylelskllkkkgtstflqrlergepaT 1035
Cdd:cd14890 538 KQSR----------------------------------------RSIREV-----------------------------S 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1036 AASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA 1115
Cdd:cd14890 549 VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLL 628
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 568953283 1116 SvllgetkgqAAEERCRLVLQRCKLQG-----WQIGVHKVFLK 1153
Cdd:cd14890 629 P---------TAENIEQLVAVLSKMLGlgkadWQIGSSKIFLK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
438-1153 |
5.48e-100 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 337.50 E-value: 5.48e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 438 LLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSPTGQRSPSlPPHLFSCAERAFHRLFQERK----PQ 512
Cdd:cd14892 3 LLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKEEATASSP-PPHVFSIAERAYRAMKGVGKgqgtPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 513 NIILSGERGSGKTQASKQIMKYLT----SRASSSCTMFDSRLRHAI--------YIVEAFGHAKTTLNNVSSCLIQYWEL 580
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIeecvllsnLILEAFGNAKTIRNDNSSRFGKYIQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 581 QCcQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEhslNK 660
Cdd:cd14892 162 HY-NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVD---DA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 661 ERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVS--DLQLLEQVAGMLQVSTDELASALTTD-I 737
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQsaDGVNVAKAAGLLGVDAAELMFKLVTQtT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 738 QYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTLD------IGILDIFGFEEFQKNEF 811
Cdd:cd14892 318 STARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGVTGGAASptfspfIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 812 EQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEesQVIWSGEP---NLP 888
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQD-CLDLIQKKPLGLLPLLEE--QMLLKRKTtdkQLL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 889 RKLQGllESSNTNAVYSPVKDgngnvafkgQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSEnvvishlfq 968
Cdd:cd14892 475 TIYHQ--THLDKHPHYAKPRF---------ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS--------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 969 sklsqtgslissypsfKFgghkstllskRTassmvgvnknylelskllkkkgtstflqrlergepataasqltkSLADIT 1048
Cdd:cd14892 535 ----------------KF----------RT--------------------------------------------QLAELM 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1049 AKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQ--- 1125
Cdd:cd14892 545 EVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNKAGVAASPdac 624
|
730 740 750
....*....|....*....|....*....|..
gi 568953283 1126 ----AAEERCRLVLQRCKLQGWQIGVHKVFLK 1153
Cdd:cd14892 625 dattARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
437-1153 |
3.86e-99 |
|
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: 336.54 E-value: 3.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-------IYSTMVSQMylsptgqrspSLPPHLFSCAE---RAFHRLF 506
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPglydlhkYREEMPGWT----------ALPPHVFSIAEgayRSLRRRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 507 QE----RKPQNIILSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIY---------IVEAFGHAKTTLNNVSSC 573
Cdd:cd14895 72 HEpgasKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISgsellsanpILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 574 LIQY----WELQCCQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAH--RYVSQG- 646
Cdd:cd14895 152 FGKFvrmfFEGHELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQefQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 647 --MREDVSTAEHSLNKerlaaLKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEAD---------------SAFV 709
Cdd:cd14895 232 cyQRNDGVRDDKQFQL-----VLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 710 SDL---QLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDE 786
Cdd:cd14895 307 SSLtvqQHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 787 YKSLQTLD-------IGILDIFGFEEFQKNEFEQLCVNLTNEKM-HHYIQEVLfLQEQTECVQEGVAMETACSPGNqAGV 858
Cdd:cd14895 387 ALNPNKAAnkdttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLqYQFIQDIL-LTEQQAHIEEGIKWNAVDYEDN-SVC 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 859 LDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKL-QGLLESSNTNAVYSPVKDgngnvafkgqgAAFTVMHYAGRVMYEMG 937
Cdd:cd14895 465 LEMLEQRPSGIFSLLDEECVVPKGSDAGFARKLyQRLQEHSNFSASRTDQAD-----------VAFQIHHYAGAVRYQAE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 938 GAVERNKDSLSQNLLFVMKTSENVVISHLFQS-KLSQTGSLISSYPSfkfgghkstLLSKRTASSMVGVnknylelskll 1016
Cdd:cd14895 534 GFCEKNKDQPNAELFSVLGKTSDAHLRELFEFfKASESAELSLGQPK---------LRRRSSVLSSVGI----------- 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1017 kkkgtstflqrlergepataASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRS 1096
Cdd:cd14895 594 --------------------GSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQ 653
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 568953283 1097 GYPVRPSFEDFLSRYEPLAsvllgeTKGQAAEERCRLVLQRCKLQGWQIGVHKVFLK 1153
Cdd:cd14895 654 SYPVRMKHADFVKQYRLLV------AAKNASDATASALIETLKVDHAELGKTRVFLR 704
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
437-1152 |
3.65e-98 |
|
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: 332.14 E-value: 3.65e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQRS---PSLPPHLFSCAERAFHR-LFQERKP- 511
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGERRAageRKLPPHVYAVADKAFRAmLFASRGQk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 512 --QNIILSGERGSGKTQASKQIMKYLTSrASSSCTMFDS---------RLRHAIYIVEAFGHAKTTLNNVSSCLIQYWEL 580
Cdd:cd14901 82 cdQSILVSGESGAGKTETTKIIMNYLAS-VSSATTHGQNaterenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 581 QCcQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGmrEDVSTAEHSLNK 660
Cdd:cd14901 161 GF-ASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSS--QCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 661 ERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAF-VSDLQLLEQVAGMLQVSTDELASALTTDIQY 739
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFsMSSLANVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 740 FKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTldIGILDIFGFEEFQKNEFEQLCVNLT 819
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASRF--IGIVDIFGFEIFATNSLEQLCINFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 820 NEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLeSSN 899
Cdd:cd14901 396 NEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDA-CVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLL-AKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 900 TNAVYSPVKDGngnvafKGQgaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENvvishlfqsklsqtgSLIS 979
Cdd:cd14901 474 ASFSVSKLQQG------KRQ---FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSN---------------AFLS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 980 SYPSFKFGGHKSTLLSKRTASsmvgvnknylelskllkkkgtstflqrlergepataasqltksladitaklqrgSPHFI 1059
Cdd:cd14901 530 STVVAKFKVQLSSLLEVLNAT------------------------------------------------------EPHFI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1060 LCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVlLGETKGQAAEERCRL------ 1133
Cdd:cd14901 556 RCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPD-GASDTWKVNELAERLmsqlqh 634
|
730 740
....*....|....*....|
gi 568953283 1134 -VLQRCKLQGWQIGVHKVFL 1152
Cdd:cd14901 635 sELNIEHLPPFQVGKTKVFL 654
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
436-1153 |
3.18e-96 |
|
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: 326.35 E-value: 3.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSptgQRSPSLPPHLFSCAERAFHRLFQERKPQNI 514
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLN---KPKEELPPHVYATSVAAYNHMKRSGRNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 515 ILSGERGSGKTQASKQIMKYLTSRASSsctMFDSRLRHAIYI---VEAFGHAKTTLNNVSSCLIQYWELQCcQRRKHITG 591
Cdd:cd14903 78 LVSGESGAGKTETTKILMNHLATIAGG---LNDSTIKKIIEVnplLESFGNAKTVRNDNSSRFGKFTQLQF-DKNGTLVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 592 ARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAH-RYVSQGMREDVSTAEHslnkerLAALKHAL 670
Cdd:cd14903 154 AKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYtGANKTIKIEGMSDRKH------FARTKEAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 671 NVIGFSTLEVENLFVILSAILHIGDIQFTALT--EADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRR 748
Cdd:cd14903 228 SLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPndDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 749 HTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNqdeyKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQ 828
Cdd:cd14903 308 LKKDQAEDCRDALAKAIYSNVFDWLVATINASLGN----DAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 829 EVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKpSGFFSLLDEESQVIWSGEPNLPRKLQGLLessntnavyspvK 908
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDFADNQD-VLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIH------------K 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 909 DGNGNVAF-KGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSLISSypsfkfg 987
Cdd:cd14903 450 DEQDVIEFpRTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTS------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 988 ghkstllSKRTASSMVGvnknylelskllkkkGTSTFlqrlergepATAASQLTKSLADITAKLQRGSPHFILCIKPNTS 1067
Cdd:cd14903 523 -------LARGARRRRG---------------GALTT---------TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSI 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1068 QLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLasVLLGETKGQAAEERCRLVLQRCKLQG---WQ 1144
Cdd:cd14903 572 KSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF--LPEGRNTDVPVAERCEALMKKLKLESpeqYQ 649
|
....*....
gi 568953283 1145 IGVHKVFLK 1153
Cdd:cd14903 650 MGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
437-1112 |
1.55e-95 |
|
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: 324.20 E-value: 1.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSY---QGKSLGTLPPHVFAIADKAYRDMKVLKQSQSII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQcCQRRKHITGARIS 595
Cdd:cd01382 79 VSGESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH-FNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 596 TYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLhlnnfcahryVSQGMREDVstaehslnkERLAALKHALNVIGF 675
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------LKDPLLDDV---------GDFIRMDKAMKKIGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 676 STLEVENLFVILSAILHIGDIQFtalTEADSAFVSDLQL-------LEQVAGMLQVSTDELASALTTDIQY-----FKGD 743
Cdd:cd01382 219 SDEEKLDIFRVVAAVLHLGNIEF---EENGSDSGGGCNVkpkseqsLEYAAELLGLDQDELRVSLTTRVMQttrggAKGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 744 VIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCL--QNQDEYkslqtldIGILDIFGFEEFQKNEFEQLCVNLTNE 821
Cdd:cd01382 296 VIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETSSYF-------IGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 822 KMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQaGVLDFFFQKPSGFFSLLDEESQviwsgepnLPRKlqglLESSNTN 901
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQ-DCIDLIEAKLVGILDLLDEESK--------LPKP----SDQHFTS 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 902 AVYSPVKD-GNGNVAFKGQGAA---------FTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKL 971
Cdd:cd01382 436 AVHQKHKNhFRLSIPRKSKLKIhrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESST 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 972 SQTGSLISSypsfkfgGHKSTLLSkrtassmVGvnknylelskllkkkgtSTFlqrlergepataASQLTKSLaditAKL 1051
Cdd:cd01382 516 NNNKDSKQK-------AGKLSFIS-------VG-----------------NKF------------KTQLNLLM----DKL 548
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953283 1052 QRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYE 1112
Cdd:cd01382 549 RSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYK 609
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
437-1112 |
5.34e-90 |
|
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: 309.99 E-value: 5.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSPTGQRSPslPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNKSP--IPHIYAVALRAYQSMVSEKKNQSII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTM----------FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQR 585
Cdd:cd14906 80 ISGESGSGKTEASKTILQYLINTSSSNQQQnnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 586 RKHITGARISTYMLEKSRVVAQPPGQG-TFLIFSWLMDGLSSEEKCGLHL-NNFCAHRYVSQgmREDV--STAEHSLNK- 660
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDA--RDDVisSFKSQSSNKn 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 661 ----------ERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFtaltEADSAFV-------SDLQLLEQVAGMLQ 723
Cdd:cd14906 238 snhnnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEF----EEDSDFSkyayqkdKVTASLESVSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 724 VSTDELASALTTdiQYFK----GDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQ-------T 792
Cdd:cd14906 314 YIESVFKQALLN--RNLKaggrGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAggsnkknN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 793 LDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSL 872
Cdd:cd14906 392 LFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKE-CIELIEKKSDGILSL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 873 LDEESQVIWSGEPNLPRKLQGllESSNTNAVYSpvkdgngNVAFKGqgaAFTVMHYAGRVMYEMGGAVERNKDSLSQNLL 952
Cdd:cd14906 471 LDDECIMPKGSEQSLLEKYNK--QYHNTNQYYQ-------RTLAKG---TLGIKHFAGDVTYQTDGWLEKNRDSLYSDVE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 953 FVMKTSENVVISHLFQSKLSQTgslissypsfkfgghkSTLLSKRTASSmvgvnknylelskllkkkgtstflqrlerge 1032
Cdd:cd14906 539 DLLLASSNFLKKSLFQQQITST----------------TNTTKKQTQSN------------------------------- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1033 paTAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYE 1112
Cdd:cd14906 572 --TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYK 649
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
438-1115 |
7.07e-90 |
|
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: 307.36 E-value: 7.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 438 LLYEIQKRFGNDQIH--TFIGDIFLLVNPFKELPiySTMVSQMYLSPTGQRspslPPHLFSCAERAFH--RLFQERK-PQ 512
Cdd:cd14891 3 ILHNLEERSKLDNQRpyTFMANVLIAVNPLRRLP--EPDKSDYINTPLDPC----PPHPYAIAEMAYQqmCLGSGRMqNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 513 NIILSGERGSGKTQASKQIMKYLTSRA------------------SSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCL 574
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkrKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 575 IQYWELQCCQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGmreDVSTA 654
Cdd:cd14891 157 GKFMKLQFTKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQS---GCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 655 EHSLNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQF----TALTEADSAFVSDLQLLEQVAGMLQVSTDELA 730
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 731 SALTT-DIQYFKGDVIIRRhTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqdEYKSLQTLDIGILDIFGFEEFQ-K 808
Cdd:cd14891 314 KVITQrEIVTRGETFTIKR-NAREAVYSRDAIAKSIYERLFLWIVQQINTSL----GHDPDPLPYIGVLDIFGFESFEtK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 809 NEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQviwsgEPNlP 888
Cdd:cd14891 389 NDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRE-CLDLIASKPNGILPLLDNEAR-----NPN-P 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 889 --RKLQGLLESSNTNAVYSPV---KDGNGNvafkgqgaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLlfvmktSENVVI 963
Cdd:cd14891 462 sdAKLNETLHKTHKRHPCFPRphpKDMREM---------FIVKHYAGTVSYTIGSFIDKNNDIIPEDF------EDLLAS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 964 SHLFqskLSQTGSLIssypsfkfgghkSTLLSKRTassmvgvnknylelskllkkkgtstflqrlergepataasqltks 1043
Cdd:cd14891 527 SAKF---SDQMQELV------------DTLEATRC--------------------------------------------- 546
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953283 1044 laditaklqrgspHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA 1115
Cdd:cd14891 547 -------------NFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVL 605
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
437-1111 |
1.28e-89 |
|
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: 307.25 E-value: 1.28e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSptgQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLK---KPRDKLQPHVYATSTAAYKHMLTNEMNQSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSsctMFDSRLRHAIYI---VEAFGHAKTTLNNVSSCLIQYWELQCCQRRKHItGA 592
Cdd:cd14904 79 VSGESGAGKTETTKIVMNHLASVAGG---RKDKTIAKVIDVnplLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI-GA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 593 RISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVsqGMREDVSTAEHSLNKERLAALKHALNV 672
Cdd:cd14904 155 KCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYL--GDSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 673 IGFSTLEVENLFVILSAILHIGDIQFTALTEADSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQ 752
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSR-ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 753 MAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLF 832
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ---IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 833 LQEQTECVQEGVAMETACSPGNQaGVLDFFFQKpSGFFSLLDEESQVIWSGEPNLPRKLQGLLESsntnavyspvKDGNG 912
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEYQDNQ-GIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQT----------KKDNE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 913 NVAF-KGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSklsqtgsliSSYPSFKFGGhks 991
Cdd:cd14904 457 SIDFpKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---------SEAPSETKEG--- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 992 tlLSKRTASSmvgvnknylelskllkkkgtstflqrlergePATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPG 1071
Cdd:cd14904 525 --KSGKGTKA-------------------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPT 571
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 568953283 1072 VFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRY 1111
Cdd:cd14904 572 EFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
437-1111 |
1.41e-89 |
|
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: 308.74 E-value: 1.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMY------LSPTGQRSpSLPPHLFSCAERAFHRLFQ-E 508
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtsTSPVSQLS-ELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 509 RKPQNIILSGERGSGKTQASKQIMKYLTS---------RASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWE 579
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSvgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 580 LQCCQRRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDG----------LSSEEKCGLHLNNFCAHRyvsqgMRE 649
Cdd:cd14902 161 IQFGANNE-IVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGadktlldllgLQKGGKYELLNSYGPSFA-----RKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 650 DVSTAEHSLNKERLAALKHalnvIGFSTLEVENLFVILSAILHIGDIQFTAL-TEADSAFVSDLQL--LEQVAGMLQVST 726
Cdd:cd14902 235 AVADKYAQLYVETVRAFED----TGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRfhLAKCAELMGVDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 727 DELASALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFL-------INTVNCCLQNQDEYKSLQTldIGILD 799
Cdd:cd14902 311 DKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLvrrlsdeINYFDSAVSISDEDEELAT--IGILD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 800 IFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNqAGVLDFFFQKPSGFFSLLDEESQv 879
Cdd:cd14902 389 IFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSN-AACLALFDDKSNGLFSLLDQECL- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 880 iwsgepnLPRklqGLLESSNTNAVYSPVKDGNgnvafkgqgaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSE 959
Cdd:cd14902 467 -------MPK---GSNQALSTKFYRYHGGLGQ-----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSS 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 960 NVVISHLFQSKlsQTGSLIssypsfkfgghKSTLLSKRTASSMVGVnknylelskllkkkgtstflqrlergepATAASQ 1039
Cdd:cd14902 526 NEVVVAIGADE--NRDSPG-----------ADNGAAGRRRYSMLRA----------------------------PSVSAQ 564
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953283 1040 LTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRY 1111
Cdd:cd14902 565 FKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
436-1153 |
3.30e-88 |
|
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: 303.47 E-value: 3.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY---RGKKRHEMPPHIYAISESAYRCMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSctmfDSRLRHAIY------------IVEAFGHAKTTLNNVSSCLIQYWELQCc 583
Cdd:cd14920 78 CTGESGAGKTENTKKVIQYLAHVASSH----KGRKDHNIPgelerqllqanpILESFGNAKTVKNDNSSRFGKFIRINF- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 584 QRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGmreDVSTAEHSlNKERL 663
Cdd:cd14920 153 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG---YIPIPGQQ-DKDNF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 664 AALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd14920 229 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 744 VIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKM 823
Cdd:cd14920 309 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 824 HHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQ--KPSGFFSLLDEESqviWSGEPNLPRKLQGLLESSNTN 901
Cdd:cd14920 386 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERpaNPPGVLALLDEEC---WFPKATDKTFVEKLVQEQGSH 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 902 AVYSPVKDGNGNvafkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTG-SLISS 980
Cdd:cd14920 463 SKFQKPRQLKDK-------ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGlDQVTG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 981 YPSFKFGghkSTLLSKRTASSMVGvnknylelskllkkkgtstflqrlergepataasQLTK-SLADITAKLQRGSPHFI 1059
Cdd:cd14920 536 MTETAFG---SAYKTKKGMFRTVG----------------------------------QLYKeSLTKLMATLRNTNPNFV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1060 LCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA--SVLLGETKGQAAeerCRLVLQR 1137
Cdd:cd14920 579 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpnAIPKGFMDGKQA---CERMIRA 655
|
730
....*....|....*...
