|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
320-1038 |
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: 1361.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGARIY 479
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKHLTGARIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 480 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLAVLKQALNVVGF 559
Cdd:cd14878 161 TYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSLNREKLAVLKQALNVVGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 560 SNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 639
Cdd:cd14878 241 SSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 640 FFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHE 719
Cdd:cd14878 321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 720 QVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGNGNVA 799
Cdd:cd14878 401 QTECVQEGVTMETAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYSPMKDGNGNVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 800 LKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLsqtgslvsaypsfkfrghksalls 879
Cdd:cd14878 481 LKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL------------------------ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 880 kkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFD 959
Cdd:cd14878 537 ---------------------------------------VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFD 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884521 960 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQGWQMGVRKVFLK 1038
Cdd:cd14878 578 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
321-1038 |
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: 670.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRS--ADLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAAS-------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQL 473
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSgssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF-DPTGRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 474 TGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-TMQDDVSTGERSLNREKLAVLKQ 552
Cdd:cd00124 159 VGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDyLNSSGCDRIDGVDDAEEFQELLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 553 ALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 630
Cdd:cd00124 239 ALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 631 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmqTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 710
Cdd:cd00124 319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAES--TSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 711 INEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAvysp 790
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDFPDNQD-CLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF---- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 791 lkdgngnVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqsklsqtgslvsaypsfkf 870
Cdd:cd00124 472 -------SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG---------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 871 rghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDIIGKLQKCTPHFIHCIRPN 950
Cdd:cd00124 517 ----------------------------------------------------SQFRSQLDALMDTLNSTQPHFVRCIKPN 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 951 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFL-REKKEHLAAERCRLVLQQCKLQGWQ 1029
Cdd:cd00124 545 DEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATeKASDSKKAAVLALLLLLKLDSSGYQ 624
|
....*....
gi 1622884521 1030 MGVRKVFLK 1038
Cdd:cd00124 625 LGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
309-1048 |
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: 613.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 309 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 388
Cdd:smart00242 9 EDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKY---RGKSRGELPPHVFAIADNAYRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 389 LFQEQRPQCFILSGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVM----CILEAFGHAKTTLNDLSSCFIKYFEL 464
Cdd:smart00242 86 MLNDKENQSIIISGESGAGKTENTKKIMQYLA--SVSGSNTEVGSVEDQIlesnPILEAFGNAKTLRNNNSSRFGKFIEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 465 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ------TMQDDVstg 538
Cdd:smart00242 164 HFDA-KGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQggcltvDGIDDA--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 539 erslnrEKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSA-FVSDLQLLEQVAGMLQVSTDELASAL 617
Cdd:smart00242 240 ------EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 618 TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQ 697
Cdd:smart00242 314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYF----IGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 698 LCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkkLQS 777
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDW-TFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTF---LEK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 778 LLESSNTNAVYSPLKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQ 857
Cdd:smart00242 466 LNQHHKKHPHFSKPK--------KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 858 TGslvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQ 937
Cdd:smart00242 538 AG-------------------SKKR-----------------------------------FQTVGSQFKEQLNELMDTLN 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 938 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCR 1017
Cdd:smart00242 564 STNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTW-PPWGGDAKKACE 642
|
730 740 750
....*....|....*....|....*....|...
gi 1622884521 1018 LVLQQCKL--QGWQMGVRKVFLKYWHADQLNDL 1048
Cdd:smart00242 643 ALLQSLGLdeDEYQLGKTKVFLRPGQLAELEEL 675
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
321-1038 |
7.06e-177 |
|
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: 548.03 E-value: 7.06e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLY---RGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCeRKQQLTGARIYT 480
Cdd:cd01379 79 SGESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT-STGAVTGARISE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEK-HGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLAVLKQALNVVGF 559
Cdd:cd01379 158 YLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 560 SNLEVENLFVILAAILHLGDIRFTALTEG----NSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 635
Cdd:cd01379 238 TKEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 636 QIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 715
Cdd:cd01379 318 EEATDARDAMAKALYGRLFSWIVNRINS-LLKPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 716 FLHEQVECVQEGVTMET-AYSpgNQNGVLDFFFQKPSGFLTLLDEESQmiwsmesnFPKKL-QSLLESSNTNavyspLKD 793
Cdd:cd01379 397 FAWEQQEYLNEGIDVDLiEYE--DNRPLLDMFLQKPMGLLALLDEESR--------FPKATdQTLVEKFHNN-----IKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 794 GNgNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrgh 873
Cdd:cd01379 462 KY-YWRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 874 ksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSK 953
Cdd:cd01379 517 ----------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSR 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 954 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtFLREKKEHLAAERCRLVLQQCKLQGWQMGVR 1033
Cdd:cd01379 551 QAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA--FKWNEEVVANRENCRLILERLKLDNWALGKT 628
|
....*
gi 1622884521 1034 KVFLK 1038
Cdd:cd01379 629 KVFLK 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
309-1038 |
1.35e-166 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 522.23 E-value: 1.35e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 309 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 388
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAY---RGKRRGELPPHIFAIADEAYRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 389 LFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC----ILEAFGHAKTTLNDLSSCFIKYFEL 464
Cdd:pfam00063 79 MLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILqsnpILEAFGNAKTVRNNNSSRFGKYIEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 465 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSlnr 544
Cdd:pfam00063 159 QF-DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 545 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 624
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 625 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTN 704
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSL---DVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 705 EKMHHYINEVLFLHEQVECVQEGVTmetaYSP---GNQNGVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKK-----LQ 776
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIE----WTFidfGDNQPCIDLIEKKPLGILSLLDE--------ECLFPKAtdqtfLD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 777 SLLESSNTNAVY-SPLKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkl 855
Cdd:pfam00063 460 KLYSTFSKHPHFqKPRLQGE---------THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD-- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 856 sqtGSLVSAYPSFKFRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGK 935
Cdd:pfam00063 529 ---YETAESAAANESGKSTPKRTKKKR-----------------------------------FITVGSQFKESLGELMKT 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 936 LQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHlAAER 1015
Cdd:pfam00063 571 LNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGD-AKKG 649
|
730 740
....*....|....*....|....*
gi 1622884521 1016 CRLVLQQCKLQG--WQMGVRKVFLK 1038
Cdd:pfam00063 650 CEAILQSLNLDKeeYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
308-1140 |
2.10e-149 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 498.83 E-value: 2.10e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 308 NDDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFH 387
Cdd:COG5022 68 VDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY---SGKNRLELEPHVFAIAEEAYR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 388 QLFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFEL 464
Cdd:COG5022 145 NLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEKQILAtnpILEAFGNAKTVRNDNSSRFGKYIKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 465 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNR 544
Cdd:COG5022 225 EFDE-NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 545 EKLAvlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFvSDLQLLEQVAGMLQVSTDELASALTTDIQYF 624
Cdd:COG5022 304 KITL---DALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIF-SDNSVLDKACYLLGIDPSLFVKWLVKRQIKT 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 625 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTN 704
Cdd:COG5022 380 GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNF----IGVLDIYGFEIFEKNSFEQLCINYTN 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 705 EKMHHYINEVLFLHEQVECVQEGVtmetAYSP----GNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLe 780
Cdd:COG5022 456 EKLQQFFNQHMFKLEQEEYVKEGI----EWSFidyfDNQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQRL- 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 781 SSNTNAVYSPLKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsqtgs 860
Cdd:COG5022 531 NKNSNPKFKKSRFRD---------NKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE------ 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 861 lvsaypsfkfrghksallskkmtassiigENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCT 940
Cdd:COG5022 596 -----------------------------ENIE--------------------SKGRFPTLGSRFKESLNSLMSTLNSTQ 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 941 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR---EKKEHLAAERCR 1017
Cdd:COG5022 627 PHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWtgeYTWKEDTKNAVK 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1018 LVLQQCKL--QGWQMGVRKVFLKywhADQLNDLCLQ----LQRKIITCQKVIRGFLARQHLLQKISiRQQEVTS-INSFL 1090
Cdd:COG5022 707 SILEELVIdsSKYQIGNTKVFFK---AGVLAALEDMrdakLDNIATRIQRAIRGRYLRRRYLQALK-RIKKIQViQHGFR 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884521 1091 QNTE-DMGLKTYDALVIQNASDIA--RENDRLRSEMNAPYHKE---KLEVRNTQEE 1140
Cdd:COG5022 783 LRRLvDYELKWRLFIKLQPLLSLLgsRKEYRSYLACIIKLQKTikrEKKLRETEEV 838
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
321-1038 |
7.74e-149 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 472.64 E-value: 7.74e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVR--SQRPPHLFWIADQAYRRLLETGRNQCILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGARIYT 480
Cdd:cd14897 80 SGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE-NGQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL-NQTMQDDV--STGERSLNREKLAVLKQALNVV 557
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrDDNRNRPVfnDSEELEYYRQMFHDLTNIMKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 558 GFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 637
Cdd:cd14897 239 GFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 638 AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTL-DIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 716
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGpSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 717 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTnavYSPLKDGNg 796
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDD-VLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR---YVASPGNR- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 797 nvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsaypsfkfrghksa 876
Cdd:cd14897 474 --------VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 877 llskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPD 956
Cdd:cd14897 521 ---------------------------------------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 957 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtFLREKKEHLAAE-RCRLVLQQCKLQGWQMGVRKV 1035
Cdd:cd14897 556 KFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEI---CDFSNKVRSDDLgKCQKILKTAGIKGYQFGKTKV 632
|
...