gi 568953283 1138 CKLQG--WQIGVHKVFLK 1153
Cdd:cd14920 656 LELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
436-1153 |
5.89e-88 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 302.66 E-value: 5.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSS-----CTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRRKhIT 590
Cdd:cd14929 78 FTGESGAGKTVNTKHIIQYFATIAAMIeskkkLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM-LS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 591 GARISTYMLEKSRVVAQPPGQGTFLIFSWLMDG--------LSSEEKCGLHlnnFCAHRYVsqgmredvsTAEHSLNKER 662
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILSGkkelrdllLVSANPSDFH---FCSCGAV---------AVESLDDAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 663 LAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 742
Cdd:cd14929 225 LLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 743 DVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqdEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEK 822
Cdd:cd14929 305 EYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVL----DAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 823 MHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFfQKPSGFFSLLDEESQVIWSGEPNLPRKLqglLESSNTNA 902
Cdd:cd14929 381 LQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKL---FDNHFGKS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 903 VY--SPVKDGngnvafKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSqTGSLIss 980
Cdd:cd14929 457 VHfqKPKPDK------KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIS-TDSAI-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 981 ypsfKFGGHKStllSKRTASSMVgvnknylelskllkkkgtstflqrlergepataASQLTKSLADITAKLQRGSPHFIL 1060
Cdd:cd14929 528 ----QFGEKKR---KKGASFQTV---------------------------------ASLHKENLNKLMTNLKSTAPHFVR 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1061 CIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQAAEERCRLVLQRCKL 1140
Cdd:cd14929 568 CINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEI 647
|
730
....*....|....*
gi 568953283 1141 QG--WQIGVHKVFLK 1153
Cdd:cd14929 648 DHtqYRFGITKVFFK 662
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
433-1156 |
5.11e-87 |
|
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: 299.08 E-value: 5.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 433 LNDSSLLYEIQKRFGNDQIHTFIGD-IFLLVNPFKELPIYSTMVSQMYLS----PTGQRSPSLPPHLFSCAERAFHRLFQ 507
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYGSeyydTTSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 508 ERKPQNIILSGERGSGKTQASKQIMKYLTSRASSSC--TMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQR 585
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkgTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 586 RKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYV--SQGMREdvSTAEHSLNKERL 663
Cdd:cd14879 161 GR-LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPL--PLGPGSDDAEGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 664 AALKHALNVIGFSTLEVENLFVILSAILHIGDIQFT--ALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 741
Cdd:cd14879 238 QELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 742 GDVIirrhTI----QMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQtldIGILDIFGFEEF---QKNEFEQL 814
Cdd:cd14879 318 KELC----TVfldpEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATF---ISLLDFPGFQNRsstGGNSLDQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 815 CVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESqviwsgepnlpRKLQG- 893
Cdd:cd14879 391 CVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSD-CVRLLRGKPGGLLGILDDQT-----------RRMPKk 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 894 ----LLES-SNTNAVYSPVKDGnGNVAFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLfvmktsenvvishlfq 968
Cdd:cd14879 459 tdeqMLEAlRKRFGNHSSFIAV-GNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 969 sklsqtgslissypsfkfgghksTLLskrtassmvgvnknylelskllkkkgtstflqrleRGepataASQLTKSLADIT 1048
Cdd:cd14879 522 -----------------------NLL-----------------------------------RG-----ATQLNAALSELL 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1049 AKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQAAE 1128
Cdd:cd14879 539 DTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAERIRQCAR 618
|
730 740 750
....*....|....*....|....*....|
gi 568953283 1129 ErcrlvLQRCKLQGWQIGVHKVFLKY--WH 1156
Cdd:cd14879 619 A-----NGWWEGRDYVLGNTKVFLSYaaWR 643
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
382-1206 |
1.10e-86 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 303.10 E-value: 1.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 382 DIMF--------KDTTKGLCKQ------ESQDGPPETSMTSNcgkpEQVQVMPpapSDDLATLSELNDSSLLYEIQKRFG 447
Cdd:PTZ00014 49 DLMFakclvlpgSTGEKLTLKQidpptnSTFEVKPEHAFNAN----SQIDPMT---YGDIGLLPHTNIPCVLDFLKHRYL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 448 NDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTgqRSPSLPPHLFSCAERAFHRLFQERKPQNIILSGERGSGKTQA 527
Cdd:PTZ00014 122 KNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAK--DSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 528 SKQIMKYLTSraSSSCTMfDSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWELQcCQRRKHITGARISTYMLEKSR 603
Cdd:PTZ00014 200 TKQIMRYFAS--SKSGNM-DLKIQNAIMaanpVLEAFGNAKTIRNNNSSRFGRFMQLQ-LGEEGGIRYGSIVAFLLEKSR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 604 VVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMRE-----DVSTAEHSLNkerlaalkhALNVIGFSTL 678
Cdd:PTZ00014 276 VVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDvpgidDVKDFEEVME---------SFDSMGLSES 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 679 EVENLFVILSAILHIGDIQFTALTEA---DSAFVSD--LQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQM 753
Cdd:PTZ00014 347 QIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDesLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 754 AAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMH-HYIQeVLF 832
Cdd:PTZ00014 427 SEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVF----IGMLDIFGFEVFKNNSLEQLFINITNEMLQkNFVD-IVF 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 833 LQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLdeESQVIWSGepnlpRKLQGLLESSNT----NAVYSPVK 908
Cdd:PTZ00014 502 ERESKLYKDEGISTEELEYTSNES-VIDLLCGKGKSVLSIL--EDQCLAPG-----GTDEKFVSSCNTnlknNPKYKPAK 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 909 -DGNGNvafkgqgaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQ------SKLSQtGSLIssy 981
Cdd:PTZ00014 574 vDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEgvevekGKLAK-GQLI--- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 982 psfkfgghkstllskrtassmvgvnknylelskllkkkgtstflqrlergepataASQLTKSLADITAKLQRGSPHFILC 1061
Cdd:PTZ00014 641 -------------------------------------------------------GSQFLNQLDSLMSLINSTEPHFIRC 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1062 IKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLaSVLLGETKGQAAEERCRLVLQRCKL- 1140
Cdd:PTZ00014 666 IKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL-DLAVSNDSSLDPKEKAEKLLERSGLp 744
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953283 1141 -QGWQIGVHKVFLKYWHVDQLSdlwlQLQRKIVTCQKVIRGFLARQHLLQRmsiKQQEVTSIKSFLQ 1206
Cdd:PTZ00014 745 kDSYAIGKTMVFLKKDAAKELT----QIQREKLAAWEPLVSVLEALILKIK---KKRKVRKNIKSLV 804
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
437-1153 |
2.18e-84 |
|
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: 292.58 E-value: 2.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMY-----LSPTGQRSP-SLPPHLFSCAERAFHRLFQE-R 509
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqeglLRSQGIESPqALGPHVFAIADRSYRQMMSEiR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 510 KPQNIILSGERGSGKTQASKQIMKYLTSRASSSCTMFDS-----------RLRHAIYIVEAFGHAKTTLNNVSSCLIQYW 578
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimdRVLQSNPILEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 579 ELQCcQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEK----------CGLHLNNFcaHRYVSQGMR 648
Cdd:cd14908 162 ELGF-NRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHekyefhdgitGGLQLPNE--FHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 649 EDVSTAEhslNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTE---ADSAFVSDLQLLEQVAGMLQVS 725
Cdd:cd14908 239 PDLREFT---DEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEdgaAEIAEEGNEKCLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 726 TDELASALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCL--QNQDEYKSlqtlDIGILDIFGF 803
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRS----SVGVLDIFGF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 804 EEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQaGVLDFFFQKPSGFFSLLDEESQVIWSG 883
Cdd:cd14908 392 ECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQ-DCLDTIQAKKKGILTMLDDECRLGIRG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 884 ----------EPNLPRKLQGLLESSNTNAvyspvkdgngNVAFKGQGaAFTVMHYAGRVMYEM-GGAVERNKDSLSqnll 952
Cdd:cd14908 471 sdanyasrlyETYLPEKNQTHSENTRFEA----------TSIQKTKL-IFAVRHFAGQVQYTVeTTFCEKNKDEIP---- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 953 fvmKTSENvvishLFQSklsqtgslissypsfkfgghkstllskrtassmvgvnknylelskllkkkgtstflqrlerge 1032
Cdd:cd14908 536 ---LTADS-----LFES--------------------------------------------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1033 pataASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYE 1112
Cdd:cd14908 545 ----GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYR 620
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953283 1113 PLASV---------LLGETKGQA-AEERCRLVLQRCKLQGW-----------QIGVHKVFLK 1153
Cdd:cd14908 621 MLLPLipevvlswsMERLDPQKLcVKKMCKDLVKGVLSPAMvsmknipedtmQLGKSKVFMR 682
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
436-1153 |
4.55e-84 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 291.50 E-value: 4.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASS---------------SCTM--FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYW 578
Cdd:cd14911 78 CTGESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpAVLIgeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 579 ELQCcQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREdVSTAEHSl 658
Cdd:cd14911 158 RINF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLP-VPGVDDY- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 659 nKERLAALKhALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQ 738
Cdd:cd14911 235 -AEFQATVK-SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 739 YFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNL 818
Cdd:cd14911 313 KVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL---DRTKRQGASFIGILDMAGFEIFELNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 819 TNEKMHHYIQEVLFLQEQTECVQEGVAMEtacspgnqagVLDF---------FFQKPSGFFSLLDEESQVIWSGEPNLPR 889
Cdd:cd14911 390 TNEKLQQLFNHTMFILEQEEYQREGIEWK----------FIDFgldlqptidLIDKPGGIMALLDEECWFPKATDKTFVD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 890 KLqgllesSNTNAVYSPVKDGNgnvaFKGQgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQS 969
Cdd:cd14911 460 KL------VSAHSMHPKFMKTD----FRGV-ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 970 klsqtgslissypsfkfgghkstllskrtaSSMVGVNKnylelskllKKKGTSTFLQRLERGEPATAASQLTKSLADITA 1049
Cdd:cd14911 529 ------------------------------AEIVGMAQ---------QALTDTQFGARTRKGMFRTVSHLYKEQLAKLMD 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1050 KLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLL--GETKGQAA 1127
Cdd:cd14911 570 TLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIpkGFMDGKKA 649
|
730 740
....*....|....*....|....*...
gi 568953283 1128 eerCRLVLQRCKLQG--WQIGVHKVFLK 1153
Cdd:cd14911 650 ---CEKMIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
445-1153 |
5.80e-84 |
|
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: 290.35 E-value: 5.80e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 445 RFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIILSGERGSGK 524
Cdd:cd14876 10 RYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYR--DAPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 525 TQASKQIMKYLtsrASSSCTMFDSRLRHAIY----IVEAFGHAKTTLNNVSSCLIQYWELQcCQRRKHITGARISTYMLE 600
Cdd:cd14876 88 TEATKQIMRYF---ASAKSGNMDLRIQTAIMaanpVLEAFGNAKTIRNNNSSRFGRFMQLD-VASEGGIRYGSVVAFLLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 601 KSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYV------SQGMrEDVSTAEhslnkERLAALKHalnvIG 674
Cdd:cd14876 164 KSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLnpkcldVPGI-DDVADFE-----EVLESLKS----MG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 675 FSTLEVENLFVILSAILHIGDIQFTALTEA---DSAFVS--DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRH 749
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKITGKTEQgvdDAAAISneSLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 750 TIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQE 829
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNF----MGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 830 VLFLQEQTECVQEGVAMETACSPGNqAGVLDFFFQKPSGFFSLLdeESQVIWSGEPNLprKLQGLLESS-NTNAVYSPVK 908
Cdd:cd14876 390 IVFERESKLYKDEGIPTAELEYTSN-AEVIDVLCGKGKSVLSIL--EDQCLAPGGSDE--KFVSACVSKlKSNGKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 909 -DGNGNvafkgqgaaFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGslissypsfKFG 987
Cdd:cd14876 465 vDSNIN---------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG---------KIA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 988 ghKSTLLSkrtassmvgvnknylelskllkkkgtSTFLqrlergepataaSQLTkSLADITAKLQrgsPHFILCIKPNTS 1067
Cdd:cd14876 527 --KGSLIG--------------------------SQFL------------KQLE-SLMGLINSTE---PHFIRCIKPNET 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1068 QLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLaSVLLGETKGQAAEERCRLVLQRCKL--QGWQI 1145
Cdd:cd14876 563 KKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL-DLGIANDKSLDPKVAALKLLESSGLseDEYAI 641
|
....*...