gi 1622884521 1036 FLK 1038
Cdd:cd14897 633 FLK 635
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
321-1038 |
7.88e-149 |
|
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: 473.28 E-value: 7.88e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLY---RNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTcrAASS------RAMLDSRfkhvmCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLT 474
Cdd:cd01381 79 SGESGAGKTESTKLILQYLA--AISGqhswieQQILEAN-----PILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV-IE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 475 GARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqtMQDDVSTGERSLNREKLAVLKQAL 554
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYL---TQGNCLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 555 NVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 632
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNldASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 633 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 712
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDS-SRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 713 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQmiwsmesnFPKKL-QSLLESSN----TNAV 787
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEFVDNQD-VLDLIALKPMNIMSLIDEESK--------FPKGTdQTMLEKLHsthgNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 788 YSPLKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsayps 867
Cdd:cd01381 458 YLKPK--------SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 868 fkfrghksallskkmtassiigenknylelskllkkkGTSTflqrleRGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCI 947
Cdd:cd01381 520 -------------------------------------GSET------RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCI 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 948 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKE---HLAAERCRLVLQQCK 1024
Cdd:cd01381 557 KPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTdcrAATRKICCAVLGGDA 636
|
730
....*....|....
gi 1622884521 1025 LqgWQMGVRKVFLK 1038
Cdd:cd01381 637 D--YQLGKTKIFLK 648
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
322-1038 |
1.55e-146 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 467.46 E-value: 1.55e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 322 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLF----QEQRPQC 397
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKS---SLPPHIFAVADRAYQSMLgrlaRGPKNQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 398 FILSGERGSGKSEASKQIIRHLT--CRAASSramLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTG 475
Cdd:cd14889 80 IVISGESGAGKTESTKLLLRQIMelCRGNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF--RNGHVKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 476 ARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTM--QDDVSTGerslnREKLAVLKQA 553
Cdd:cd14889 155 AKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAgcKREVQYW-----KKKYDEVCNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 554 LNVVGFSNLEVENLFVILAAILHLGDIRFTaLTEGNSAFVSDLQ--LLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 631
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITFE-MDDDEALKVENDSngWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 632 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 711
Cdd:cd14889 309 HHTKQQAEDARDSIAKVAYGRVFGWIVSKINQ-LLAPKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 712 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVYSpl 791
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITYKDNKP-ILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG---NSYYG-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 792 KDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfr 871
Cdd:cd14889 462 KSRS-------KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPR------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 872 ghksallSKKMTASSiigenknylelskllkKKGTSTFLQrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNN 951
Cdd:cd14889 528 -------AKLPQAGS----------------DNFNSTRKQ--------SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNH 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 952 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEHLAAERCRLVLQQCKLQGWQMG 1031
Cdd:cd14889 577 VKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKLVGWKCG 652
|
....*..
gi 1622884521 1032 VRKVFLK 1038
Cdd:cd14889 653 KTRLFFK 659
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
326-1038 |
2.36e-141 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 452.77 E-value: 2.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 326 IQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERG 405
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESY---RGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 406 SGKSEASKQIIRHLTcrAASSRAMLD-SRFKHVM----CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 480
Cdd:cd01378 84 AGKTEASKRIMQYIA--AVSGGSESEvERVKDMLlasnPLLEAFGNAKTLRNDNSSRFGKYMEIQF-DFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStgerSLNREK-LAVLKQALNVVGF 559
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVD----GIDDAAdFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 560 SNLEVENLFVILAAILHLGDIRFTALTEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM---IIRRHTIQ 636
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEEGNAA-ISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 637 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLLS-QDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 715
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAkSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 716 FLHEQVECVQEGVTMETayspgnqngvLDFFF---------QKPSGFLTLLDEESqmiwsmesNFPKK------LQSLLE 780
Cdd:cd01378 392 LKAEQEEYVREGIEWTP----------IKYFNnkiicdlieEKPPGIFAILDDAC--------LTAGDatdqtfLQKLNQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 781 SSNTNAVYSPLKDgngnvALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgs 860
Cdd:cd01378 454 LFSNHPHFECPSG-----HFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 861 lvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQKCT 940
Cdd:cd01378 527 ------------------SKKR-----------------------------------PPTAGTKFKNSANALVETLMKKQ 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 941 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAD-TFLRekKEHLAAERCRLV 1019
Cdd:cd01378 554 PSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPkTWPA--WDGTWQGGVESI 631
|
730 740
....*....|....*....|.
gi 1622884521 1020 LQQCKLQG--WQMGVRKVFLK 1038
Cdd:cd01378 632 LKDLNIPPeeYQMGKTKIFIR 652
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
1126-1471 |
5.02e-141 |
|
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal family of eukaryotic proteins that are substrates of tyrosine kinase in the brain. When first identified, the family members were referred to as unconventional myosin XVI, or Myr 8. However, proteins have now been identified as being integrally involved in neuronal function and morphogenesis. The family is involved in both the activation of phosphoinositide 3-kinase (PI3K) and the recruitment of the downstream effector WAVE complex to the close vicinity of PI3K; it also appears to regulate the brain size and neurite outgrowth in mice.
Pssm-ID: 464717 [Multi-domain] Cd Length: 379 Bit Score: 441.52 E-value: 5.02e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1126 PYHKEKLEVRNTQEEGSKRTEDK---------SGPRHFHPSSMSVCMAVDGLG-QCLAGPSIWSPSLHSVFSMDDNSSLP 1195
Cdd:pfam15439 1 LYRKEKLEKRRRQEEGIKRSGEEvagkvrdisSEGRHFRMGFMTMPASQDRLPhPCAAGMSIRSQSLHSVGSGDEDGSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1196 SPRKQPPPKPKRDPNTRLSASYEAVSACLS-AAREAA--NEALARPRPHSDDYStmKKIPPRKPKRSPNTKLSGSYEEIS 1272
Cdd:pfam15439 81 SSRKQPPPKPKRDPSTKLSMSSEAVSAGLSaGAKETPseTEALSKPRPHSDEYS--RKIPPPKPKRSPNTQLSGSFDEIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1273 GSRPgdaRPPGAPGTAArvlTPGTPQCAlppatpPGDEDDGEPVYIEMLGHPAR-------PDSPDPGESVYEEMKCCLP 1345
Cdd:pfam15439 159 APYI---RPHGLLQRAS---SSDGPSPA------PLPDEEEEPVYIEMVGNVLRdfspttpDDDPDQSEAVYEEMKYPLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1346 DDGGPGAGSFLRASPPLL-----HGAPEDE--------AAGPPGDMCDIPPPFPNLLPHRPPLLVFPPTPVTCSPASDES 1412
Cdd:pfam15439 227 EDSGAANGPPPLASSPLLadphsPISPESDsalpssqcATPTKKDLCDIPAPFPNLLPHRPPLLVFPPAPVTCSPASDES 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884521 1413 PLTPLEVKKLPVLEtNLKYPVQSEgSSPLSPQYSKSQKGDGDRPASPGLALFNGSGRAS 1471
Cdd:pfam15439 307 PLTPLEVKKLPVLE-NVSYSKQPA-SSPLSPQESKHQREDKDRPSSPGLAVLTPSGRAR 363
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
320-1038 |
9.02e-138 |
|
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: 444.51 E-value: 9.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSsgKLcSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNR--RL-GKLPPHIFAIADVAYHAMLRKKKNQCIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGA 476
Cdd:cd01385 78 ISGESGSGKTESTNFLLHHLT--ALSQKGYGSGVEQTILGagpVLEAFGNAKTAHNNNSSRFGKFIQVNYRE-NGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 477 RIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTGERSLNREKLAVLKQALNV 556
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQS---DCYTLEGEDEKYEFERLKQAMEM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 557 VGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 634
Cdd:cd01385 232 VGFLPETQRQIFSVLSAVLHLGNIEYKKKAYHRdeSVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 635 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 714
Cdd:cd01385 312 LPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 715 LFLHEQVECVQEGVTMETAYSPGNqNGVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKKL-QSLLE------SSNTNAV 787
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEYTDN-TGCLQLISKKPTGLLCLLDE--------ESNFPGATnQTLLAkfkqqhKDNKYYE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 788 YSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgSLVSAYPS 867
Cdd:cd01385 463 KPQVME-----------PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVR-----------ELIGIDPV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 868 FKFRghkSALLS---KKMTASSIIGEN--KNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQKCTPH 942
Cdd:cd01385 521 AVFR---WAVLRaffRAMAAFREAGRRraQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPF 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 943 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQ 1022
Cdd:cd01385 598 FIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDR 677
|
730
....*....|....*.
gi 1622884521 1023 CKlqgWQMGVRKVFLK 1038
Cdd:cd01385 678 DN---YQIGKTKVFLK 690
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
321-1038 |
2.88e-137 |
|
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: 442.15 E-value: 2.88e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFsssGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYF---GKRMGALPPHIFALAEAAYTNMQEDGKNQSVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLtCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 480
Cdd:cd14883 79 SGESGAGKTETTKLILQYL-CAVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCF-DASGHIKGAIIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDG--LSAEEKHGLHLNNLCAHRYLNQtmqDDVSTGERSLNREKLAVLKQALNVVG 558
Cdd:cd14883 157 YLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQ---SGCIRIDNINDKKDFDHLRLAMNVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 559 FSNLEVENLFVILAAILHLGDIRFTALtEGNSA--FVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQ 636
Cdd:cd14883 234 IPEEMQEGIFSVLSAILHLGNLTFEDI-DGETGalTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 637 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 716
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF----IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 717 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVY-SPLKdgn 795
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFTDNQE-CLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEK---HPYYeKPDR--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 796 gnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsAYPSfkfrghks 875
Cdd:cd14883 462 -----RRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELF------------TYPD-------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 876 alLSKKMTASSIIGENKNylelskllkKKGTStflqrleRGDPvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLP 955
Cdd:cd14883 517 --LLALTGLSISLGGDTT---------SRGTS-------KGKP-TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 956 DTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLAAERCRLVLQQCKLQG--WQMGVR 1033
Cdd:cd14883 578 NVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL-DPRARSADHKETCGAVRALMGLGGLPEdeWQVGKT 656
|
....*
gi 1622884521 1034 KVFLK 1038
Cdd:cd14883 657 KVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
323-1038 |
9.32e-134 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 431.71 E-value: 9.32e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 323 LYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILS 401
Cdd:cd01384 4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQY---KGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 402 GERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVM---CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 478
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLesnPLLEAFGNAKTVRNNNSSRFGKFVEIQF-DDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 479 YTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ---DDVSTGErslnrEKLAVLKqALN 555
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCfelDGVDDAE-----EYRATRR-AMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 556 VVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSD---LQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 632
Cdd:cd01384 234 VVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 633 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 712
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL----IGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 713 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLqsllessntnavYSPLK 792
Cdd:cd01384 390 QHVFKMEQEEYTKEEIDWSYIEFVDNQD-VLDLIEKKPGGIIALLDEACMFPRSTHETFAQKL------------YQTLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 793 DGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKD---SLSQNLLfvmKTSENVVINHLFQSKLSQTGSlvsayPSFK 869
Cdd:cd01384 457 DHKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDyvvAEHQALL---NASKCPFVAGLFPPLPREGTS-----SSSK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 870 FrghksallskkmtaSSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLTDIIGKLQKCTPHFIHCIRP 949
Cdd:cd01384 529 F--------------SS----------------------------------IGSRFKQQLQELMETLNTTEPHYIRCIKP 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 950 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLreKKEHLAAERCRLVLQQCKLQGWQ 1029
Cdd:cd01384 561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL--KGSDDEKAACKKILEKAGLKGYQ 638
|
....*....
gi 1622884521 1030 MGVRKVFLK 1038
Cdd:cd01384 639 IGKTKVFLR 647
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
321-1038 |
3.52e-133 |
|
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: 430.71 E-value: 3.52e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQY---SGRALGELPPHLFAIANLAFAKMLDAKQNQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARIYT 480
Cdd:cd01387 79 SGESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF--EGGVIVGAITSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStGERSlnREKLAVLKQALNVVGFS 560
Cdd:cd01387 157 YLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIA-GKSD--ADDFRRLLAAMQVLGFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 561 NLEVENLFVILAAILHLGDIRF-----TALTEGNSaFVSDLQlLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 635
Cdd:cd01387 234 SEEQDSIFRILASVLHLGNVYFhkrqlRHGQEGVS-VGSDAE-IQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 636 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEqrsmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 715
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQ----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 716 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKKLQ-SLLESSNTNAVYSPLKDG 794
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAFADNQP-VINLISKKPVGILHILDD--------ECNFPQATDhSFLEKCHYHHALNELYSK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 795 NgnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsaypsfkfrgHK 874
Cdd:cd01387 459 P-----RMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ---------------TD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 875 SALLSKkmtassiigenknylelskllkkkGTSTFLQRLERGDpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKL 954
Cdd:cd01387 519 KAPPRL------------------------GKGRFVTMKPRTP--TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKE 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 955 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQG-WQMGVR 1033
Cdd:cd01387 573 PMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPKDmYRLGAT 652
|
....*
gi 1622884521 1034 KVFLK 1038
Cdd:cd01387 653 KVFLR 657
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
321-1038 |
8.10e-128 |
|
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: 415.56 E-value: 8.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLcsSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY---RQKL--LDSPHVYAVADTAYREMMRDEINQSIII 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 480
Cdd:cd01383 77 SGESGAGKTETAKIAMQYLAALGGGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHF-DAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTGERSLNREKLAVLKQALNVVGFS 560
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQS---NCLTIDGVDDAKKFHELKEALDTVGIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 561 NLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEF 640
Cdd:cd01383 232 KEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 641 FRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQ--RSmqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 718
Cdd:cd01383 312 ARDALAKAIYASLFDWLVEQINKSLEVGKRRtgRS-----ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 719 EQVECVQEG-----VTMETayspgNQNgVLDFFFQKPSGFLTLLDEesqmiwsmESNFPK--------KLQSLLessNTN 785
Cdd:cd01383 387 EQEEYELDGidwtkVDFED-----NQE-CLDLIEKKPLGLISLLDE--------ESNFPKatdltfanKLKQHL---KSN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 786 AVYSplkdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSEnvviNHLFQsklsqtgslvsay 865
Cdd:cd01383 450 SCFK-----------GERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCS----CQLPQ------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 866 psfkfrghksaLLSKKMTassiigenkNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLTDIIGKLQKCTPHFIH 945
Cdd:cd01383 502 -----------LFASKML---------DASRKALPLTKASGSDSQKQ-------SVATKFKGQLFKLMQRLENTTPHFIR 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 946 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAerCRLVLQQCKL 1025
Cdd:cd01383 555 CIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLST--SVAILQQFNI 632
|
730
....*....|....*
gi 1622884521 1026 QG--WQMGVRKVFLK 1038
Cdd:cd01383 633 LPemYQVGYTKLFFR 647
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
321-1038 |
3.16e-127 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 413.09 E-value: 3.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd01380 2 AVLHNLKVRFCQrNAIYTYCGIVLVAINPYEDLPIYGEDIIQAY---SGQNMGELDPHIFAIAEEAYRQMARDEKNQSII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAMlDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGA 476
Cdd:cd01380 79 VSGESGAGKTVSAKYAMRYFATVGGSSSGE-TQVEEKVLAsnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKN-YRIIGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 477 RIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ---TMQDDVStgerslNREKLAVLKQA 553
Cdd:cd01380 157 NMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQggsPVIDGVD------DAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 554 LNVVGFSNLEVENLFVILAAILHLGDIRFTAlTEGNSAFVS-DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 632
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKA-TRNDSASISpDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 633 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 712
Cdd:cd01380 310 LTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 713 EVLFLHEQVECVQEGVTMETAYSPGNQnGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL-QSLLESSntNAVYSPL 791
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDFYDNQ-PCID-LIEGKLGILDLLDEECRLPKGSDENWAQKLyNQHLKKP--NKHFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 792 KDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvvinhlfqsklsqtgslvsaypsfkfr 871
Cdd:cd01380 464 RFSN---------TAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 872 gHKSallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNN 951
Cdd:cd01380 508 -RKK--------------------------------------------TVGSQFRDSLILLMETLNSTTPHYVRCIKPND 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 952 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA---DTFLREKKEHLAAERCRLVLQQCKlqgW 1028
Cdd:cd01380 543 EKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLpskEWLRDDKKKTCENILENLILDPDK---Y 619
|
730
....*....|
gi 1622884521 1029 QMGVRKVFLK 1038
Cdd:cd01380 620 QFGKTKIFFR 629
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
320-1031 |
5.09e-124 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 404.54 E-value: 5.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPK---EMPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 479
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG-VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF-DNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 480 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLhlNNLCAHRYLNQTMQDDVSTGERSLNREKLavlKQALNVVGF 559
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSLSGCIEVEGVDDVADFEEV---VLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 560 SNLEVENLFVILAAILHLGDIRFTALTEGNSAF---VSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG--DMIIRRHT 634
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 635 IQiAEFFRDLLAKSLYSRLFSFLVNTMNsclLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 714
Cdd:cd14872 311 AQ-ATDACDALAKAAYSRLFDWLVKKIN---ESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 715 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQsllessNTNAVYSPLKDG 794
Cdd:cd14872 387 TFKLEEALYQSEGVKFEHIDFIDNQP-VLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN------QTHAAKSTFVYA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 795 NgnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsayPSFKFRghk 874
Cdd:cd14872 460 E----VRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------PPSEGD--- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 875 sallskkmtassiigenknylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKL 954
Cdd:cd14872 519 ---------------------------------------QKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 955 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREKKehLAAERCRLVLQ---QCKlQGWQM 1030
Cdd:cd14872 560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvKTIAKRVGP--DDRQRCDLLLKslkQDF-SKVQV 636
|
.