gi 568953283 1146 GVHKVFLK 1153
Cdd:cd14876 642 GKTMVFLK 649
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
436-1153 |
1.00e-83 |
|
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: 290.39 E-value: 1.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDS------------RLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCc 583
Cdd:cd14932 78 CTGESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 584 QRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMredvSTAEHSLNKERL 663
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN----VTIPGQQDKELF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 664 AALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd14932 233 AETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 744 VIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKM 823
Cdd:cd14932 313 YVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 824 HHYIQEVLFLQEQTECVQEGVametacspgnQAGVLDF---------FFQKPS---GFFSLLDEESqviWSGEPNLPRKL 891
Cdd:cd14932 390 QQLFNHTMFILEQEEYQREGI----------EWSFIDFgldlqpcieLIEKPNgppGILALLDEEC---WFPKATDKSFV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 892 QGLLESSNTNAVYSPVKDGNGNvafkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFqskl 971
Cdd:cd14932 457 EKVVQEQGNNPKFQKPKKLKDD-------ADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELW---- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 972 sqtgslissypsfkfgghkstllskRTASSMVGVNKnylelskllkKKGTSTFLQ---RLERGEPATAASQLTKSLADIT 1048
Cdd:cd14932 526 -------------------------KDVDRIVGLDK----------VAGMGESLHgafKTRKGMFRTVGQLYKEQLMNLM 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1049 AKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA--SVLLGETKGQA 1126
Cdd:cd14932 571 TTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpnAIPKGFMDGKQ 650
|
730 740
....*....|....*....|....*....
gi 568953283 1127 AeerCRLVLQRCKLQG--WQIGVHKVFLK 1153
Cdd:cd14932 651 A---CVLMVKALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
436-1153 |
2.42e-83 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 288.85 E-value: 2.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMY---KGKKRTEMPPHLFSISDNAYHDMLMDRENQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDSR------LRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRRKhI 589
Cdd:cd14934 78 ITGESGAGKTENTKKVIQYFANIGGTGKQSSDGKgsledqIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK-L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 590 TGARISTYMLEKSRVVAQPPGQGTFLIFSWLMdglsSEEKCGLHLNNFCA-----HRYVSQGmredVSTAEHSLNKERLA 664
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQIL----SNKKPELIESLLLVpnpkeYHWVSQG----VTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 665 ALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDV 744
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 745 IIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqdEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMH 824
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTL----DTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 825 HYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDfFFQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNtna 902
Cdd:cd14934 385 QFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACID-LLEKPMGIFSILEEQCVFPKATDATFKAALydNHLGKSSN--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 903 vYSPVKDGNGnvafKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSlissyp 982
Cdd:cd14934 461 -FLKPKGGKG----KGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 983 sfkfgghkstlLSKRTASSMVGVNKNYLelskllkkkgtstflqrlergepataaSQLTKsladITAKLQRGSPHFILCI 1062
Cdd:cd14934 530 -----------KKQKRGSSFMTVSNFYR---------------------------EQLNK----LMTTLHSTAPHFVRCI 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1063 KPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLL--GETKGQAAEErcrLVLQRCKL 1140
Cdd:cd14934 568 VPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIpqGFVDNKKASE---LLLGSIDL 644
|
730
....*....|....*
gi 568953283 1141 Q--GWQIGVHKVFLK 1153
Cdd:cd14934 645 DvnEYKIGHTKVFFR 659
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
436-1153 |
7.73e-83 |
|
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: 287.68 E-value: 7.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDS--------RLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcQRRK 587
Cdd:cd14921 78 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 588 HITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEHSLNKERLaalk 667
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 668 HALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIR 747
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 748 RHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYI 827
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 828 QEVLFLQEQTECVQEGV-------------AMETACSPGNqagvldfffqkPSGFFSLLDEESQVIWSGEPNLPRKLqgL 894
Cdd:cd14921 390 NHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKL--C 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 895 LESSNTNAVYSP--VKDgngnvafkgqGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLS 972
Cdd:cd14921 457 TEQGNHPKFQKPkqLKD----------KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDR 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 973 QTGslissypsfkfgghkSTLLSKRTASSMVGVNKNylelskllkkkgtstflqrlERGEPATAASQLTKSLADITAKLQ 1052
Cdd:cd14921 527 IVG---------------LDQMAKMTESSLPSASKT--------------------KKGMFRTVGQLYKEQLGKLMTTLR 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1053 RGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA--SVLLGETKGQAAeer 1130
Cdd:cd14921 572 NTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAanAIPKGFMDGKQA--- 648
|
730 740
....*....|....*....|....*
gi 568953283 1131 CRLVLQRCKLQG--WQIGVHKVFLK 1153
Cdd:cd14921 649 CILMIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
436-1153 |
9.33e-83 |
|
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: 287.62 E-value: 9.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYAIADNAYNDMLRNRENQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTM--------------FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQ 581
Cdd:cd14927 78 ITGESGAGKTVNTKRVIQYFAIVAALGDGPgkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 582 CCQRRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLN-NFCAHRYVSQGmredVSTAEHSLNK 660
Cdd:cd14927 158 FGPTGK-LASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQG----VTTVDNMDDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 661 ERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:cd14927 233 EELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 741 KGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqdeYKSL-QTLDIGILDIFGFEEFQKNEFEQLCVNLT 819
Cdd:cd14927 313 GNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTL-----DTKLpRQFFIGVLDIAGFEIFEFNSFEQLCINFT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 820 NEKMHHYIQEVLFLQEQTECVQEGVametacspgnQAGVLDF---------FFQKPSGFFSLLDEESQVIWSGEPNLPRK 890
Cdd:cd14927 388 NEKLQQFFNHHMFILEQEEYKREGI----------EWVFIDFgldlqacidLIEKPLGILSILEEECMFPKASDASFKAK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 891 L--QGLLESSNTNavySPVKDGNgnvafKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQ 968
Cdd:cd14927 458 LydNHLGKSPNFQ---KPRPDKK-----RKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYE 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 969 SKLSQTGSlissypsfkfGGHKSTLLSKR-TASSMVGVnknylelskllkkkgtstflqrlergepataaSQLTK-SLAD 1046
Cdd:cd14927 530 NYVGSDST----------EDPKSGVKEKRkKAASFQTV--------------------------------SQLHKeNLNK 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1047 ITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETK--- 1123
Cdd:cd14927 568 LMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDDKfvd 647
|
730 740 750
....*....|....*....|....*....|
gi 568953283 1124 GQAAEERCRLVLQRCKLQgWQIGVHKVFLK 1153
Cdd:cd14927 648 SRKATEKLLGSLDIDHTQ-YQFGHTKVFFK 676
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
437-1116 |
2.11e-81 |
|
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: 282.19 E-value: 2.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSPTGQRSPS--------LPPHLFSCAERAFHR--- 504
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLLSFEARSSStrnkgsdpMPPHIYQVAGEAYKAmml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 505 -LFQERKPQNIILSGERGSGKTQASKQIMKYL-----------TSRASSSCTMFDSRLRHAIyIVEAFGHAKTTLNNVSS 572
Cdd:cd14900 82 gLNGVMSDQSILVSGESGSGKTESTKFLMEYLaqagdnnlaasVSMGKSTSGIAAKVLQTNI-LLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 573 CLIQYWELQCCQRRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKcglhlnnfcahryvsqgmredvs 652
Cdd:cd14900 161 RFGKFIKLHFTSGGR-LTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR----------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 653 tAEHSLNKerlaaLKHALNVIGFSTLEVENLFVILSAILHIGDIQFTA--LTEADSAFVSDL-----QLLEQVAGMLQVS 725
Cdd:cd14900 217 -KRDMYRR-----VMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHdeNSDRLGQLKSDLapssiWSRDAAATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 726 TDELASALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTLD-IGILDIFGFE 804
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHfIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 805 EFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQVIWSGE 884
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQD-CVNLISQRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 885 PNLPRKLQGLLEsSNTNAVYSPVKDGNGnvafkgqgaAFTVMHYAGRVMYEMGGAVERNKDSLSQNllfvmktsenvvIS 964
Cdd:cd14900 450 TTLASKLYRACG-SHPRFSASRIQRARG---------LFTIVHYAGHVEYSTDGFLEKNKDVLHQE------------AV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 965 HLFQSKLsqtgslissypsfkfgghkstllskrtassmvgvnknylelskllkkkgtstflqrlergepataasQLTKSL 1044
Cdd:cd14900 508 DLFVYGL-------------------------------------------------------------------QFKEQL 520
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568953283 1045 ADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLAS 1116
Cdd:cd14900 521 TTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLAR 592
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
436-1153 |
2.19e-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: 283.52 E-value: 2.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDS-----RLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcQRRKHIT 590
Cdd:cd14919 78 CTGESGAGKTENTKKVIQYLAHVASSHKSKKDQgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 591 GARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMredvSTAEHSLNKERLAALKHAL 670
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH----VTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 671 NVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHT 750
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 751 IQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEV 830
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 831 LFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQK--PSGFFSLLDEESqviWSGEPNLPRKLQGLLESSNTNAVYSPVK 908
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEEC---WFPKATDKSFVEKVVQEQGTHPKFQKPK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 909 DgngnvaFKGQgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQS-----KLSQTGSLissyps 983
Cdd:cd14919 467 Q------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiGLDQVAGM------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 984 fkfgghkstllskrTASSMVGVNKNylelskllkkkgtstflqrlERGEPATAASQLTKSLADITAKLQRGSPHFILCIK 1063
Cdd:cd14919 534 --------------SETALPGAFKT--------------------RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCII 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1064 PNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA--SVLLGETKGQAAeerCRLVLQRCKLQ 1141
Cdd:cd14919 580 PNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTpnSIPKGFMDGKQA---CVLMIKALELD 656
|
730
....*....|....
gi 568953283 1142 G--WQIGVHKVFLK 1153
Cdd:cd14919 657 SnlYRIGQSKVFFR 670
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
437-1153 |
1.19e-79 |
|
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: 278.47 E-value: 1.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRA----------SSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRR 586
Cdd:cd14913 79 TGESGAGKTVNTKRVIQYFATIAatgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 587 KhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEE-KCGLHLNNFCAHRYVSQGmreDVSTAEHSlNKERLAA 665
Cdd:cd14913 159 K-LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFISQG---EILVASID-DAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 666 LKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVI 745
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 746 IRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclQNQDEYKSLQTLdIGILDIFGFEEFQKNEFEQLCVNLTNEKMHH 825
Cdd:cd14913 314 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRIN---QQLDTKLPRQHF-IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 826 YIQEVLFLQEQTECVQEGVAMeTACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNtnav 903
Cdd:cd14913 390 FFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN---- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 904 YSPVKDGNGNVAfkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSlissyps 983
Cdd:cd14913 465 FQKPKVVKGRAE-----AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAD------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 984 fkfgghkstlLSKRTASSMVGvnknylelskllkkkgtSTFlqrlergepATAASQLTKSLADITAKLQRGSPHFILCIK 1063
Cdd:cd14913 533 ----------SGKKKVAKKKG-----------------SSF---------QTVSALFRENLNKLMSNLRTTHPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1064 PNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQAAEERCRLVLQRCKLQ-- 1141
Cdd:cd14913 577 PNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDht 656
|
730
....*....|..
gi 568953283 1142 GWQIGVHKVFLK 1153
Cdd:cd14913 657 QYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
436-1153 |
2.79e-79 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in 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: 277.11 E-value: 2.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMY---RGKRRNEVPPHIFAISDGAYVDMLTNHVNQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIY--------IVEAFGHAKTTLNNVSSCLIQYWELQCCQRRK 587
Cdd:cd14909 78 ITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEdqvvqtnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 588 hITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSS--EEKCGLHlNNFCAHRYVSQGMredvSTAEHSLNKERLAA 665
Cdd:cd14909 158 -LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPgvKEMCLLS-DNIYDYYIVSQGK----VTVPNVDDGEEFSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 666 LKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVI 745
Cdd:cd14909 232 TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 746 IRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHH 825
Cdd:cd14909 312 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF----IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 826 YIQEVLFLQEQTECVQEGVametacspgnQAGVLDF---------FFQKPSGFFSLLDEESQVIWSGEPNLPRKL-QGLL 895
Cdd:cd14909 388 FFNHHMFVLEQEEYKREGI----------DWAFIDFgmdllacidLIEKPMGILSILEEESMFPKATDQTFSEKLtNTHL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 896 ESSNTNAVYSPVKDGNgnvafkgQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTG 975
Cdd:cd14909 458 GKSAPFQKPKPPKPGQ-------QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 976 SlissyPSFKFGGhkstllskrtassmvgvnknylelskllkkkgtstflQRLERGEPATAASQLTKSLADITAKLQRGS 1055
Cdd:cd14909 531 G-----GEQAKGG-------------------------------------RGKKGGGFATVSSAYKEQLNSLMTTLRSTQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1056 PHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA-SVLLGETKGQAAEERCrlv 1134
Cdd:cd14909 569 PHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNpAGIQGEEDPKKAAEII--- 645
|
730 740
....*....|....*....|.
gi 568953283 1135 LQRCKL--QGWQIGVHKVFLK 1153
Cdd:cd14909 646 LESIALdpDQYRLGHTKVFFR 666
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
436-1153 |
4.91e-79 |
|
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: 276.56 E-value: 4.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFDS------------RLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCc 583
Cdd:cd15896 78 CTGESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 584 QRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMredvSTAEHSLNKERL 663
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGN----VTIPGQQDKDLF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 664 AALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd15896 233 TETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 744 VIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKM 823
Cdd:cd15896 313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 824 HHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQ--KPSGFFSLLDEESqviWSGEPNLPRKLQGLLESSNTN 901
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKpaSPPGILALLDEEC---WFPKATDKSFVEKVLQEQGTH 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 902 AVYSPVKDgngnvaFKGQgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGslissy 981
Cdd:cd15896 467 PKFFKPKK------LKDE-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 982 psfkfgghkstlLSKRTA-SSMVGVNKNylelskllkkkgtstflqrlERGEPATAASQLTKSLADITAKLQRGSPHFIL 1060
Cdd:cd15896 534 ------------LDKVSGmSEMPGAFKT--------------------RKGMFRTVGQLYKEQLSKLMATLRNTNPNFVR 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1061 CIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA--SVLLGETKGQAAeerCRLVLQRC 1138
Cdd:cd15896 582 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpnAIPKGFMDGKQA---CVLMIKSL 658
|
730
....*....|....*..