gi 1622884521 1031 G 1031
Cdd:cd14872 637 G 637
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
320-1038 |
6.41e-124 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 404.56 E-value: 6.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCF 398
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQY---SRRHLGELPPHIFAIANECYRCLWKRHDNQCI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 399 ILSGERGSGKSEASKQIIRHLT----------CRAASSR---AMLDSRfkhvmCILEAFGHAKTTLNDLSSCFIKYFELQ 465
Cdd:cd14873 78 LISGESGAGKTESTKLILKFLSvisqqslelsLKEKTSCveqAILESS-----PIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 466 FCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQT--MQDDVSTGERSLN 543
Cdd:cd14873 153 ICQ-KGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSgcVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 544 ReklaVLKqALNVVGFSNLEVENLFVILAAILHLGDIRFtaLTEGnSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 623
Cdd:cd14873 232 E----VIT-AMEVMQFSKEEVREVSRLLAGILHLGNIEF--ITAG-GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 624 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmqtldIGILDIFGFEEFQKNEFEQLCVNMT 703
Cdd:cd14873 304 LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS-----IGILDIFGFENFEVNHFEQFNINYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 704 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSlleSSN 783
Cdd:cd14873 379 NEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGE-CLD-LIEKKLGLLALINEESHFPQATDSTLLEKLHS---QHA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 784 TNAVYSPLKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvs 863
Cdd:cd14873 454 NNHFYVKPRVAVNN---------FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQ--- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 864 aypsfkfrghksallSKKMTASsiigenknylelskllkkkgtstflqrlERGDPvTIASQLRKSLTDIIGKLQKCTPHF 943
Cdd:cd14873 522 ---------------DTLKCGS----------------------------KHRRP-TVSSQFKDSLHSLMATLSSSNPFF 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 944 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKkehlaaerCRL 1018
Cdd:cd14873 558 VRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmrnlaLPEDVRGK--------CTS 629
|
730 740
....*....|....*....|..
gi 1622884521 1019 VLQQCKLQG--WQMGVRKVFLK 1038
Cdd:cd14873 630 LLQLYDASNseWQLGKTKVFLR 651
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
321-1038 |
9.98e-123 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 401.84 E-value: 9.98e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKY---KGKRREEMPPHIFAIADNAYRNMLQDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKH-------VMC--ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQ 471
Cdd:cd01377 79 TGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledqiLQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGS-TG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 472 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ------TMQDDVstgerslnrE 545
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltiDGVDDA---------E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 546 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIqyFK 625
Cdd:cd01377 229 EFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPR--IK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 626 -GDMIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMT 703
Cdd:cd01377 307 vGREWVTKGqNKEQVVFSVGALAKALYERLFLWLVKRINKTL---DTKSKRQYF-IGVLDIAGFEIFEFNSFEQLCINYT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 704 NEKMHHYINEVLFLHEQVECVQEGVTMEtayspgnqngVLDF---------FFQKPS-GFLTLLDEESQMIWSMESNFPK 773
Cdd:cd01377 383 NEKLQQFFNHHMFVLEQEEYKKEGIEWT----------FIDFgldlqptidLIEKPNmGILSILDEECVFPKATDKTFVE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 774 KLQSLLESSNTN-AVYSPLKDGNGnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ 852
Cdd:cd01377 453 KLYSNHLGKSKNfKKPKPKKSEAH----------FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 853 SKLSQTGSlvsaypSFKFRGHKSALLskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDI 932
Cdd:cd01377 523 DYEESGGG------GGKKKKKGGSFR-----------------------------------------TVSQLHKEQLNKL 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 933 IGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLA 1012
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGK 635
|
730 740
....*....|....*....|....*...
gi 1622884521 1013 AErCRLVLQQCKL--QGWQMGVRKVFLK 1038
Cdd:cd01377 636 AA-CEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
321-1038 |
3.26e-120 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 394.83 E-value: 3.26e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcsSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSI----SKSPHVFSTASSAYQGMCNNKKSQTIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASS---RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQ----- 471
Cdd:cd14888 78 ISGESGAGKTESTKYVMKFLACAGSEDikkRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKSkrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 472 ---QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL--NNLCAHR-YLNQTMQDDVSTGERSLNRE 545
Cdd:cd14888 158 drgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYeeNDEKLAKgADAKPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 546 KLAV-----------LKQ------ALNVVGFSNLEVENLFVILAAILHLGDIRFT---ALTEGNSAFVSDLQLLEQVAGM 605
Cdd:cd14888 238 YLTKsschelpdvddLEEfestlyAMQTVGISPEEQNQIFSIVAAILYLGNILFEnneACSEGAVVSASCTDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 606 LQVSTDELASALTTDiqyfkgdMIIRRH-------TIQIAEFFRDLLAKSLYSRLFSFLVNTMNScllSQDEQRSMQTLD 678
Cdd:cd14888 318 LGVDAEDLLNALCYR-------TIKTAHefytkplRVDEAEDVRDALARALYSCLFDKVVERTNE---SIGYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 679 IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLD 758
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCV-DLLQEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 759 EESQmiwsmesnFPK-KLQSLlessnTNAVYSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLF 837
Cdd:cd14888 467 EECF--------VPGgKDQGL-----CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 838 VMKTSENVVINHLFQSKLSqtgslvsaypsfkfRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergd 917
Cdd:cd14888 534 VIKNSKNPFISNLFSAYLR--------------RGTDGNTKKKKF----------------------------------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 918 pVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYK 997
Cdd:cd14888 565 -VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYR 643
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1622884521 998 PLADTFLREkkehlaaercrlvlqqcKLQGWQMGVRKVFLK 1038
Cdd:cd14888 644 ILLNGEGKK-----------------QLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
322-996 |
1.03e-119 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 393.63 E-value: 1.03e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 322 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFS-----SSGKLCSSLPPHLFSCVERAFHQLFQEQRP 395
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiiqnGEYFDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 396 QCFILSGERGSGKSEASKQIIRHLT-------------CRAASSRAMLDSRF----KHVMC--ILEAFGHAKTTLNDLSS 456
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTqlsqqeqnseevlTLTSSIRATSKSTKsieqKILSCnpILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 457 CFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCA---HRYLNQTMQD 533
Cdd:cd14907 163 RFGKYVSILVDKKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 534 DVSTgersLNREKL-AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRF--TALTEGNSAFVSDLQLLEQVAGMLQVST 610
Cdd:cd14907 243 EVDT----INDEKLfKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGIDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 611 DELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLL--SQDEQRSMQ--TLDIGILDIFG 686
Cdd:cd14907 319 EELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMpkDEKDQQLFQnkYLSIGLLDIFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 687 FEEFQKNEFEQLCVNMTNEKMHH-YINEVlFLHEQVECVQEGVT---METAYsPGNQNgVLDFFFQKPSGFLTLLDEESQ 762
Cdd:cd14907 399 FEVFQNNSFEQLCINYTNEKLQQlYISYV-FKAEEQEFKEEGLEdylNQLSY-TDNQD-VIDLLDKPPIGIFNLLDDSCK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 763 MIWSMESNFPKKLQSLLESSNTNAVYSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTS 842
Cdd:cd14907 476 LATGTDEKLLNKIKKQHKNNSKLIFPNKINK-----------DTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 843 ENVVINHLF----QSKLSQTGSLVSAYPSFKFRGHKsallskkmtassiigenknylelskllkkkgtstflqrlergdp 918
Cdd:cd14907 545 KNRIISSIFsgedGSQQQNQSKQKKSQKKDKFLGSK-------------------------------------------- 580
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884521 919 vtiasqLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 996
Cdd:cd14907 581 ------FRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQY 652
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
321-1038 |
1.01e-115 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 381.44 E-value: 1.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14896 2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASY---HPRKALNTTPHIFAIAASAYRLSQSTGQDQCILL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqfCERKQQLTGARIYT 480
Cdd:cd14896 79 SGHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRL--HLQHGVIVGASVSH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSlnrEKLAVLKQALNVVGFS 560
Cdd:cd14896 157 YLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDA---QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 561 NLEVENLFVILAAILHLGDIRFTAlTEGNS---AFVSDLQLLEQVAGMLQVSTDELASALT---TDIQYfkgDMIIRRHT 634
Cdd:cd14896 234 AEELTAIWAVLAAILQLGNICFSS-SERESqevAAVSSWAEIHTAARLLQVPPERLEGAVThrvTETPY---GRVSRPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 635 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 714
Cdd:cd14896 310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAT--IGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 715 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkkLQSLLESSNTNAVYS----P 790
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIPQPPRES-CLDLLVDQPHSLLSILDDQTWLSQATDHTF---LQKCHYHHGDHPSYAkpqlP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 791 LKdgngnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkf 870
Cdd:cd14896 464 LP-------------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYG----------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 871 rghksallskkmtassiigenknylelskllkkkgtstflqrLERGDPvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPN 950
Cdd:cd14896 520 ------------------------------------------LGQGKP-TLASRFQQSLGDLTARLGRSHVYFIHCLNPN 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 951 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADtflREKKEHLAAERCRLVLQQckLQG--- 1027
Cdd:cd14896 557 PGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS---ERQEALSDRERCGAILSQ--VLGaes 631
|
730
....*....|...