gi 568953283 1139 KLQG--WQIGVHKVFLK 1153
Cdd:cd15896 659 ELDPnlYRIGQSKVFFR 675
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
442-1153 |
1.70e-78 |
|
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: 274.46 E-value: 1.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 442 IQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSPTGQRS--PSLPPHLFSCAERAFHRLFQERKPQNIILSG 518
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSRGfpSDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 519 ERGSGKTQASKQIMKYLTSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQcCQRRKHITGARISTYM 598
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLL-VGPDGGLKGGKITSYM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 599 LEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEhslNKERLAALKHALNVIgFSTL 678
Cdd:cd14886 166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGID---DQKEFAPVRSQLEKL-FSKN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 679 EVENLFVILSAILHIGDIQFTALTEA---DSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQMAA 755
Cdd:cd14886 242 EIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 756 FYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQE 835
Cdd:cd14886 322 VNIRAVAKDLYGALFELCVDTLNEIIQFDADARPW----IGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 836 QTECVQEGV--AMETACSPGNQAGVLDfffqKPS-GFFSLLdEESQVIWSGEPnlprklqglleSSNTNAVYSPVKDgNG 912
Cdd:cd14886 398 IQEYEIEGIdhSMITFTDNSNVLAVFD----KPNlSIFSFL-EEQCLIQTGSS-----------EKFTSSCKSKIKN-NS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 913 NVAFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSLissypsfkfgghKST 992
Cdd:cd14886 461 FIPGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNM------------KGK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 993 LLSKRTASSMvgvnknylelskllkkkgtstflqrlergepataaSQLTKSLADITAklqrgspHFILCIKPNTSQLPGV 1072
Cdd:cd14886 529 FLGSTFQLSI-----------------------------------DQLMKTLSATKS-------HFIRCIKTNQDKVPNK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1073 FDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASV-LLGETKGQAAEERCRLVLQRCKL--QGWQIGVHK 1149
Cdd:cd14886 567 YETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHnSSSQNAGEDLVEAVKSILENLGIpcSDYRIGKTK 646
|
....
gi 568953283 1150 VFLK 1153
Cdd:cd14886 647 VFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
436-1153 |
1.47e-77 |
|
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: 272.07 E-value: 1.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFgnDQIH---TFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQRSpsLPPHLFSCAERAFHRLF-QERKP 511
Cdd:cd14875 1 ATLLHCIKERF--EKLHqqySLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRL--LPPHIWQVAHKAFNAIFvQGLGN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 512 QNIILSGERGSGKTQASKQIMKYL--TSRASSSCTM-------FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQC 582
Cdd:cd14875 77 QSVVISGESGSGKTENAKMLIAYLgqLSYMHSSNTSqrsiadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 583 CQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGL-HLNNFCAHRYVSQG---MREDVSTaeHSL 658
Cdd:cd14875 157 DPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGntfVRRGVDG--KTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 659 N-KERLAALKHALNVIGFsTLEVEN-LFVILSAILHIGDIQFTAlTEADSAFVSDLQLLEQVAGMLQVSTDELASALttd 736
Cdd:cd14875 235 DdAHEFQNVRHALSMIGV-ELETQNsIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLRECF--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 737 iqyfkgdvIIRRHTI--------QMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTldIGILDIFGFEEFQK 808
Cdd:cd14875 310 --------LVKSKTSlvtilankTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGCKY--IGLLDIFGFENFTR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 809 NEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVlDFFFQKPSGFFSLLDEESQviWSGEpNLP 888
Cdd:cd14875 380 NSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECV-NMFDQKRTGIFSMLDEECN--FKGG-TTE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 889 RKLQGLLES-SNTNAVYSPVKDGNGNvafkgqgaAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLF 967
Cdd:cd14875 456 RFTTNLWDQwANKSPYFVLPKSTIPN--------QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 968 QSKlsqtgslissypsfkfgghksTLLSKRtassmvgvnKNylelskllkkkgtstflqrlergepaTAASQLTKSLADI 1047
Cdd:cd14875 528 STE---------------------KGLARR---------KQ--------------------------TVAIRFQRQLTDL 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1048 TAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFlSRY----EPLASVLLgeTK 1123
Cdd:cd14875 552 RTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF-CRYfyliMPRSTASL--FK 628
|
730 740 750
....*....|....*....|....*....|....*.
gi 568953283 1124 GQAAEERCRLVLQRC-KLQGWQ-----IGVHKVFLK 1153
Cdd:cd14875 629 QEKYSEAAKDFLAYYqRLYGWAkpnyaVGKTKVFLR 664
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
437-1153 |
3.37e-77 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 270.46 E-value: 3.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTgqRSPSlPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKS--RSDN-APHIFSVADSAYQDMLHHEEPQHIIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLT--SRASSSCTMfdsRLRHAIYIVEAFGHAKTTLNNVSS-CLIQYwELQCCQRRKhITGAR 593
Cdd:cd14882 79 SGESYSGKTTNARLLIKHLCylGDGNRGATG---RVESSIKAILALVNAGTPLNADSTrCILQY-QLTFGSTGK-MSGAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 594 ISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKcglhLNNFC-----AHRYvsqgMREDVSTAEHSL---------N 659
Cdd:cd14882 154 FWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR----LKEYNlkagrNYRY----LRIPPEVPPSKLkyrrddpegN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 660 KERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTaltEAD-SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQ 738
Cdd:cd14882 226 VERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR---QNGgYAELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 739 YFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclQNQDEYKSL--QTLDIGILDIFGFEEFQKNEFEQLCV 816
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRIN---MKMSFPRAVfgDKYSISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 817 NLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVlDFFFQKPSGFFSLLDEESqviwsgepnlpRKLQGlle 896
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAV-DQLMTKPDGLFYIIDDAS-----------RSCQD--- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 897 ssnTNAVYSPVKDGNGNVAFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSklSQTGS 976
Cdd:cd14882 445 ---QNYIMDRIKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--SQVRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 977 LissypsfkfgghkstllskRTASsmvgvnknylelskllkkkgtSTFlqrlergePATAAsQLTKSLADITAKlqrGSP 1056
Cdd:cd14882 520 M-------------------RTLA---------------------ATF--------RATSL-ELLKMLSIGANS---GGT 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1057 HFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLAsVLLGETKgQAAEERCRLVLQ 1136
Cdd:cd14882 548 HFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLA-FDFDETV-EMTKDNCRLLLI 625
|
730
....*....|....*..
gi 568953283 1137 RCKLQGWQIGVHKVFLK 1153
Cdd:cd14882 626 RLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
437-1153 |
7.46e-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: 267.37 E-value: 7.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCT------------MFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQ 584
Cdd:cd14910 79 TGESGAGKTVNTKRVIQYFATIAVTGEKkkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 585 RRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSE--EKCGLHLNNFcAHRYVSQGMredvSTAEHSLNKER 662
Cdd:cd14910 159 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDliEMLLITTNPY-DYAFVSQGE----ITVPSIDDQEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 663 LAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 742
Cdd:cd14910 233 LMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 743 DVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclqNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEK 822
Cdd:cd14910 313 EYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 823 MHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDfFFQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNt 900
Cdd:cd14910 389 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSNN- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 901 navYSPVKDGNGNVAfkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSliss 980
Cdd:cd14910 467 ---FQKPKPAKGKVE-----AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAE---- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 981 ypsfKFGGHKStllSKRTASSMvgvnknylelskllkkkgtstflqrlergepATAASQLTKSLADITAKLQRGSPHFIL 1060
Cdd:cd14910 535 ----EGGGKKG---GKKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPHFVR 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1061 CIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETK---GQAAEERCRLVLQR 1137
Cdd:cd14910 577 CIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLGSIDI 656
|
730
....*....|....*.
gi 568953283 1138 CKLQgWQIGVHKVFLK 1153
Cdd:cd14910 657 DHTQ-YKFGHTKVFFK 671
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
442-1152 |
2.15e-75 |
|
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: 264.67 E-value: 2.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 442 IQKRFGNDQIHTFIGDIFLLVNPFKELPiystmvsqMYLSPTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIILSGERG 521
Cdd:cd14881 7 LQARFYAKEFFTNVGPILLSVNPYRDVG--------NPLTLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 522 SGKTQASKQIMKYLTSRAS--SSCTMFdSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQccqrrkhIT-GA----RI 594
Cdd:cd14881 79 SGKTYASMLLLRQLFDVAGggPETDAF-KHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQ-------VTdGAlyrtKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 595 STYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAH--RYVSQG-MREDvsTAEhslNKERLAALKHALN 671
Cdd:cd14881 151 HCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPAnlRYLSHGdTRQN--EAE---DAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 672 VIGFSTLEVENlfvILSAILHIGDIQFTALTEADSAFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTI 751
Cdd:cd14881 226 ILGIPFLDVVR---VLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 752 QMAAFYRDLLAKSLYSRLFGFLINTVNCcLQNQDEYKSLQTLD--IGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQE 829
Cdd:cd14881 302 NMSNMTRDALAKALYCRTVATIVRRANS-LKRLGSTLGTHATDgfIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 830 VLFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPR-KLQglleSSNTNAVYSPVK 908
Cdd:cd14881 381 HIFKSSIESCRDEGIQCEVEVDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTAESYVAKiKVQ----HRQNPRLFEAKP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 909 DGngnvafkgqGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKtsenvvishlfqsklSQTGslissypSFKFGG 988
Cdd:cd14881 457 QD---------DRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY---------------KQNC-------NFGFAT 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 989 HkstllskrtassmvgvnknylelskllkkkgTSTFLQRLErgepataasQLTKSLADitAKlqrgsPHFILCIKPNTSQ 1068
Cdd:cd14881 506 H-------------------------------TQDFHTRLD---------NLLRTLVH--AR-----PHFVRCIRSNTTE 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1069 LPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASV-LLGETKGQAAEErCRLVLQRCKLQ------ 1141
Cdd:cd14881 539 TPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFrLLRRVEEKALED-CALILQFLEAQppskls 617
|
730
....*....|....*
gi 568953283 1142 ----GWQIGVHKVFL 1152
Cdd:cd14881 618 svstSWALGKRHIFL 632
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
436-1153 |
2.59e-75 |
|
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: 265.81 E-value: 2.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY---RGKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTM--------FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcQRRK 587
Cdd:cd14930 78 CTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 588 HITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDvSTAEHSLNKERLAALK 667
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 668 halnVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIR 747
Cdd:cd14930 236 ----VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 748 RHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYI 827
Cdd:cd14930 312 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 828 QEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQ--KPSGFFSLLDEESqviWSGEPNLPRKLQGLLESSNTNAVYS 905
Cdd:cd14930 389 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERpaNPPGLLALLDEEC---WFPKATDKSFVEKVAQEQGGHPKFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 906 PVKDgngnvaFKGQgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQS-----KLSQTGSLISS 980
Cdd:cd14930 466 RPRH------LRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 981 YPsfkfGGhkstllskrtassmvgvnknylelskllkkkgtstflqRLERGEPATAASQLTKSLADITAKLQRGSPHFIL 1060
Cdd:cd14930 539 PP----GG--------------------------------------RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVR 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1061 CIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA--SVLLGETKGQAAeerCRLVLQRC 1138
Cdd:cd14930 577 CIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTpnAIPKGFMDGKQA---CEKMIQAL 653
|
730
....*....|....*..
gi 568953283 1139 KLQG--WQIGVHKVFLK 1153
Cdd:cd14930 654 ELDPnlYRVGQSKIFFR 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
437-1153 |
3.43e-74 |
|
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: 262.36 E-value: 3.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRA---------SSSCTM---FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQ 584
Cdd:cd14915 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 585 RRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSE--EKCGLHLNNFcAHRYVSQGMredvSTAEHSLNKER 662
Cdd:cd14915 159 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEliEMLLITTNPY-DFAFVSQGE----ITVPSIDDQEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 663 LAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 742
Cdd:cd14915 233 LMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 743 DVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclqNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEK 822
Cdd:cd14915 313 EYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 823 MHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDfFFQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNt 900
Cdd:cd14915 389 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSNN- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 901 navYSPVKDGNGNVAfkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLF---QSKLSQTGsl 977
Cdd:cd14915 467 ---FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFsggQTAEAEGG-- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 978 issypsfkfGGHKStllSKRTASSMvgvnknylelskllkkkgtstflqrlergepATAASQLTKSLADITAKLQRGSPH 1057
Cdd:cd14915 537 ---------GGKKG---GKKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPH 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1058 FILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQAAEERCRLVLQR 1137
Cdd:cd14915 574 FVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGS 653
|
730
....*....|....*...
gi 568953283 1138 CKLQ--GWQIGVHKVFLK 1153
Cdd:cd14915 654 IDIDhtQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
437-1153 |
3.54e-74 |
|
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: 262.36 E-value: 3.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCT------------MFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQ 584
Cdd:cd14912 79 TGESGAGKTVNTKRVIQYFATIAVTGEKkkeeitsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 585 RRKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSE--EKCGLHLNNFcAHRYVSQGmreDVSTAEHSlNKER 662
Cdd:cd14912 159 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPEliEMLLITTNPY-DYPFVSQG---EISVASID-DQEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 663 LAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 742
Cdd:cd14912 233 LMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 743 DVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclqNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEK 822
Cdd:cd14912 313 EYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 823 MHHYIQEVLFLQEQTECVQEGVAMeTACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNt 900
Cdd:cd14912 389 LQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSAN- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 901 navYSPVKdgngnvAFKGQGAA-FTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSklSQTGSLIS 979
Cdd:cd14912 467 ---FQKPK------VVKGKAEAhFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG--AQTAEGAS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 980 SYPSFKFGGhkstllsKRTASSMvgvnknylelskllkkkgtstflqrlergepATAASQLTKSLADITAKLQRGSPHFI 1059
Cdd:cd14912 536 AGGGAKKGG-------KKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPHFV 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1060 LCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETK---GQAAEERCRLVLQ 1136
Cdd:cd14912 578 RCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLASID 657
|
730
....*....|....*..
gi 568953283 1137 RCKLQgWQIGVHKVFLK 1153
Cdd:cd14912 658 IDHTQ-YKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
437-1130 |
8.93e-74 |
|
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: 261.15 E-value: 8.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTS-----------RASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQR 585
Cdd:cd14916 79 TGESGAGKTVNTKRVIQYFASiaaigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 586 RKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEE-KCGLHLNNFCAHRYVSQGmreDVSTAEHSlNKERLA 664
Cdd:cd14916 159 GK-LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELlDMLLVTNNPYDYAFVSQG---EVSVASID-DSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 665 ALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDV 744
Cdd:cd14916 234 ATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 745 IIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqdEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMH 824
Cdd:cd14916 314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 825 HYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFfQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNtna 902
Cdd:cd14916 390 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLydNHLGKSNN--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 903 vYSPVKDGNGNvafkgQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKtsenvvishlfQSKLSQTGSLISSYP 982
Cdd:cd14916 466 -FQKPRNVKGK-----QEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQ-----------KSSLKLMATLFSTYA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 983 SFKFGGHKSTLLSKRTASSMvgvnknylelskllkkkGTSTFLQRlergepataasqltKSLADITAKLQRGSPHFILCI 1062
Cdd:cd14916 529 SADTGDSGKGKGGKKKGSSF-----------------QTVSALHR--------------ENLNKLMTNLKTTHPHFVRCI 577
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953283 1063 KPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGEtkGQAAEER 1130
Cdd:cd14916 578 IPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE--GQFIDSR 643
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
437-1130 |
4.26e-73 |
|
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: 258.88 E-value: 4.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRA----------SSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRR 586
Cdd:cd14917 79 TGESGAGKTVNTKRVIQYFAVIAaigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 587 KhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHL-NNFCAHRYVSQGMredvSTAEHSLNKERLAA 665
Cdd:cd14917 159 K-LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGE----TTVASIDDAEELMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 666 LKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVI 745
Cdd:cd14917 234 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 746 IRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLqnqdEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHH 825
Cdd:cd14917 314 TKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 826 YIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDfFFQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNTNav 903
Cdd:cd14917 390 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSNNFQ-- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 904 yspvKDGNgnvaFKGQGAA-FTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSqtgsliSSYP 982
Cdd:cd14917 467 ----KPRN----IKGKPEAhFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAG------ADAP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 983 SFKFGGHKSTLLSKRTASSmvgvnknylelskllkkkgtstfLQRlergepataasqltKSLADITAKLQRGSPHFILCI 1062
Cdd:cd14917 533 IEKGKGKAKKGSSFQTVSA-----------------------LHR--------------ENLNKLMTNLRSTHPHFVRCI 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953283 1063 KPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGEtkGQAAEER 1130
Cdd:cd14917 576 IPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE--GQFIDSR 641
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
437-1153 |
2.15e-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: 256.92 E-value: 2.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRA-----------SSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQR 585
Cdd:cd14923 79 TGESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 586 RKhITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLN-NFCAHRYVSQGmreDVSTAEHSlNKERLA 664
Cdd:cd14923 159 GK-LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQG---EVTVASID-DSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 665 ALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDV 744
Cdd:cd14923 234 ATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 745 IIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclQNQDEYKSLQTLdIGILDIFGFEEFQKNEFEQLCVNLTNEKMH 824
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRIN---QQLDTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 825 HYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFfQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNtna 902
Cdd:cd14923 390 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 903 vYSPVKDGNGNVAfkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFqsklsqtgsliSSYP 982
Cdd:cd14923 466 -FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-----------SNYA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 983 SFKFG-GHKSTLLSKRTASSMvgvnknylelskllkkkgtstflqrlergepATAASQLTKSLADITAKLQRGSPHFILC 1061
Cdd:cd14923 529 GAEAGdSGGSKKGGKKKGSSF-------------------------------QTVSAVFRENLNKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1062 IKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKGQAAEERCRLVLQRCKL- 1140
Cdd:cd14923 578 LIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFIDSKNASEKLLNSIDVd 657
|
730
....*....|....
gi 568953283 1141 -QGWQIGVHKVFLK 1153
Cdd:cd14923 658 rEQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
438-1153 |
2.58e-72 |
|
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: 256.58 E-value: 2.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 438 LLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIILS 517
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 518 GERGSGKTQASKQIMKYLTS-------RASSSCTM---FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRRK 587
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATiavtgekKKEESGKMqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 588 hITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSE--EKCGLHLNNFcAHRYVSQGMredvSTAEHSLNKERLAA 665
Cdd:cd14918 160 -LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDliEMLLITTNPY-DYAFVSQGE----ITVPSIDDQEELMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 666 LKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDVI 745
Cdd:cd14918 234 TDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 746 IRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNcclqNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHH 825
Cdd:cd14918 314 TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 826 YIQEVLFLQEQTECVQEGVAMeTACSPGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKL--QGLLESSNtnav 903
Cdd:cd14918 390 FFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLydQHLGKSAN---- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 904 YSPVKdgngnvAFKGQGAA-FTVMHYAGRVMYEMGGAVERNKDSLSqnllfvmktseNVVISHLFQSKLSQTGSLISSYP 982
Cdd:cd14918 465 FQKPK------VVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLN-----------DTVVGLYQKSAMKTLASLFSTYA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 983 SfkfgghkstllSKRTASSMVGVNKNylelskllkkkgTSTFlqrlergepATAASQLTKSLADITAKLQRGSPHFILCI 1062
Cdd:cd14918 528 S-----------AEADSGAKKGAKKK------------GSSF---------QTVSALFRENLNKLMTNLRSTHPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1063 KPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETK---GQAAEERCRLVLQRCK 1139
Cdd:cd14918 576 IPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQfidSKKASEKLLASIDIDH 655
|
730
....*....|....
gi 568953283 1140 LQgWQIGVHKVFLK 1153
Cdd:cd14918 656 TQ-YKFGHTKVFFK 668
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
436-1140 |
6.04e-72 |
|
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: 256.95 E-value: 6.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYL----SPTGQRSPSL---PPHLFSCAERAFHRLFQ 507
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnSQFGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 508 ERKPQNIILSGERGSGKTQASKQIMKYL-----------------TSRASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNV 570
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFavhcgtgnnnltnsesiSPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 571 SSCLIQYWELQCCQRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDG----LSSEEKCGLHLN----NFcahRY 642
Cdd:cd14899 161 SSRFGKFIELRFRDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSggpqSF---RL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 643 VSQGM----REDVSTAEhslnkeRLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEA--DSAFVSDLQLLE 716
Cdd:cd14899 238 LNQSLcskrRDGVKDGV------QFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKgdDTVFADEARVMS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 717 QVAG----------MLQVSTDELASALTTDIQYFKGDVIIRRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQ-- 784
Cdd:cd14899 312 STTGafdhftkaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQas 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 785 DEYKSLQTLD---------IGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQ 855
Cdd:cd14899 392 APWGADESDVddeedatdfIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 856 AgVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESSNTNAVYSpvkdgngNVAFKGQGAAFTVMHYAGRVMYE 935
Cdd:cd14899 472 A-CLELFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFR-------SAPLIQRTTQFVVAHYAGCVTYT 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 936 MGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSLISSYPSfkFGGHKSTLLSKRTASSMVGvnknylelskl 1015
Cdd:cd14899 544 IDGFLAKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDG--FGGRTRRRAKSAIAAVSVG----------- 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1016 lkkkgtstflqrlergepataaSQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFR 1095
Cdd:cd14899 611 ----------------------TQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVAR 668
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 568953283 1096 SGYPVRPSFEDFLSRYEP-LASVLLGETKGQAAEERCRLVLQRCKL 1140
Cdd:cd14899 669 AGFPVRLTHKQFLGRYRRvLLSLYKWGDNDFERQMRCGVSLGKTRV 714
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
436-1115 |
1.01e-71 |
|
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: 254.78 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYLSPTgqRSPSLPPHLFSCAERAFHRLFQERKP--Q 512
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAP--QPQKLKPHIFTVGEQTYRNVKSLIEPvnQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 513 NIILSGERGSGKTQASKQIMKYLTSRASSSCTM--------FDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcQ 584
Cdd:cd14880 79 SIVVSGESGAGKTWTSRCLMKFYAVVAASPTSWeshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL-N 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 585 RRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQgmredvstAEHSLNKERLA 664
Cdd:cd14880 158 RAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPN--------PERNLEEDCFE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 665 ALKHALNVIGFSTLEVENLFVILSAILHIGDIQFT-ALTEADSAFVSDL--QLLEQVAGMLQVSTDELASALTT-DIQYF 740
Cdd:cd14880 230 VTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFAdSEDEAQPCQPMDDtkESVRTSALLLKLPEDHLLETLQIrTIRAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 741 KGDVIIRRHTIQMAA-FYRDLLAKSLYSRLFGFLINTVNcclQNQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLT 819
Cdd:cd14880 310 KQQQVFKKPCSRAECdTRRDCLAKLIYARLFDWLVSVIN---SSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 820 NEKM-HHYIQEVLFLQeQTECVQEGVAMETACSPGNQAgVLDFFFQKPSGFFSLLDEESQViwsGEPNLPRKLQGLLESS 898
Cdd:cd14880 387 NEKLqQHFVAHYLRAQ-QEEYAVEGLEWSFINYQDNQT-CLDLIEGSPISICSLINEECRL---NRPSSAAQLQTRIESA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 899 NTNavyspvKDGNGNVAFKGQgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKlsqtgsli 978
Cdd:cd14880 462 LAG------NPCLGHNKLSRE-PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN-------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 979 ssypsfkfgGHKSTLLSKRTASSMVGVnknylelskllkkkgtstflqrlergepaTAASQLTKSLADITAKLQRGSPHF 1058
Cdd:cd14880 527 ---------PEEKTQEEPSGQSRAPVL-----------------------------TVVSKFKASLEQLLQVLHSTTPHY 568
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 568953283 1059 ILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLA 1115
Cdd:cd14880 569 IRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
451-1112 |
6.61e-71 |
|
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: 254.19 E-value: 6.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 451 IHTFIGDIFLLVNPFKELPIYStmvsQMYLSPTGQRSPS-LPPHLFSCAERAFHRLFQERKPQNIILSGERGSGKTQASK 529
Cdd:cd14887 24 IYTYTGTLLIAVNPYRFFNLYD----RQWISRFDTEANSrLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 530 QIMKYLTS----RASSSCTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCCQRRKhITGARISTYMLEKSRVV 605
Cdd:cd14887 100 HVLTYLAAvsdrRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGK-LTRASVATYLLANERVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 606 AQPPGQGTFLIFSWLMDG--LSSEEKcglhlnnfcahryVSQGMREDVSTAehslnkerLAALKHALNVIGFSTLEVENL 683
Cdd:cd14887 179 RIPSDEFSFHIFYALCNAavAAATQK-------------SSAGEGDPESTD--------LRRITAAMKTVGIGGGEQADI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 684 FVILSAILHIGDIQFTALTEADSAFVSDL-----QLLEQVAGMLQVS-TDELASALTTDIQYFKGDVIIRR--------- 748
Cdd:cd14887 238 FKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvGCEETAADRSHSSeVKCLSSGLKVTEASRKHLKTVARllglppgve 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 749 --------------------HTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDE------------YKSLQTldIG 796
Cdd:cd14887 318 geemlrlalvsrsvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsdedtpsTTGTQT--IG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 797 ILDIFGFEEFQ---KNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVL-DFFFQKPSGFFSL 872
Cdd:cd14887 396 ILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLaSTLTSSPSSTSPF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 873 LDEESQVIWSGEPNLPRKLQGLLESSNTNAVYSPVKDGNGNV----------------------AFKGQGAAFTVMHYAG 930
Cdd:cd14887 476 SPTPSFRSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSdlfyeklnkniinsakyknitpALSRENLEFTVSHFAC 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 931 RVMYEMGGAVERNKDSLSQNLlfvmktsenvvishlfqsklsqtgslissypsfkfgghKSTLLSKRTASSMVGVNKNYL 1010
Cdd:cd14887 556 DVTYDARDFCRANREATSDEL--------------------------------------ERLFLACSTYTRLVGSKKNSG 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1011 elskllkkkgtstflQRLERGEPATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGL 1090
Cdd:cd14887 598 ---------------VRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDL 662
|
730 740
....*....|....*....|..