gi 1622884521 1028 --WQMGVRKVFLK 1038
Cdd:cd14896 632 plYHLGATKVLLK 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
321-1038 |
4.99e-115 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 380.28 E-value: 4.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRP---- 395
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLY---HGTTAGELPPHVFAIADHAYTQLIQSGVLdpsn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 396 QCFILSGERGSGKSEASKQIIRHLTcRAASSRA-------------------MLDSRFKHVMCILEAFGHAKTTLNDLSS 456
Cdd:cd14890 79 QSIIISGESGAGKTEATKIIMQYLA-RITSGFAqgasgegeaaseaieqtlgSLEDRVLSSNPLLESFGNAKTLRNDNSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 457 CFIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQtmQDDVS 536
Cdd:cd14890 158 RFGKFIEIQF-DHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRG--ECSSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 537 TGERslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG-NSAFVSDLQLLEQVAGMLQVSTDELAS 615
Cdd:cd14890 235 PSCD--DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTtVLEDATTLQSLKLAAELLGVNEDALEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 616 ALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEF 695
Cdd:cd14890 313 ALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGF----IGVLDIYGFEKFEWNTF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 696 EQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQN-GVLDFFFQKPSG----FLTLLDeesqmIWSMESN 770
Cdd:cd14890 389 EQLCINYANEKLQRHFNQHMFEVEQVEYSNEGI--DWQYITFNDNqACLELIEGKVNGkpgiFITLDD-----CWRFKGE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 771 FP-KKLQSLLESSntnavYSPLKDGNGNVALK-----------DHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFV 838
Cdd:cd14890 462 EAnKKFVSQLHAS-----FGRKSGSGGTRRGSsqhphfvhpkfDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKEL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 839 MKTSEnvvinhlfqsklsqtgslvsaypsfkfrghksallskkmtaSSIigenknylelskllkkkgtstflqrleRGdp 918
Cdd:cd14890 537 IKQSR-----------------------------------------RSI---------------------------RE-- 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 919 VTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKP 998
Cdd:cd14890 547 VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQV 626
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1622884521 999 LADTflREKKEHLAAERCRLvLQQCKLQgWQMGVRKVFLK 1038
Cdd:cd14890 627 LLPT--AENIEQLVAVLSKM-LGLGKAD-WQIGSSKIFLK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
322-1038 |
8.24e-114 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 376.41 E-value: 8.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 322 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQ----EQRPQC 397
Cdd:cd14892 3 LLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASSPPPHVFSIAERAYRAMKGvgkgQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 398 FILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVM------C------ILEAFGHAKTTLNDLSSCFIKYFELQ 465
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAhesieeCvllsnlILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 466 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStgERSLNRE 545
Cdd:cd14892 163 Y-NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVD--GVDDATE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 546 kLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALT--EGNSAFVSDLQLLEQVAGMLQVSTDELASALTTD-IQ 622
Cdd:cd14892 240 -FKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENAddEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQtTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 623 YFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSC---LLSQDEQRSM---QTLDIGILDIFGFEEFQKNEFE 696
Cdd:cd14892 319 TARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqQTSGVTGGAAsptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 697 QLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQNG-VLDFFFQKPSGFLTLLDEesQMIWSMESNfPKKL 775
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGI--DVSAIEFQDNQdCLDLIQKKPLGLLPLLEE--QMLLKRKTT-DKQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 776 QSLLESSN--TNAVYSPLKDGNgnvalkDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqs 853
Cdd:cd14892 474 LTIYHQTHldKHPHYAKPRFEC------DE---FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS----------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 854 klsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDII 933
Cdd:cd14892 534 ---------------------------------------------------------------------SKFRTQLAELM 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 934 GKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA------DTFLREK 1007
Cdd:cd14892 545 EVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvAASPDAC 624
|
730 740 750
....*....|....*....|....*....|..
gi 1622884521 1008 KEHLAAERCR-LVLQQCKLQGWQMGVRKVFLK 1038
Cdd:cd14892 625 DATTARKKCEeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
321-1038 |
3.17e-110 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 366.41 E-value: 3.17e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLcsSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14903 2 AILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKE--ELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLtcrAASSRAMLDSRFK---HVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGAR 477
Cdd:cd14903 80 SGESGAGKTETTKILMNHL---ATIAGGLNDSTIKkiiEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF-DKNGTLVGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 478 IYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHrylnqTMQDDVSTGERSLNREKLAVLKQALNVV 557
Cdd:cd14903 156 CRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAY-----TGANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 558 GFSNLEVENLFVILAAILHLGDIRFTALT--EGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 635
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPndDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 636 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 715
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASL--GNDAKMANH--IGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 716 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKpSGFLTLLDEESQMIWSMESNFPKKLQSLLEsSNTNAVYSPlkdgn 795
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDFADNQD-VLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHK-DEQDVIEFP----- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 796 gnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKS 875
Cdd:cd14903 459 -----RTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 876 ALLSKkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLP 955
Cdd:cd14903 534 ALTTT---------------------------------------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSP 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 956 DTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYkplaDTFLREKKEHL--AAERCRLVLQQCKLQG---WQM 1030
Cdd:cd14903 575 TELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKF----WLFLPEGRNTDvpVAERCEALMKKLKLESpeqYQM 650
|
....*...
gi 1622884521 1031 GVRKVFLK 1038
Cdd:cd14903 651 GLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
320-1038 |
6.85e-108 |
|
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: 359.25 E-value: 6.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCF 398
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSY---QGKSLGTLPPHVFAIADKAYRDMKVLKQSQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 399 ILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 478
Cdd:cd01382 78 IVSGESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF-NEKSSVVGGFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 479 YTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLhlnnlcahryLNQTMQDDVstgerslnrEKLAVLKQALNVVG 558
Cdd:cd01382 157 SHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------LKDPLLDDV---------GDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 559 FSNLEVENLFVILAAILHLGDIRFTALTEGNSA----FVSDLQLLEQVAGMLQVSTDELASALTTDIQY-----FKGDMI 629
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgcnvKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQttrggAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 630 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeqRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 709
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE---TSSYF--IGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 710 YINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkklqsllessnTNAVYS 789
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEYVDNQD-CIDLIEAKLVGILDLLDEESKLPKPSDQHF------------TSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 790 PLKDgNGNVA------LKDHGT-----AFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 858
Cdd:cd01382 440 KHKN-HFRLSiprkskLKIHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 859 GSLVSAypsfkfrghksallSKKMTASSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLTDIIGKLQK 938
Cdd:cd01382 519 KDSKQK--------------AGKLSFIS----------------------------------VGNKFKTQLNLLMDKLRS 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 939 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladTFLREKKEHLAAER-CR 1017
Cdd:cd01382 551 TGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYK----KYLPPKLARLDPRLfCK 626
|
730 740
....*....|....*....|...