gi 568953283 1091 VRLFRSGYPVRPSFEDFLSRYE 1112
Cdd:cd14887 663 LRVMADGFPCRLPYVELWRRYE 684
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
436-1153 |
3.38e-65 |
|
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: 234.77 E-value: 3.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYlsptgqrspslppHLFSCAERAFHRLFQ-ERKPQNI 514
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC-------------HISGVAENALDRIKSmSSNAESI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 515 ILSGERGSGKTQASKQIMKYLTSRASSSCTMFDSrlrHAI-YIVEAFGHAKTTLNNVSScliQY-WELQCCQRRKHITGA 592
Cdd:cd14874 68 VFGGESGSGKSYNAFQVFKYLTSQPKSKVTTKHS---SAIeSVFKSFGCAKTLKNDEAT---RFgCSIDLLYKRNVLTGL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 593 RIS-TYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGmrEDVSTAEHSLNkeRLAALKHALN 671
Cdd:cd14874 142 NLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQG--NSTENIQSDVN--HFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 672 VIGFSTLEVENLFVILSAILHIGDIQFTAL----TEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQyfKGDVIir 747
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTKrnpnVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSE--DGTTI-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 748 rhTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNqdeykSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYI 827
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-----PLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 828 QEVLFLQEQTECVQEGVAMETACSPGNQAG-VLDFFFQKPSGFFSLLDEESQviwsgepnLPR-KLQGLLESSNTNAVYs 905
Cdd:cd14874 367 VKHSFHDQLVDYAKDGISVDYKVPNSIENGkTVELLFKKPYGLLPLLTDECK--------FPKgSHESYLEHCNLNHTD- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 906 pvKDGNGNVAFKGQgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSLISSypsfk 985
Cdd:cd14874 438 --RSSYGKARNKER-LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVS----- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 986 fgghkstllskrtassmvgvnknylelskllkkkgtstflqrlergepatAASQLTKSLADITAKLQRGSPHFILCIKPN 1065
Cdd:cd14874 510 --------------------------------------------------QAQFILRGAQEIADKINGSHAHFVRCIKSN 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1066 TSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLasvLLGE-TKGQAAEERCRLVLQRcklQG-- 1142
Cdd:cd14874 540 NERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL---LPGDiAMCQNEKEIIQDILQG---QGvk 613
|
730
....*....|....*
gi 568953283 1143 ----WQIGVHKVFLK 1153
Cdd:cd14874 614 yendFKIGTEYVFLR 628
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
437-1118 |
5.26e-63 |
|
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: 226.70 E-value: 5.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQrspslpPHLFSCAERAFHRLFQERKpQNIIL 516
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE------PHVYDVAEASVQDLLVHGN-QTIVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSScTMFDSRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWELQCcqrRKHITGARIST 596
Cdd:cd14898 75 SGESGSGKTENAKLVIKYLVERTAST-TSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF---DGKITGAKFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 597 YMLEKSRVVAQPPGQGTFLIFSwlmdglsseekcglhlnNFCAHRYVSqgMRED-VSTAEHSLNKERLA-------ALKH 668
Cdd:cd14898 151 YLLEKSRVTHHEKGERNFHIFY-----------------QFCASKRLN--IKNDfIDTSSTAGNKESIVqlsekykMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 669 ALNVIGFSTL-EVENLfviLSAILHIGDIQFTalTEADSAFVSDlQLLEQVAGMLQVSTDELASALTT-DIQYfKGDVII 746
Cdd:cd14898 212 AMKSLGIANFkSIEDC---LLGILYLGSIQFV--NDGILKLQRN-ESFTEFCKLHNIQEEDFEESLVKfSIQV-KGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 747 RRHTIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEykslqtLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHY 826
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGE------RSISVLDIFGFEIFESNGLDQLCINWTNEKIQND 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 827 IQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDffFQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLessntnavysp 906
Cdd:cd14898 359 FIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRD--FEKPCGLMDLISEESFNAWGNVKNLLVKIKKYL----------- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 907 vkdgNGNVAFKGqGAAFTVMHYAGRVMYEMGGAVERNKDSLS----QNLLFVMKTSENVVISHlfqsklsqtgslissyp 982
Cdd:cd14898 426 ----NGFINTKA-RDKIKVSHYAGDVEYDLRDFLDKNREKGQllifKNLLINDEGSKEDLVKY----------------- 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 983 sFKfgghkstllskrtassmvgvnknylelskllkkkgtstflqrlergepataasqltKSLADITAKLQRGSPHFILCI 1062
Cdd:cd14898 484 -FK--------------------------------------------------------DSMNKLLNSINETQAKYIKCI 506
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 568953283 1063 KPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYEPLASVL 1118
Cdd:cd14898 507 RPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
437-1101 |
1.69e-62 |
|
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: 227.87 E-value: 1.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELP-IYSTMVSQMYL----SPTGQRSPSLPPHLFSCAERAFHRLFQERKP 511
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksNSAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 512 QNIILSGERGSGKTQASKQIMKYLTSRASSSctMFDSRLRHAIY---IVEAFGHAKTTLNNVSS-C----LIQYWELQCC 583
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS--QMTERIDKLIYinnILESMSNATTIKNNNSSrCgrinLLIFEEVENT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 584 QRRKH---ITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEE--------KCGLH--LNNFCAH--RYVSQGMR 648
Cdd:cd14884 160 QKNMFngcFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDlarrnlvrNCGVYglLNPDESHqkRSVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 649 -----EDVSTAEHSLNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAgMLQ 723
Cdd:cd14884 240 lgsdsLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKAAAECLQIEEEDLENVIKYK-NIR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 724 VSTDelasalttdiqyfkgdvIIRRH-TIQMAAFYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLQTLD-------- 794
Cdd:cd14884 319 VSHE-----------------VIRTErRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDiysineai 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 795 IGILDIFGFEEFQKNEFEQLCVNLTNEKMH-HYIQEVLFlQEQTECVQEGVAMETACSPgNQAGVLDFffqkPSGFFSLL 873
Cdd:cd14884 382 ISILDIYGFEELSGNDFDQLCINLANEKLNnYYINNEIE-KEKRIYARENIICCSDVAP-SYSDTLIF----IAKIFRRL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 874 DEESQVIWSG----EPNLPRKL-----QGLLESSNTNAVYSPVKDGNGNVAFKGQGAAFTVMHYAGRVMYEMGGAVERNK 944
Cdd:cd14884 456 DDITKLKNQGqkktDDHFFRYLlnnerQQQLEGKVSYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 945 DSLSQNLLFVMKTSENVVishlfqskLSQTGSlissypsfkfGGHKSTLLSkrtassmvgVNKNYlelskllkkkgtstf 1024
Cdd:cd14884 536 DKIETSIETLISCSSNRF--------LREANN----------GGNKGNFLS---------VSKKY--------------- 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953283 1025 lqrlergepataasqlTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVR 1101
Cdd:cd14884 574 ----------------IKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK 634
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
436-1112 |
2.66e-58 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 216.76 E-value: 2.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSpTGQRSP--------SLPPHLFSCAERAFHRLFQ 507
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNK-SREQTPlyekdtvnDAPPHVFALAQNALRCMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 508 ERKPQNIILSGERGSGKTQASKQIMKYLTSRASSSCTMFDS------------RLRHAIYIVEAFGHAKTTLNNVSSCLI 575
Cdd:cd14893 80 AGEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSegasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 576 QYWELQCCQRRkHITGARISTYMLEKSRVVaqppgqgtflifswlmdglsseeKCGLHLNNFCAHRYVSQGMREDVSTAE 655
Cdd:cd14893 160 KMISVEFSKHG-HVIGGGFTTHYFEKSRVI-----------------------DCRSHERNFHVFYQVLAGVQHDPTLRD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 656 H-SLNK--ERLAALKHALNVIG---------------FSTLEVEN-----LFVILSAILHIGDIQF-------------- 698
Cdd:cd14893 216 SlEMNKcvNEFVMLKQADPLATnfaldardyrdlmssFSALRIRKnqrveIVRIVAALLHLGNVDFvpdpeggksvggan 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 699 -TALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDiQYFKGD-----VIIRRHTIQMAAFYRDLLAKSLYSRLFGF 772
Cdd:cd14893 296 sTTVSDAQSCALKDPAQILLAAKLLEVEPVVLDNYFRTR-QFFSKDgnktvSSLKVVTVHQARKARDTFVRSLYESLFNF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 773 LINTVNCCLQNQ-DEYKS----LQTLDIGILDIFGFEEF--QKNEFEQLCVNLTNEKMHH-YIQEVL-----FLQEQTEC 839
Cdd:cd14893 375 LVETLNGILGGIfDRYEKsnivINSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHfYVQNTLainfsFLEDESQQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 840 VQEGVAMETACS-PGNQAGVLDFFFQKPSGFFSLLDEESQVIWSGEPNLPRKL------QGLLESSNTNAVY-----SPV 907
Cdd:cd14893 455 VENRLTVNSNVDiTSEQEKCLQLFEDKPFGIFDLLTENCKVRLPNDEDFVNKLfsgneaVGGLSRPNMGADTtneylAPS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 908 KDGNgnvafkgqgAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSQTGSLissypsfkfG 987
Cdd:cd14893 535 KDWR---------LLFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSE---------K 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 988 GHKSTLLSKRTASSMvgvnknylelskllkkkGTSTFLQRLERGEPATAASQLTKSLADITAKLQRGSPHFILCIKPNTS 1067
Cdd:cd14893 597 AAKQTEERGSTSSKF-----------------RKSASSARESKNITDSAATDVYNQADALLHALNHTGKNFLVCIKPNET 659
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 568953283 1068 QLPGVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRYE 1112
Cdd:cd14893 660 LEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
436-1153 |
7.27e-57 |
|
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: 211.40 E-value: 7.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 436 SSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMylsPTGQRSPSLPPHLFSCAERAFHRLFQERKPQNII 515
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKM---FKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 516 LSGERGSGKTQASKQIMKYLTSRASSSCTMFD-SRLRHAIYIVEAFGHAKTTLNNVSSCLIQYWEL---QCCQrrkhITG 591
Cdd:cd01386 78 LLGRSGSGKTTNCRHILEYLVTAAGSVGGVLSvEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLdfdQAGQ----LAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 592 ARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRyvSQGMR-----EDVSTAEHSLNKerlaaL 666
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESN--SFGIVplqkpEDKQKAAAAFSK-----L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 667 KHALNVIGFSTLEVENLFVILSAILHIGDIQFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALttdiqyFKGDVii 746
Cdd:cd01386 227 QAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAI------FKHHL-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 747 rRHTIQMAAFYR---------------------DLLAKSLYSRLFGFLINTVNCCLQNQdeykSLQTLDIGILDIFGFE- 804
Cdd:cd01386 299 -SGGPQQSTTSSgqesparsssggpkltgvealEGFAAGLYSELFAAVVSLINRSLSSS----HHSTSSITIVDTPGFQn 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 805 -EFQKNE----FEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAM---ETACSPGNQAGVLDfffQKPS--------- 867
Cdd:cd01386 374 pAHSGSQrgatFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVdfdLPELSPGALVALID---QAPQqalvrsdlr 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 868 -----GFFSLLDEESQVIWSGEPNLPRKLQGLLESSNTNAVYSPVKDGNGNVAFKgqgaaftVMHYAGR--VMYEMGGav 940
Cdd:cd01386 451 dedrrGLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEGPLQFV-------LGHLLGTnpVEYDVSG-- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 941 ernkdslsqnllFVMKTSENVvishlfqSKLSQTGSLISSypSFKFGGHKStllskrtassmvgvnknylelskllkkkg 1020
Cdd:cd01386 522 ------------WLKAAKENP-------SAQNATQLLQES--QKETAAVKR----------------------------- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1021 TSTFLQrlergepataasqlTKSLAD-ITAKLQRGSPHFILCIKPNTSQLPGV------------FDHFYVSAQLQYLGV 1087
Cdd:cd01386 552 KSPCLQ--------------IKFQVDaLIDTLRRTGLHFVHCLLPQHNAGKDErstsspaagdelLDVPLLRSQLRGSQL 617
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953283 1088 LGLVRLFRSGYPVRPSFEDFLSRYEPLASVLLGETKG--------QAAEErcrlVLQRCKLQ--GWQIGVHKVFLK 1153
Cdd:cd01386 618 LDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLnsevaderKAVEE----LLEELDLEksSYRIGLSQVFFR 689
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
437-1111 |
8.56e-57 |
|
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: 210.72 E-value: 8.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIystMVSQMYLSPTGQRSpSLPPHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPF---LHSQELVRNYNQRR-GLPPHLFALAAKAISDMQDFRRDQLIFI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKY-LTSRASSSCTMFDSRLRHAIyIVEAFGHAKTTLNNVSSCLIQYWELqCCQRRKHITGARIS 595
Cdd:cd14905 78 GGESGSGKSENTKIIIQYlLTTDLSRSKYLRDYILESGI-ILESFGHASTDSNHNSSRWGKYFEM-FYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 596 TYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQGMREDVSTAEHSLNKERlaaLKHALNVIGF 675
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDR---LKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 676 STLEVENLFVILSAILHIGDIQFtaLTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDiqyfkgdviiRRHTIQMAA 755
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTF--FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPVNEAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 756 FYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldiGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQE 835
Cdd:cd14905 301 ENRDSLARSLYSALFHWIIDFLNSKLKPTQYSHTL-----GILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 836 QTECVQEGVAMETACS-PGNQAGVldfffQKPSGFFSLLDEESQVIWSGEPNLPRKLQGLLESSNTnavyspvkdgngnv 914
Cdd:cd14905 376 QREYQTERIPWMTPISfKDNEESV-----EMMEKIINLLDQESKNINSSDQIFLEKLQNFLSRHHL-------------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 915 aFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKtseNVVISHLFQS----KLSQTGSLISSYPSFKFGGHK 990
Cdd:cd14905 437 -FGKKPNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHK---NSITKYLFSRdgvfNINATVAELNQMFDAKNTAKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 991 STLLSKRTASSMVGVNKNYLELSKLLKKKGTSTflQRLERGEPATAASQLTKSLADITAKLQRGSPHFILCIKPNTSQLP 1070
Cdd:cd14905 513 SPLSIVKVLLSCGSNNPNNVNNPNNNSGGGGGG--GNSGGGSGSGGSTYTTYSSTNKAINNSNCDFHFIRCIKPNSKKTH 590
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 568953283 1071 GVFDHFYVSAQLQYLGVLGLVRLFRSGYPVRPSFEDFLSRY 1111
Cdd:cd14905 591 LTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRF 631
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
445-1153 |
4.78e-54 |
|
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: 201.78 E-value: 4.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 445 RFGNDQIHTFIGDIFLLVNPFKelpIYSTMVSQMYLSPTGQrspsLPPHLFSCAERAFHRLFQERKPQNIILSGERGSGK 524
Cdd:cd14937 10 RYKKNYIYTIAEPMLISINPYQ---VIDVDINEYKNKNTNE----LPPHVYSYAKDAMTDFINTKTNQSIIISGESGSGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 525 TQASKQIMKYLTSRASS----SCTMFDSRlrhaiYIVEAFGHAKTTLNNVSSCLIQYWELQCcQRRKHITGARISTYMLE 600
Cdd:cd14937 83 TEASKLVIKYYLSGVKEdneiSNTLWDSN-----FILEAFGNAKTLKNNNSSRYGKYIKIEL-DEYQNIVSSSIEIFLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 601 KSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFCAHRYVSQgmrEDVSTAEHSLNKErLAALKHALNVIGFSTLEv 680
Cdd:cd14937 157 NIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVN---KNVVIPEIDDAKD-FGNLMISFDKMNMHDMK- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 681 ENLFVILSAILHIGDIQFTALTEADSAFVSDL-----QLLEQVAGMLQVSTDELASALTTDIQYFKGDVIIRRHTIQMAA 755
Cdd:cd14937 232 DDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELdknnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 756 FYRDLLAKSLYSRLFGFLINTVNCCLQNQDEYKSLqtldIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQE 835
Cdd:cd14937 312 SICKSISKDLYNKIFSYITKRINNFLNNNKELNNY----IGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 836 QTECVQEGVAMETACSPGNQAgVLDFFFQKPSgFFSLLDEESQViwsgepnlPRKLQGLLESSNTNAvYSpvKDGNGNVA 915
Cdd:cd14937 388 TELYKAEDILIESVKYTTNES-IIDLLRGKTS-IISILEDSCLG--------PVKNDESIVSVYTNK-FS--KHEKYAST 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 916 FKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQNLLFVMKTSENVVISHLFQSkLSQTGSLissypsfkfgGHKSTLls 995
Cdd:cd14937 455 KKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-VEVSESL----------GRKNLI-- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 996 krtassmvgvnknylelskllkkkgtsTFlqrlergepataasQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDH 1075
Cdd:cd14937 522 ---------------------------TF--------------KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQ 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1076 FYVSAQLQYLGV---LGLVRLFRSGYpvrpSFEDFLSRYEPLASVLLGETKGQAAEERCRLVLQRCKLQGWQIGVHKVFL 1152
Cdd:cd14937 561 KKVFPQLFSLSIietLNISFFFQYKY----TFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQNTVDPDLYKVGKTMVFL 636
|
.
gi 568953283 1153 K 1153
Cdd:cd14937 637 K 637
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
81-336 |
3.01e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.98 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 81 GLADMIQDAVIHHHDKEVLQLLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDN 160
Cdd:COG0666 53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 161 PDIVLLLILAGANVFLQDVNGNIPLDYAVEGtessaillayldekgvdlsslRQIKLqrplsmltdVRHFLSSGGDVNEK 240
Cdd:COG0666 133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAAN---------------------GNLEI---------VKLLLEAGADVNAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 241 NDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASE 320
Cdd:COG0666 183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
|
250
....*....|....*.
gi 568953283 321 SIEEMLLKAEIAWEEK 336
Cdd:COG0666 263 GAALIVKLLLLALLLL 278
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
82-358 |
5.74e-44 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 162.43 E-value: 5.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 82 LADMIQDAVIHHHDKEVLQLLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNP 161
Cdd:COG0666 21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 162 DIVLLLILAGANVFLQDVNGNIPLDYAVEGtessaillayldekgvdlsslRQIKLqrplsmltdVRHFLSSGGDVNEKN 241
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLAAYN---------------------GNLEI---------VKLLLEAGADVNAQD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 242 DDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASE- 320
Cdd:COG0666 151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENg 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568953283 321 --SIEEMLLKAEIAWEEKMKESPSAPSLAQEELYEILHDL 358
Cdd:COG0666 231 nlEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
437-1152 |
1.50e-33 |
|
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: 140.36 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 437 SLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTMVSQMYLSPTGQRSPSLppHLFSCAERAFHRLFQERKPQNIIL 516
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEDLSL--NEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 517 SGERGSGKTQASKQIMKYLTSRASSSCTM-----------------------FDSRLRHAIYIVEAFGHAKTTLNNVSSC 573
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKGSRRLptnlndqeednihneentdyqfnMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 574 LIQYWELQCcqRRKHITGARISTYMLEKSRVVAQPPGQGTFLIFSWLMDGLSSEEKCGLHLNNFcahRYVSQgMREDVST 653
Cdd:cd14938 160 FSKFCTIHI--ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNI---ENYSM-LNNEKGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 654 AEHSLNKERLAALKHALNVIGFSTLEVENLFVILSAILHIGDIQFT---------------ALTEADSAFVSDLQLLEQV 718
Cdd:cd14938 234 EKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVkafrkksllmgknqcGQNINYETILSELENSEDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 719 AGMLQVSTDELASAL-----TTDIQYFKGD------VIIRRHT---IQ--MAAFyrdllAKSLYSRLFGFLINTVNC-CL 781
Cdd:cd14938 314 GLDENVKNLLLACKLlsfdiETFVKYFTTNyifndsILIKVHNetkIQkkLENF-----IKTCYEELFNWIIYKINEkCT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 782 QNQDEykSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDF 861
Cdd:cd14938 389 QLQNI--NINTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 862 FFQKPSG-FFSLLDEESQVIWSGEPNLprkLQGLLESSNTNAVYSPVKDGNGNvafkgqGAAFTVMHYAGRVMYEMGGAV 940
Cdd:cd14938 467 LVGPTEGsLFSLLENVSTKTIFDKSNL---HSSIIRKFSRNSKYIKKDDITGN------KKTFVITHSCGDIIYNAENFV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 941 ERNKDSLSQNLLFVMKTSENVVISHLFQS-KLSQTGSLISSypSFKFGGHKSTLLSKRTASSmvgvnKNylelskllkkk 1019
Cdd:cd14938 538 EKNIDILTNRFIDMVKQSENEYMRQFCMFyNYDNSGNIVEE--KRRYSIQSALKLFKRRYDT-----KN----------- 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1020 gtstflqrlergepATAASQLTKSLADITAKLQRGSPHFILCIKPNTS--QLPgVFDHFYVSAQLQYLGVLGLVRLFRSG 1097
Cdd:cd14938 600 --------------QMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESkrELC-SFDANIVLRQVRNFSIVEASQLKVGY 664
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 568953283 1098 YPVRPSFEDFLSryeplasvlLGETKGQAAEERCRLVLQRCKL--QGWQIGVHKVFL 1152
Cdd:cd14938 665 YPHKFTLNEFLS---------IFDIKNEDLKEKVEALIKSYQIsnYEWMIGNNMIFL 712
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
92-313 |
3.53e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 108.57 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 92 HHHDKEVLQ-LLKEGADPHTLVSSGGSLLHLCARYDNVF-IAEVLIDRGVNVNHQDEDFWTPMHIACA--CDNPDIVLLL 167
Cdd:PHA03095 59 SEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 168 ILAGANVFLQDVNGNIPLDYAVEGTESSAILLAYLDEKGVDLS-------SLRQIKLQRPLSMLTDVRHFLSSGGDVNEK 240
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVYavddrfrSLLHHHLQSFKPRARIVRELIRAGCDPAAT 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568953283 241 NDDGVTLLH-MACASGYKEVVLL-LLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKP 313
Cdd:PHA03095 219 DMLGNTPLHsMATGSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
101-302 |
1.54e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.82 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 101 LLKEGADPHTLVSSGGSLLHLCARY-----DNVFIAEVLIDRGVNVNHQDEDFWTPMHIA-CACDN-PDIVLLLILAGAN 173
Cdd:PHA03100 54 LLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKSNsYSIVEYLLDNGAN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 174 VFLQDVNGNIPLDYAVEGTESSAILLAYLDEKGVDLSSLRQIKLqrplsmltdvrhFLSSGGDVNEKNDDGVTLLHMACA 253
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAKNRVNY------------LLSYGVPINIKDVYGFTPLHYAVY 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568953283 254 SGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQAN 302
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
119-326 |
3.81e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 95.50 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 119 LHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACAC-----DNPDIVLLLILAGANVFLQDVNGNIPLDYAVEGTE 193
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 194 SSAILLAYLdekgvdlsslrqiklqrplsmltdvrhfLSSGGDVNEKNDDGVTLLHMACASGY--KEVVLLLLEHGGDLN 271
Cdd:PHA03100 119 NSYSIVEYL----------------------------LDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDIN 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953283 272 G----------------TDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASESIEEML 326
Cdd:PHA03100 171 AknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
84-301 |
3.74e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 90.89 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 84 DMIQDAVIHHHDKE------VLQLLKEGADPHTLVSSGGSLLHLCAR--YDNVFIaEVLIDRGVNVNHQDEDFWTPMHIA 155
Cdd:PHA02876 270 DDCKNTPLHHASQApslsrlVPKLLERGADVNAKNIKGETPLYLMAKngYDTENI-RTLIMLGADVNAADRLYITPLHQA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 156 CACD-NPDIVLLLILAGANVFLQDVNGNIPLDYAveGTESSAILLAYLDEKGVDLSSLRQiKLQRPLSM-------LTDV 227
Cdd:PHA02876 349 STLDrNKDIVITLLELGANVNARDYCDKTPIHYA--AVRNNVVIINTLLDYGADIEALSQ-KIGTALHFalcgtnpYMSV 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568953283 228 RHFLSSGGDVNEKNDDGVTLLHMACASGYK-EVVLLLLEHGGDLNGTDDRYWTPLHLAAKYgqTTLVKLLLAHQA 301
Cdd:PHA02876 426 KTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGA 498
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
438-1081 |
1.25e-17 |
|
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: 89.80 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 438 LLYEIQKRFGNDQIHTFIGD-IFLLVNPFKEL------PIYSTMVSQMYlSPTGQRSPSLPPHLFSCAERAFHRLF---- 506
Cdd:cd14894 3 LVDALTSRFDDDRIYTYINHhTMAVMNPYRLLqtarftSIYDEQVVLTY-ADTANAETVLAPHPFAIAKQSLVRLFfdne 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 507 ---------------QERKPQNIILSGERGSGKTQASKQIMKYL------------------------------TSRASS 541
Cdd:cd14894 82 htmplpstissnrsmTEGRGQSLFLCGESGSGKTELAKDLLKYLvlvaqpalskgseetckvsgstrqpkiklfTSSTKS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 542 SCTM------------------------------------------------------FDSRLRH--------------- 552
Cdd:cd14894 162 TIQMrteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgFYEKLEHledeeqlrmyfknph 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 553 ----------AIYIVEAFGHAKTTLNNVSSCL-----------IQYWELQCCqrrkhitGARISTYMLEKSRVVAQ---P 608
Cdd:cd14894 242 aakklsivldSNIVLEAFGHATTSMNLNSSRFgkmttlqvafgLHPWEFQIC-------GCHISPFLLEKSRVTSErgrE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 609 PGQGTFLIFSWLMDGLSSeekcglhLNNFCAHRYVSQGMRED---------VSTAEHSL------------NKERLAALK 667
Cdd:cd14894 315 SGDQNELNFHILYAMVAG-------VNAFPFMRLLAKELHLDgidcsaltyLGRSDHKLagfvskedtwkkDVERWQQVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 668 HALNVIGFSTLEVENLFVILSAILHIGDIQF-------------TALTEADSAFVSDLQL--LEQVAGMLQVSTDELASA 732
Cdd:cd14894 388 DGLDELNVSPDEQKTIFKVLSAVLWLGNIELdyrevsgklvmssTGALNAPQKVVELLELgsVEKLERMLMTKSVSLQST 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 733 LTT-DIQYFKGDViirRHTiqmaafyRDLLAKSLYSRLFGFLINTVNCCLQ--------NQDEYKSLQTLD-----IGIL 798
Cdd:cd14894 468 SETfEVTLEKGQV---NHV-------RDTLARLLYQLAFNYVVFVMNEATKmsalstdgNKHQMDSNASAPeavslLKIV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 799 DIFGFEEFQKNEFEQLCVNltnekmhhYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLdFFFQKPSGFFSLLDEESQ 878
Cdd:cd14894 538 DVFGFEDLTHNSLDQLCIN--------YLSEKLYAREEQVIAVAYSSRPHLTARDSEKDVL-FIYEHPLGVFASLEELTI 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 879 VIWSGEPNLPRK-------LQGLLESSNTNAVYSP--VKDGNGNVAFKGQGAAFTVMHYAGRVMYEMGGAVERNKDSLSQ 949
Cdd:cd14894 609 LHQSENMNAQQEekrnklfVRNIYDRNSSRLPEPPrvLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYA 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 950 NLLFVMKTSENvviSHlFQSKLSQTGSLissypsfkfgghkstLLSKRTASSMVGvnknylelSKLLKKKGTSTFLqrle 1029
Cdd:cd14894 689 NLLVGLKTSNS---SH-FCRMLNESSQL---------------GWSPNTNRSMLG--------SAESRLSGTKSFV---- 737
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 568953283 1030 rgepataaSQLTKSLADITAKLQRGSPHFILCIKPNTSQLPGVFDHFYVSAQ 1081
Cdd:cd14894 738 --------GQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQ 781
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
462-572 |
1.26e-17 |
|
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: 82.39 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 462 VNPFKELPIY-STMVSQMYlspTGQRSPSLPPHLFSCAERAFHRLFQERKPQNIILSGERGSGKTQASKQIMKYLTSRAS 540
Cdd:cd01363 5 VNPFKELPIYrDSKIIVFY---RGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAF 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568953283 541 SSCTMFDS---------------RLRHAIYIVEAFGHAKTTLNNVSS 572
Cdd:cd01363 82 NGINKGETegwvylteitvtledQILQANPILEAFGNAKTTRNENSS 128
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
227-307 |
1.76e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 227 VRHFLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHgGDLNGTDDRyWTPLHLAAKYGQTTLVKLLLAHQANPHLV 306
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90
|
.
gi 568953283 307 N 307
Cdd:pfam12796 91 D 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
101-302 |
8.36e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 80.11 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 101 LLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDedfwtpMHIACACDNPDI--VLLLILAGANVFLQD 178
Cdd:PHA02876 197 LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND------LSLLKAIRNEDLetSLLLYDAGFSVNSID 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 179 VNGNIPLDYAVEgTESSAILLAYLDEKGVDLSSlRQIKLQRPLSMLT-------DVRHFLSSGGDVNEKNDDGVTLLHMA 251
Cdd:PHA02876 271 DCKNTPLHHASQ-APSLSRLVPKLLERGADVNA-KNIKGETPLYLMAkngydteNIRTLIMLGADVNAADRLYITPLHQA 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568953283 252 CA-SGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQAN 302
Cdd:PHA02876 349 STlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
89-178 |
8.88e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.30 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 89 AVIHHHDKEVLQLLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRgVNVNHQDEDfWTPMHIACACDNPDIVLLLI 168
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLL 81
|
90
....*....|
gi 568953283 169 LAGANVFLQD 178
Cdd:pfam12796 82 EKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
107-327 |
3.35e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.37 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 107 DPHTLVSSGGSLLHLCARYDNVFIAEV--LIDRGVNVNHQDEDFWTPMH--IACACDN-PDIVLLLILAGANVFLQDVNG 181
Cdd:PHA03095 4 DESVDIIMEAALYDYLLNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 182 NIPLDYavegtessaillaYLDEKgvdlSSLRQIKLqrplsmltdvrhFLSSGGDVNEKNDDGVTLLHmACASGY---KE 258
Cdd:PHA03095 84 FTPLHL-------------YLYNA----TTLDVIKL------------LIKAGADVNAKDKVGRTPLH-VYLSGFninPK 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568953283 259 VVLLLLEHGGDLNGTDdrywtplhlaaKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASESIEEMLL 327
Cdd:PHA03095 134 VIRLLLRKGADVNALD-----------LYGMTPLAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLL 191
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
248-331 |
5.03e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.37 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 248 LHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAH-QANphlVNCNGEKPSDIAASESIEEM- 325
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHaDVN---LKDNGRTALHYAARSGHLEIv 77
|
....*...
gi 568953283 326 --LLKAEI 331
Cdd:pfam12796 78 klLLEKGA 85
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
124-309 |
1.27e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.39 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 124 RYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVFLqdvngnIPLDyAVEGTESSAILlayld 203
Cdd:PHA02874 44 RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIP-CIEKDMIKTIL----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 204 EKGVDLSsLRQIKLQRPLSM------LTDVRHFLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRY 277
Cdd:PHA02874 112 DCGIDVN-IKDAELKTFLHYaikkgdLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
|
170 180 190
....*....|....*....|....*....|..
gi 568953283 278 WTPLHLAAKYGQTTLVKLLLAHQANPhLVNCN 309
Cdd:PHA02874 191 ESPLHNAAEYGDYACIKLLIDHGNHI-MNKCK 221
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
119-274 |
6.09e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.29 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 119 LHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLIlaganvflqdvngnipldyavegtessail 198
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------------------------------ 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568953283 199 layldekgvdlsslrqiklqrplsmltdvrhflsSGGDVNEKnDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTD 274
Cdd:pfam12796 51 ----------------------------------EHADVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
130-313 |
7.78e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 73.07 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 130 IAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVflQDVNGNIPLDYAVEGTESSAILLAYLDEKGVDL 209
Cdd:PHA02874 17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADI--NHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 210 SSLrqiklqrPLSMLTD--VRHFLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKY 287
Cdd:PHA02874 95 SIL-------PIPCIEKdmIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167
|
170 180
....*....|....*....|....*.
gi 568953283 288 GQTTLVKLLLAHQANPHLVNCNGEKP 313
Cdd:PHA02874 168 NFFDIIKLLLEKGAYANVKDNNGESP 193
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
101-357 |
1.48e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.92 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 101 LLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVFLQDVN 180
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 181 GNIPLDYAVEgtessaillaYLDEKgvdlsslrqiklqrplsmltDVRHFLSSGGDVNEKNDDGVTLLHMACAsgYKEVV 260
Cdd:PHA02874 190 GESPLHNAAE----------YGDYA--------------------CIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 261 LLLLEHGGDLNGTDDRYWTPLHLAAKYG-QTTLVKLLLAHQANPHLVNCNGEKPSDIAASESIEEMLLKAEIAWEEKMKE 339
Cdd:PHA02874 238 IELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKE 317
|
250
....*....|....*...
gi 568953283 340 SPSAPSLAQEELYEILHD 357
Cdd:PHA02874 318 ADKLKDSDFLEHIEIKDN 335
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
126-302 |
3.04e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.02 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 126 DNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVFLQDVNGNIPLDYAVEGTESSAIlLAYLDEK 205
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTI-KAIIDNR 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 206 G----VDLSSLRQIK-------------------------------LQRP-LSMLtdVRHFLSSGGDVNEKNDDGVTLLH 249
Cdd:PHA02876 235 SninkNDLSLLKAIRnedletslllydagfsvnsiddckntplhhaSQAPsLSRL--VPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568953283 250 MACASGY-KEVVLLLLEHGGDLNGTDDRYWTPLHLAA---KYGQTTLVKLLLAHQAN 302
Cdd:PHA02876 313 LMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVITLLELGANVN 369
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
119-328 |
2.78e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.37 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 119 LHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIV--LLLILAGANVFLQDVNGNIPLDYA-VEGTESs 195
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMkeMIRSINKCSVFYTLVAIKDAFNNRnVEIFKI- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 196 aILLAYLD-EKGVDLSSLRQIKLQRPLSMLTdVRHFLSSGGDVNEKNDD-GVTLLHMACASGYKEVVLLLLEHGGDLNGT 273
Cdd:PHA02878 120 -ILTNRYKnIQTIDLVYIDKKSKDDIIEAEI-TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568953283 274 DDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASESIEEMLLK 328
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILK 252
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
227-324 |
3.93e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 68.39 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 227 VRHFLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLV 306
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
|
90
....*....|....*...