gi 1622884521 1018 LVLQQCKLQG--WQMGVRKVFLK 1038
Cdd:cd01382 627 ALFKALGLNEndFKFGLTKVFFR 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
321-1038 |
2.88e-107 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 359.65 E-value: 2.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvsQLY----FSSSGKLCSSLPPHLFSCVERAF-------HQL 389
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYdlhkYREEMPGWTALPPHVFSIAEGAYrslrrrlHEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 390 FQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC---------ILEAFGHAKTTLNDLSSCFIK 460
Cdd:cd14895 75 GASKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISgsellsanpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 461 Y----FELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH--RYLNQTM--- 531
Cdd:cd14895 155 FvrmfFEGHELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQefQYISGGQcyq 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 532 -QDDVStgerslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN---------------SAFVSD 595
Cdd:cd14895 235 rNDGVR------DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 596 L---QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlSQDEQR 672
Cdd:cd14895 309 LtvqQHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS-PQRQFA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 673 SMQTLD--------IGILDIFGFEEFQKNEFEQLCVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNqNGVL 743
Cdd:cd14895 388 LNPNKAankdttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLqYQFIQDIL-LTEQQAHIEEGIKWNAVDYEDN-SVCL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 744 DFFFQKPSGFLTLLDEESQMIWSMESNFPKKL-QSLLESSNTNAVYSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVG 822
Cdd:cd14895 466 EMLEQRPSGIFSLLDEECVVPKGSDAGFARKLyQRLQEHSNFSASRTDQAD-----------VAFQIHHYAGAVRYQAEG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 823 AIEKNKDSLSQNLLFVMKTSENVVINHLFQS-KLSQTGSLVSAYPsfKFRGHKSALLSkkmtassiigenknylelskll 901
Cdd:cd14895 535 FCEKNKDQPNAELFSVLGKTSDAHLRELFEFfKASESAELSLGQP--KLRRRSSVLSS---------------------- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 902 kkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 981
Cdd:cd14895 591 -----------------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQ 653
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884521 982 GYPVRLSFSDFLSRYKPLADTflREKKEHLAAErcrlVLQQCKLQGWQMGVRKVFLK 1038
Cdd:cd14895 654 SYPVRMKHADFVKQYRLLVAA--KNASDATASA----LIETLKVDHAELGKTRVFLR 704
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
321-1037 |
1.21e-106 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 356.02 E-value: 1.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGK---LCSSLPPHLFSCVERAFHQLFQEQRP-- 395
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGERraaGERKLPPHVYAVADKAFRAMLFASRGqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 396 --QCFILSGERGSGKSEASKQIIRHLTC--------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQ 465
Cdd:cd14901 82 cdQSILVSGESGAGKTETTKIIMNYLASvssatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 466 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGerSLNRE 545
Cdd:cd14901 162 F-ASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDG--VDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 546 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF-VSDLQLLEQVAGMLQVSTDELASALTTDIQYF 624
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFsMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 625 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTN 704
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASRF--IGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 705 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLeSSNT 784
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDA-CVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLL-AKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 785 NAVYSPLKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVInhlfqsklsqtgslvsa 864
Cdd:cd14901 475 SFSVSKLQQGKRQ---------FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL----------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 865 ypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQKCTPHFI 944
Cdd:cd14901 529 -----------------------------------------------------SSTVVAKFKVQLSSLLEVLNATEPHFI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 945 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTfLREKKEHL--AAERCRLVLQQ 1022
Cdd:cd14901 556 RCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPD-GASDTWKVneLAERLMSQLQH 634
|
730 740
....*....|....*....|
gi 1622884521 1023 CKLQG-----WQMGVRKVFL 1037
Cdd:cd14901 635 SELNIehlppFQVGKTKVFL 654
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
321-996 |
2.49e-104 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 349.24 E-value: 2.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRD---KLQPHVYATSTAAYKHMLTNEMNQSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 479
Cdd:cd14904 79 VSGESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF-DGRGKLIGAKCE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 480 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGersLNREKL-AVLKQALNVVG 558
Cdd:cd14904 158 TYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPG---LDDAKLfASTQKSLSLIG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 559 FSNLEVENLFVILAAILHLGDIRFTALTEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 638
Cdd:cd14904 235 LDNDAQRTLFKILSGVLHLGEVMFDKSDENGSR-ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 639 EFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 718
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ---IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 719 EQVECVQEGVTMETAYSPGNQnGVLDFFFQKpSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntnavysplKDGNGNV 798
Cdd:cd14904 391 VEEEYIREGLQWDHIEYQDNQ-GIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQT----------KKDNESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 799 AL-KDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvSAYPSfkfrghksal 877
Cdd:cd14904 459 DFpKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---------SEAPS---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 878 lSKKMTASsiiGENKNylelskllkkkgtstflqrlergDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDT 957
Cdd:cd14904 520 -ETKEGKS---GKGTK-----------------------APKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE 572
|
650 660 670
....*....|....*....|....*....|....*....
gi 1622884521 958 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 996
Cdd:cd14904 573 FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
321-1006 |
2.46e-99 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 336.95 E-value: 2.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVsqLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLI--LNEYKDINQNKSPIPHIYAVALRAYQSMVSEKKNQSII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAML-------DSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCER 469
Cdd:cd14906 80 ISGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnNSIEKDILTsnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 470 KQQLTGARIYTYLLEKSRLVSQP-LGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLN-----------QTMQDDVS 536
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDarddvissfksQSSNKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 537 TGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNS-AFVSD--LQLLEQVAGMLQVSTDEL 613
Cdd:cd14906 240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKyAYQKDkvTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 614 ASALTTdiQYFK----GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQ-------TLDIGIL 682
Cdd:cd14906 320 KQALLN--RNLKaggrGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAggsnkknNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 683 DIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQ 762
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKE-CIELIEKKSDGILSLLDDECI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 763 MiwsmesnfPK-KLQSLLES-----SNTNAVYS-PLKDGngnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNL 835
Cdd:cd14906 477 M--------PKgSEQSLLEKynkqyHNTNQYYQrTLAKG-----------TLGIKHFAGDVTYQTDGWLEKNRDSLYSDV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 836 LFVMKTSENVVINHLFQSKLSQTGSlvsaypsfkfrghksalLSKKMTASsiigenknylelskllkkkgtstflqrler 915
Cdd:cd14906 538 EDLLLASSNFLKKSLFQQQITSTTN-----------------TTKKQTQS------------------------------ 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 916 gdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSR 995
Cdd:cd14906 571 ---NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSR 647
|
730
....*....|.
gi 1622884521 996 YKPLADTFLRE 1006
Cdd:cd14906 648 YKCIVDMYNRK 658
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
317-1041 |
6.89e-97 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 327.58 E-value: 6.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 317 LNDGSLLYEIQKRFGNNQIYTFIGD-ILLLVNPYKELPIYS--SM---VSQLYFSSSGKLcSSLPPHLFSCVERAFHQLF 390
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSdaSLgeyGSEYYDTTSGSK-EPLPPHAYDLAARAYLRMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 391 QEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSR--AMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCE 468
Cdd:cd14879 80 RRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkgTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 469 RKQqLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLA 548
Cdd:cd14879 160 RGR-LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGCHPLPLGPGSDDAEGFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 549 VLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 626
Cdd:cd14879 239 ELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGeeSAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVRK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 627 DmiirRHTI----QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQtldIGILDIFGFEEF---QKNEFEQLC 699
Cdd:cd14879 319 E----LCTVfldpEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATF---ISLLDFPGFQNRsstGGNSLDQFC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 700 VNMTNEKMHHYINEVLFLHEQVECVQEGVTM-ETAYsPGNQnGVLDFFFQKPSGFLTLLDEESqmiwsmeSNFPKKL-QS 777
Cdd:cd14879 392 VNFANERLHNYVLRSFFERKAEELEAEGVSVpATSY-FDNS-DCVRLLRGKPGGLLGILDDQT-------RRMPKKTdEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 778 LLES-SNTNAVYSPLKDGNGNVALKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktsenvvinhlfqskls 856
Cdd:cd14879 463 MLEAlRKRFGNHSSFIAVGNFATRSGSAS-FTVNHYAGEVTYSVEGFLERNGDVLS------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 857 qtGSLVSAypsfkFRGhksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLTDIIGKL 936
Cdd:cd14879 518 --PDFVNL-----LRG-------------------------------------------------ATQLNAALSELLDTL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 937 QKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEHLAAERC 1016
Cdd:cd14879 542 DRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKST----LRGSAAERIRQCA 617
|
730 740
....*....|....*....|....*..
gi 1622884521 1017 RLVLQQCKLQGWqMGVRKVFLKY--WH 1041
Cdd:cd14879 618 RANGWWEGRDYV-LGNTKVFLSYaaWR 643
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
321-1020 |
6.40e-95 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 324.15 E-value: 6.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-----FSSSGKLCSSLPPHLFSCVERAFHQLFQEQR 394
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtSTSPVSQLSELPPHVFAIGGKAFGGLLKPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 395 P-QCFILSGERGSGKSEASKQIIRHLTC---------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFEL 464
Cdd:cd14902 82 RnQSILVSGESGSGKTESTKFLMQFLTSvgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 465 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ---TMQDDVSTGERS 541
Cdd:cd14902 162 QF-GANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 542 LNREKLAVlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF-VSDLQL--LEQVAGMLQVSTDELASALT 618
Cdd:cd14902 241 AQLYVETV--RAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATaVTAASRfhLAKCAELMGVDVDKLETLLS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 619 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLV----NTMN---SCLLSQDEQRSMQTldIGILDIFGFEEFQ 691
Cdd:cd14902 319 SREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVrrlsDEINyfdSAVSISDEDEELAT--IGILDIFGFESLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 692 KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsmesnf 771
Cdd:cd14902 397 RNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDDKSNGLFSLLDQECLM-------- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 772 PKKLQsllESSNTNAVYSPLKDGNgnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVInhlf 851
Cdd:cd14902 468 PKGSN---QALSTKFYRYHGGLGQ-----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 852 qsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKnylelskllkkkgtstflQRLERGDPVTIAS---QLRKS 928
Cdd:cd14902 530 -----------------------VAIGADENRDSPGADNGA------------------AGRRRYSMLRAPSvsaQFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 929 LTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADT 1002
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFkcflstRDR 648
|
730
....*....|....*...