gi 568953283 307 NCNGeKPSDIAASESIEE 324
Cdd:PTZ00322 178 GANA-KPDSFTGKPPSLE 194
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
244-297 |
5.67e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.21 E-value: 5.67e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568953283 244 GVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLL 297
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
95-299 |
2.21e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 65.29 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 95 DKEVLQLLKE-GADPHTLV-SSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGA 172
Cdd:PHA02878 146 EAEITKLLLSyGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 173 NVFLQDVNGNIPLDYAVegtessaillayldekgvdlSSLRQIKLqrpLSMLtdvrhfLSSGGDVNEKND-DGVTLLHMA 251
Cdd:PHA02878 226 STDARDKCGNTPLHISV--------------------GYCKDYDI---LKLL------LEHGVDVNAKSYiLGLTALHSS 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568953283 252 CASgyKEVVLLLLEHGGDLNGTDDRYWTPLHLAAK-YGQTTLVKLLLAH 299
Cdd:PHA02878 277 IKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILISN 323
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
101-310 |
9.26e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.09 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 101 LLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACacDNPDIVLLLILAGANVFLQDV- 179
Cdd:PHA02875 21 LLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAV--EEGDVKAVEELLDLGKFADDVf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 180 --NGNIPLDYAvegtessaillayldekgvdlSSLRQIKLQRPLsmltdvrhfLSSGGDVNEKNDDGVTLLHMACASGYK 257
Cdd:PHA02875 99 ykDGMTPLHLA---------------------TILKKLDIMKLL---------IARGADPDIPNTDKFSPLHLAVMMGDI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568953283 258 EVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNG 310
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
134-188 |
1.74e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 55.05 E-value: 1.74e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568953283 134 LIDRG-VNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVFLQDVNGNIPLDYA 188
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
115-168 |
4.76e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 4.76e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568953283 115 GGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLI 168
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
85-283 |
7.47e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.04 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 85 MIQDAVIHH---HDKEVLQLLKEGADPHTLVSSGGSLLHLCARYDNVFIAEvLIDRGVNVNHQDEDFWTPMHIACACDNP 161
Cdd:PLN03192 493 ILKNFLQHHkelHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEE-LLKAKLDPDIGDSKGRTPLHIAASKGYE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 162 DIVLLLILAGANVFLQDVNGNIPLDYAVEGTESSAILLAYL------DEKGVDLssLRQIKLQRPLSMLtdvRHFLSSGG 235
Cdd:PLN03192 572 DCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfasisdPHAAGDL--LCTAAKRNDLTAM---KELLKQGL 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568953283 236 DVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLN--GTDDRYwTPLHL 283
Cdd:PLN03192 647 NVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkaNTDDDF-SPTEL 695
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
236-284 |
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
....*....|....*....|....*....|....*....|....*....
gi 568953283 236 DVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLA 284
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
263-317 |
2.78e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.96 E-value: 2.78e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568953283 263 LLEHGG-DLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIA 317
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
152-327 |
4.95e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.69 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 152 MHIACACD-----NPDIVLLLILAGANVFLQDVNGNIPLDYAVEGTESSAILL-----AYLDEKGVDLSSLRQIKLQR-- 219
Cdd:PHA02875 1 MDQVALCDailfgELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLlmkhgAIPDVKYPDIESELHDAVEEgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 220 --PLSMLTDVRHFLSsggDVNEKndDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLL 297
Cdd:PHA02875 81 vkAVEELLDLGKFAD---DVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
|
170 180 190
....*....|....*....|....*....|...
gi 568953283 298 AHQANPHLVNCNGEKPSDIAASE---SIEEMLL 327
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKgdiAICKMLL 188
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
114-313 |
3.25e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 55.69 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 114 SGGSLLH--LCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDN--PDIVLLLILAGANVFLQDVNGNIP-LDYA 188
Cdd:PHA02716 176 TGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPiMTYI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 189 VE----GTESSAILLAYLDE---KGVDLSSLRQIKLQRPLSmLTDVRHFLSSGGDVNEKNDDGVTLLHMACASGY--KEV 259
Cdd:PHA02716 256 INidniNPEITNIYIESLDGnkvKNIPMILHSYITLARNID-ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDI 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568953283 260 VLLLLEHGGDLNGTDD-------RYWTPLHLAAKYGQTT-------LVKLLLAHQANPHLVNCNGEKP 313
Cdd:PHA02716 335 IKLLHEYGNDLNEPDNigntvlhTYLSMLSVVNILDPETdndirldVIQCLISLGADITAVNCLGYTP 402
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
118-190 |
3.95e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 3.95e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568953283 118 LLHLCARYDNVFiAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVFLQDVNGNIPLDYAVE 190
Cdd:PTZ00322 86 LCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
87-183 |
4.23e-06 |
|
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: 51.32 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 87 QDAVIHHHDKEvLQLLKEGADPHTLVSSGGSLLHL-----CARYDNV---FIAEVLI--DRGVNVNHQDED--FWTPMHI 154
Cdd:pfam15439 7 LEKRRRQEEGI-KRSGEEVAGKVRDISSEGRHFRMgfmtmPASQDRLphpCAAGMSIrsQSLHSVGSGDEDgsLPSSRKQ 85
|
90 100
....*....|....*....|....*....
gi 568953283 155 ACACDNPDIVLLLILAGANVFLQDVNGNI 183
Cdd:pfam15439 86 PPPKPKRDPSTKLSMSSEAVSAGLSAGAK 114
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
245-369 |
1.84e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 245 VTLLHMAcASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASES--- 321
Cdd:PTZ00322 84 VELCQLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfre 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568953283 322 IEEMLLKAEIAWEEKMKESPSAPSLAQEELYE---ILHDLPDLSSKLSPLV 369
Cdd:PTZ00322 163 VVQLLSRHSQCHFELGANAKPDSFTGKPPSLEdspISSHHPDFSAVPQPMM 213
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
159-297 |
2.98e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 48.68 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 159 DNP--DIVLLLILAGANVFLQDVNGNIPLdyavegtesSAILLAYLDEKgvdlsslrqiklqrplSMLTDVRHFLSSGGD 236
Cdd:PHA02798 47 DSPstDIVKLFINLGANVNGLDNEYSTPL---------CTILSNIKDYK----------------HMLDIVKILIENGAD 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568953283 237 VNEKNDDGVTLLHMACASGY---KEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYG---QTTLVKLLL 297
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLL 168
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
278-307 |
4.18e-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: 4.18e-05
10 20 30
....*....|....*....|....*....|.
gi 568953283 278 WTPLHLAA-KYGQTTLVKLLLAHQANPHLVN 307
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
243-271 |
4.25e-05 |
|
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: 42.19 E-value: 4.25e-05
10 20
....*....|....*....|....*....
gi 568953283 243 DGVTLLHMACASGYKEVVLLLLEHGGDLN 271
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
243-271 |
1.11e-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: 41.09 E-value: 1.11e-04
10 20
....*....|....*....|....*....
gi 568953283 243 DGVTLLHMACASGYKEVVLLLLEHGGDLN 271
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
95-211 |
1.15e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 45.58 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 95 DKEVLQLL-KEGAD-PHTLVSSGGSLLHLCARYD---NVFIAEVLIDRGVNVNHQDEDFWTPMHI-ACACD-NPDIVLLL 167
Cdd:PHA02859 65 NVEILKFLiENGADvNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLL 144
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568953283 168 ILAGANVFLQDVNGNIPLdYAVEGTESSAILLAYLDEKGVDLSS 211
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNIL-YSYILFHSDKKIFDFLTSLGIDINE 187
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
277-326 |
1.83e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 1.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568953283 277 YWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASESIEEML 326
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
101-325 |
2.75e-04 |
|
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: 45.77 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 101 LLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLID---RGVNVNHQDEDFW--TPMHIACACDNPDIVLLLILAGANVF 175
Cdd:cd22192 37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDLYQgeTALHIAVVNQNLNLVRELIARGADVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 176 LQDVNGNipldYAVEGTESsailLAYLDEkgvdlsslrqiklqrplsmltdvrHFLSsggdvneknddgvtllHMACAsG 255
Cdd:cd22192 117 SPRATGT----FFRPGPKN----LIYYGE------------------------HPLS----------------FAACV-G 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 256 YKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVK----LLLAHQAN------PHLVNCNGEKPSDIAASESIEEM 325
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEddlqplDLVPNNQGLTPFKLAAKEGNIVM 227
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
276-304 |
3.55e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.55 E-value: 3.55e-04
10 20
....*....|....*....|....*....
gi 568953283 276 RYWTPLHLAAKYGQTTLVKLLLAHQANPH 304
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
262-310 |
3.66e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.44 E-value: 3.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568953283 262 LLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNG 310
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDD 211
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
278-305 |
4.10e-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: 39.11 E-value: 4.10e-04
10 20
....*....|....*....|....*...
gi 568953283 278 WTPLHLAAKYGQTTLVKLLLAHQANPHL 305
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
227-264 |
4.21e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 4.21e-04
10 20 30
....*....|....*....|....*....|....*...
gi 568953283 227 VRHFLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLL 264
Cdd:pfam13637 17 LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
243-275 |
4.42e-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: 39.19 E-value: 4.42e-04
10 20 30
....*....|....*....|....*....|....
gi 568953283 243 DGVTLLHMACAS-GYKEVVLLLLEHGGDLNGTDD 275
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
81-271 |
7.30e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.21 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 81 GLADMIQDAVIHHHDKEVLQLLKEGADPHTLV-SSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACD 159
Cdd:PHA02875 67 DIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 160 NPDIVLLLILAGANVFLQDVNGNIPLDYAVegtessaillayldekgvdlsSLRQIKLQRPLsmltdvrhfLSSGGDVN- 238
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAM---------------------AKGDIAICKML---------LDSGANIDy 196
|
170 180 190
....*....|....*....|....*....|....
gi 568953283 239 -EKNDDgVTLLHMACASGYKEVVLLLLEHGGDLN 271
Cdd:PHA02875 197 fGKNGC-VAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
236-325 |
1.27e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.50 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 236 DVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLA--AKYGQT---TLVKLLLAHQANPHLVNCNG 310
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLsnIKYNLTdvkEIVKLLLEYGANVNAPDNNG 106
|
90
....*....|....*
gi 568953283 311 EKPSDIAASESIEEM 325
Cdd:PHA03100 107 ITPLLYAISKKSNSY 121
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
149-178 |
1.51e-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: 37.65 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|.
gi 568953283 149 WTPMHIACA-CDNPDIVLLLILAGANVFLQD 178
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
130-287 |
1.68e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 43.28 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 130 IAEVLIDRGVNVNHQDEDFWTPM-----HIACACDNPDIVLLLILAGANVFLQDVNGNIPLdYAV--EGTESSAILLAYL 202
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLlsNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 203 DEKGVDLSSLrqiklqrplsmltdvrhflssggdvnekNDDGVTLLHMACASGYK---EVVLLLLEHGGDLNGTDDRY-W 278
Cdd:PHA02798 132 IENGADTTLL----------------------------DKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNKEkY 183
|
....*....
gi 568953283 279 TPLHLAAKY 287
Cdd:PHA02798 184 DTLHCYFKY 192
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
149-174 |
2.00e-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: 37.24 E-value: 2.00e-03
10 20
....*....|....*....|....*.
gi 568953283 149 WTPMHIACACDNPDIVLLLILAGANV 174
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
147-176 |
2.20e-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: 37.18 E-value: 2.20e-03
10 20 30
....*....|....*....|....*....|
gi 568953283 147 DFWTPMHIACACDNPDIVLLLILAGANVFL 176
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
231-318 |
3.08e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 42.55 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 231 LSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGTDDRYWTPLHLAAKYGQTTLVKLL--LAHQANPHL--- 305
Cdd:PLN03192 545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagd 624
|
90
....*....|...
gi 568953283 306 VNCNGEKPSDIAA 318
Cdd:PLN03192 625 LLCTAAKRNDLTA 637
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
115-183 |
3.62e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.96 E-value: 3.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568953283 115 GGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLILAGANVflQDVNGNI 183
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI--KTIIETL 258
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
188-282 |
3.72e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 188 AVEGTESSAILLAYLDEKGVDLSSLRQIklqrplsmltdvrhfLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHG 267
Cdd:PHA02946 31 AIEPSGNYHILHAYCGIKGLDERFVEEL---------------LHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHG 95
|
90
....*....|....*
gi 568953283 268 GDLNGTDDRYWTPLH 282
Cdd:PHA02946 96 ADPNACDKQHKTPLY 110
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
244-332 |
4.08e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 42.10 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 244 GVTLLHMACASGYKEVVLLLLEHGGDLN------------GTDDRYW--TPLHLAAKYGQTTLVKLLLahqANPHlvncn 309
Cdd:cd22196 94 GQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkkkGGPGFYFgeLPLSLAACTNQLDIVKFLL---ENPH----- 165
|
90 100
....*....|....*....|....*
gi 568953283 310 geKPSDIAASESIEEMLLKA--EIA 332
Cdd:cd22196 166 --SPADISARDSMGNTVLHAlvEVA 188
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
115-143 |
5.08e-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: 5.08e-03
10 20
....*....|....*....|....*....
gi 568953283 115 GGSLLHLCARYDNVFIAEVLIDRGVNVNH 143
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
149-189 |
6.20e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.48 E-value: 6.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568953283 149 WTPMHIACACDNPDIVLLLILAGANVFLQDVNGNIPLDYAV 189
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
101-155 |
6.21e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 6.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568953283 101 LLKEG-ADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWTPMHIA 155
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
1335-1541 |
7.46e-03 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 41.10 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1335 AAKDAAGEALTRPrphSDDYSTMKKIPPRKPKRSPHTKlsgSYEEIWGPPRPSGTMGQGGRHQAPGTLSVQWARPDSVPq 1414
Cdd:PHA03321 486 AAPPPEPAAAPSP---ATYYTRMGGGPPRLPPRNRATE---TLRPDWGPPAAAPPEQMEDPYLEPDDDRFDRRDGAAAA- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953283 1415 ctpqlpLHLPLPQGDYDDDaEPVYIemvgnaaraggsetDSPDQGESVYEEMKYI--------LPEEGCGLGMLTFLPAS 1486
Cdd:PHA03321 559 ------ATSHPREAPAPDD-DPIYE--------------GVSDSEEPVYEEIPTPrvyqnplpRPMEGAGEPPDLDAPTS 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568953283 1487 PPLFLETRKAIILEAAEGNCQPSKDTcdiPPPFPNLLPHRPPLLVFPPTPVTRSP 1541
Cdd:PHA03321 618 PWVEEENPIYGWGDSPLFSPPPAARF---PPPDPALSPEPPALPAHRPRPGALAP 669
|
|
| |