gi 1622884521 1003 FLREKKEHLAAERCRLVL 1020
Cdd:cd14902 649 AAKMNNHDLAQALVTVLM 666
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
322-1000 |
1.62e-94 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 320.84 E-value: 1.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 322 LLYEIQKRFG--NNQIYTFIGDILLLVNPYKELPiySSMVSqLYFSSSGKLCsslPPHLFSCVERAFHQLF---QEQRPQ 396
Cdd:cd14891 3 ILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPDKS-DYINTPLDPC---PPHPYAIAEMAYQQMClgsGRMQNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 397 CFILSGERGSGKSEASKQIIRHLTCRAASSRAM------------------LDSRFKHVMCILEAFGHAKTTLNDLSSCF 458
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFLTTRAVGGKKAsgqdieqsskkrklsvtsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 459 IKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTG 538
Cdd:cd14891 157 GKFMKLQFTKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQS---GCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 539 ERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRF----TALTEGNSAFVSDLQLLEQVAGMLQVSTDELA 614
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 615 SALTT-DIQYFKGDMIIRRhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQ-K 692
Cdd:cd14891 314 KVITQrEIVTRGETFTIKR-NAREAVYSRDAIAKSIYERLFLWIVQQINTSL----GHDPDPLPYIGVLDIFGFESFEtK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 693 NEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwSMESNfp 772
Cdd:cd14891 389 NDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRE-CLDLIASKPNGILPLLDNEARN--PNPSD-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 773 KKLQSLLESSNTNAVYSPLKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLlfvmktsENVVinhlfq 852
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHP------KDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDF-------EDLL------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 853 sklsqtgslvsaypsfkfrgHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLTDi 932
Cdd:cd14891 525 --------------------ASSAKFSDQM--------------------------------------------QELVD- 539
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884521 933 igKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1000
Cdd:cd14891 540 --TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVL 605
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
321-1008 |
2.56e-94 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 321.47 E-value: 2.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFS---------SSGKlcsSLPPHLFSCVERAFHQLFQ 391
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqgiESPQ---ALGPHVFAIADRSYRQMMS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 392 EQRP-QCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDS-----------RFKHVMCILEAFGHAKTTLNDLSSCFI 459
Cdd:cd14908 79 EIRAsQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimdRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 460 KYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH-----RYLNQTMQDD 534
Cdd:cd14908 159 KFIELGF-NRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpNEFHYTGQGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 535 VSTGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF---VSDLQLLEQVAGMLQVSTD 611
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEiaeEGNEKCLARVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 612 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLL--SQDEQRSmqtlDIGILDIFGFEE 689
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRS----SVGVLDIFGFEC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 690 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQM-IWSME 768
Cdd:cd14908 394 FAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQD-CLDTIQAKKKGILTMLDDECRLgIRGSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 769 SNFPKKLqsllessntNAVYSPLKDGNGNVALKDHGTA-------FTIMHYAGRVMYDV-VGAIEKNKDSLSqnllfvmK 840
Cdd:cd14908 473 ANYASRL---------YETYLPEKNQTHSENTRFEATSiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIP-------L 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 841 TSENvvinhLFQSklsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvt 920
Cdd:cd14908 537 TADS-----LFES------------------------------------------------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 921 iASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1000
Cdd:cd14908 545 -GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLL 623
|
....*...
gi 1622884521 1001 DTFLREKK 1008
Cdd:cd14908 624 PLIPEVVL 631
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
321-1038 |
1.16e-93 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 318.84 E-value: 1.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14929 2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRA-----MLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLTG 475
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESkkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM-LSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 476 ARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDG--------LSAEEKHGLHLnnlCAHRYLNQTMQDDVstgerslnrEKL 547
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGkkelrdllLVSANPSDFHF---CSCGAVAVESLDDA---------EEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 548 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 627
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 628 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 707
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVL---DAKLSRQFF-IGILDITGFEILDYNSLEQLCINFTNEKL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 708 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSMESNFPKKLqslLESSNTNAV 787
Cdd:cd14929 382 QQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKL---FDNHFGKSV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 788 Y--SPLKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqTGSlvsay 865
Cdd:cd14929 458 HfqKPKPDK------KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIS-TDS----- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 866 psfkfrghksallskkmtaSSIIGENKNylelskllkKKGTSTFLqrlergdpvtIASQLRKSLTDIIGKLQKCTPHFIH 945
Cdd:cd14929 526 -------------------AIQFGEKKR---------KKGASFQT----------VASLHKENLNKLMTNLKSTAPHFVR 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 946 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREK--KEHLAAERCRLVLQQ 1022
Cdd:cd14929 568 CINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILnPRTFPKSKfvSSRKAAEELLGSLEI 647
|
730
....*....|....*.
gi 1622884521 1023 CKLQgWQMGVRKVFLK 1038
Cdd:cd14929 648 DHTQ-YRFGITKVFFK 662
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
309-1076 |
1.04e-91 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 317.74 E-value: 1.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 309 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQ 388
Cdd:PTZ00014 99 GDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDS--DKLPPHVFTTARRALEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 389 LFQEQRPQCFILSGERGSGKSEASKQIIRHLtcrAASSRAMLDSRF-KHVMC---ILEAFGHAKTTLNDLSSCFIKYFEL 464
Cdd:PTZ00014 177 LHGVKKSQTIIVSGESGAGKTEATKQIMRYF---ASSKSGNMDLKIqNAIMAanpVLEAFGNAKTIRNNNSSRFGRFMQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 465 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTGE 539
Cdd:PTZ00014 254 QL-GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLdvpgiDDVKDFE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 540 RSLnreklavlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG---NSAFVSD--LQLLEQVAGMLQVSTDELA 614
Cdd:PTZ00014 333 EVM---------ESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDesLEVFNEACELLFLDYESLK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 615 SALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNE 694
Cdd:PTZ00014 404 KELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVF----IGMLDIFGFEVFKNNS 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 695 FEQLCVNMTNEKMH-HYINeVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPK 773
Cdd:PTZ00014 480 LEQLFINITNEMLQkNFVD-IVFERESKLYKDEGISTEELEYTSNES-VIDLLCGKGKSVLSILEDQCLAPGGTDEKFVS 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 774 KLQSLLESsntNAVYSPLK-DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ 852
Cdd:PTZ00014 558 SCNTNLKN---NPKYKPAKvDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 853 SKLSQTGSlvsaypsfkfrghksalLSKKMtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDI 932
Cdd:PTZ00014 626 GVEVEKGK-----------------LAKGQ-------------------------------------LIGSQFLNQLDSL 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 933 IGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLA 1012
Cdd:PTZ00014 652 MSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL-DLAVSNDSSLDP 730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884521 1013 AERCRLVLQQCKL--QGWQMGVRKVFLKYWHADQLNdlclQLQRKIITCQK--------VIRGFLARQHLLQKI 1076
Cdd:PTZ00014 731 KEKAEKLLERSGLpkDSYAIGKTMVFLKKDAAKELT----QIQREKLAAWEplvsvleaLILKIKKKRKVRKNI 800
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
321-1027 |
1.86e-89 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 305.69 E-value: 1.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS--------LPPHLFSCVERAFHQ--- 388
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLLSFEARSSStrnkgsdpMPPHIYQVAGEAYKAmml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 389 -LFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCI----------LEAFGHAKTTLNDLSSC 457
Cdd:cd14900 82 gLNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIaakvlqtnilLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 458 FIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGlSAEEKHGLHLnnlcahryLNQTMqddvst 537
Cdd:cd14900 162 FGKFIKLHF-TSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG-ASEAARKRDM--------YRRVM------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 538 gerslnreklavlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDL-----QLLEQVAGMLQVST 610
Cdd:cd14900 226 --------------DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrlGQLKSDLapssiWSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 611 DELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLD-IGILDIFGFEE 689
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHfIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 690 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMES 769
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQD-CVNLISQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 770 NFPKKLQSLLEsSNTNAVYSPLKDGNGnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinH 849
Cdd:cd14900 451 TLASKLYRACG-SHPRFSASRIQRARG---------LFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------D 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 850 LFQSKLsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiasQLRKSL 929
Cdd:cd14900 509 LFVYGL--------------------------------------------------------------------QFKEQL 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 930 TDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtflREKKE 1009
Cdd:cd14900 521 TTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLA----RAKNR 596
|
730
....*....|....*...
gi 1622884521 1010 HLAAERCRLVLQQCKLQG 1027
Cdd:cd14900 597 LLAKKQGTSLPDTDSDHG 614
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
321-1038 |
3.50e-89 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 306.14 E-value: 3.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASS-----------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFE 463
Cdd:cd14911 79 TGESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 464 LQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTG 538
Cdd:cd14911 159 INF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLpvpgvDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 539 ERSLNreklavlkqALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALT 618
Cdd:cd14911 238 QATVK---------SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 619 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQL 698
Cdd:cd14911 309 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL---DRTKRQGASFIGILDMAGFEIFELNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 699 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSl 778
Cdd:cd14911 386 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKLVS- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 779 LESSNTNAVYSPLKdgngnvalkdhGTA-FTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsq 857
Cdd:cd14911 464 AHSMHPKFMKTDFR-----------GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD---- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 858 tgslvsaypsfkfrghksallskkmtaSSIIGenknylelsKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQ 937
Cdd:cd14911 529 ---------------------------AEIVG---------MAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLR 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 938 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT-----FLREKKEhla 1012
Cdd:cd14911 573 NTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNvipkgFMDGKKA--- 649
|
730 740
....*....|....*....|....*...
gi 1622884521 1013 aerCRLVLQQCKLQG--WQMGVRKVFLK 1038
Cdd:cd14911 650 ---CEKMIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
321-1038 |
6.26e-89 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 305.40 E-value: 6.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY---RGKKRHEMPPHIYAISESAYRCMLQDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQ 472
Cdd:cd14920 79 TGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 473 LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-----TMQDDvstgerslnREKL 547
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNgyipiPGQQD---------KDNF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 548 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 627
Cdd:cd14920 229 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 628 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 707
Cdd:cd14920 309 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 708 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLQSllESSNTN 785
Cdd:cd14920 386 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 786 AVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG-SLVSA 864
Cdd:cd14920 464 KFQKPRQ-------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGlDQVTG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 865 YPSFKFrghKSALLSKKmtassiigenknylelskllkkkgtstflqrlerGDPVTIASQLRKSLTDIIGKLQKCTPHFI 944
Cdd:cd14920 536 MTETAF---GSAYKTKK----------------------------------GMFRTVGQLYKESLTKLMATLRNTNPNFV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 945 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA-----DTFLREKkehlaaERCRLV 1019
Cdd:cd14920 579 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpnaipKGFMDGK------QACERM 652
|
730 740
....*....|....*....|.
gi 1622884521 1020 LQQCKLQG--WQMGVRKVFLK 1038
Cdd:cd14920 653 IRALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
329-1038 |
7.34e-89 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 304.60 E-value: 7.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 329 RFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGK 408
Cdd:cd14876 10 RYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPD--LTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 409 SEASKQIIRHLtcrAASSRAMLDSRF-KHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGArIYTYLLE 484
Cdd:cd14876 88 TEATKQIMRYF---ASAKSGNMDLRIqTAIMAanpVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS-VVAFLLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 485 KSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTGERslnreklavLKQALNVVGF 559
Cdd:cd14876 164 KSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLdvpgiDDVADFEE---------VLESLKSMGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 560 SNLEVENLFVILAAILHLGDIRFTALTEG---NSAFVS--DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 634
Cdd:cd14876 235 TEEQIDTVFSIVSGVLLLGNVKITGKTEQgvdDAAAISneSLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 635 IQIAEFFRDLLAKSLYSRLFSFLVNTMNScllSQDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINe 713
Cdd:cd14876 315 KDDAEMLKLSLAKAMYDKLFLWIIRNLNS---TIEPPGGFKNF-MGMLDIFGFEVFKNNSLEQLFINITNEMLQkNFID- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 714 VLFLHEQVECVQEGV-TMETAYSPGNQngVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVYSPLK 792
Cdd:cd14876 390 IVFERESKLYKDEGIpTAELEYTSNAE--VIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS---NGKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 793 -DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkfr 871
Cdd:cd14876 465 vDSNIN---------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG------------ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 872 ghksallskKMTASSIIGenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDIIGKLQKCTPHFIHCIRPNN 951
Cdd:cd14876 524 ---------KIAKGSLIG---------------------------------SQFLKQLESLMGLINSTEPHFIRCIKPNE 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 952 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLAAERCRLVLQQCKL--QGWQ 1029
Cdd:cd14876 562 TKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL-DLGIANDKSLDPKVAALKLLESSGLseDEYA 640
|
....*....
gi 1622884521 1030 MGVRKVFLK 1038
Cdd:cd14876 641 IGKTMVFLK 649
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
321-1038 |
1.28e-88 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 304.57 E-value: 1.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAM--------------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQF 466
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPgkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 467 CErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLN-NLCAHRYLNQ--TMQDDVSTGErsln 543
Cdd:cd14927 159 GP-TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQgvTTVDNMDDGE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 544 reKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 623
Cdd:cd14927 234 --ELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 624 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 703
Cdd:cd14927 312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFF----IGVLDIAGFEIFEFNSFEQLCINFT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 704 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLES 781
Cdd:cd14927 388 NEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACID-LIEKPLGILSILEEECMFPKASDASFKAKLydNHLGKS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 782 SNTNavySPLKDGNgnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgsl 861
Cdd:cd14927 467 PNFQ---KPRPDKK-----RKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSD--- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 862 vSAYPsfkfrgHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpvTIASQLRK-SLTDIIGKLQKCT 940
Cdd:cd14927 536 -STED------PKSGVKEKRKKAASF--------------------------------QTVSQLHKeNLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 941 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADTFLREKKehlAAE 1014
Cdd:cd14927 577 PHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILnpsaipDDKFVDSRK---ATE 653
|
730 740
....*....|....*....|....
gi 1622884521 1015 RCRLVLQQCKLQgWQMGVRKVFLK 1038
Cdd:cd14927 654 KLLGSLDIDHTQ-YQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
321-1038 |
2.02e-88 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 303.68 E-value: 2.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14909 2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMY---RGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASS--------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQ 472
Cdd:cd14909 79 TGESGAGKTENTKKVIAYFATVGASKktdeaaksKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP-TGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 473 LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLNQ--TMQDDVSTGErslnreKLAV 549
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQgkVTVPNVDDGE------EFSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 550 LKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 629
Cdd:cd14909 232 TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 630 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 709
Cdd:cd14909 312 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL---DTQQKRQHF-IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 710 YINEVLFLHEQVECVQEGVtmETAYspgnqngvLDF---------FFQKPSGFLTLLDEESQMIWSMESNFPKKLQSL-L 779
Cdd:cd14909 388 FFNHHMFVLEQEEYKREGI--DWAF--------IDFgmdllacidLIEKPMGILSILEEESMFPKATDQTFSEKLTNThL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 780 ESSNTNAVYSPLKDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG 859
Cdd:cd14909 458 GKSAPFQKPKPPKPGQ-------QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 860 SLVSAYPSfkfRGHKSALLSkkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKC 939
Cdd:cd14909 531 GGEQAKGG---RGKKGGGFA----------------------------------------TVSSAYKEQLNSLMTTLRST 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 940 TPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR-EKKEHLAAERCrl 1018
Cdd:cd14909 568 QPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQgEEDPKKAAEII-- 645
|
730 740
....*....|....*....|..
gi 1622884521 1019 vLQQCKL--QGWQMGVRKVFLK 1038
Cdd:cd14909 646 -LESIALdpDQYRLGHTKVFFR 666
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
320-1038 |
1.24e-86 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 298.85 E-value: 1.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDS--------RFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 471
Cdd:cd14921 78 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 472 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLavlk 551
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 552 QALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 631
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 632 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 711
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 712 NEVLFLHEQVECVQEGV-------------TMETAYSPGNqngvldfffqkPSGFLTLLDEESQMIWSMESNFPKKLQSl 778
Cdd:cd14921 390 NHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCT- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 779 lESSNTNAVYSPLKdgngnvaLKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 858
Cdd:cd14921 458 -EQGNHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 859 GSLVSAypsfkfrghksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQK 938
Cdd:cd14921 529 GLDQMA----------------KMTESSLPSASKT--------------------KKGMFRTVGQLYKEQLGKLMTTLRN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 939 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRL 1018
Cdd:cd14921 573 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACIL 651
|
730 740
....*....|....*....|..
gi 1622884521 1019 VLQQCKLQG--WQMGVRKVFLK 1038
Cdd:cd14921 652 MIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
321-1038 |
2.02e-86 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 297.88 E-value: 2.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLF-QEQRPQCF 398
Cdd:cd14875 2 TLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDP--RLLPPHIWQVAHKAFNAIFvQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 399 ILSGERGSGKSEASKQII------RHLTCRAASSRAM---LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCER 469
Cdd:cd14875 80 VISGESGSGKTENAKMLIaylgqlSYMHSSNTSQRSIadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 470 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGL-HLNNLCAHRYLN--QTMQDDVSTGERSLNREK 546
Cdd:cd14875 160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNggNTFVRRGVDGKTLDDAHE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 547 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTAlTEGNSAFVSDLQLLEQVAGMLQVSTDELASALttdiqyfkg 626
Cdd:cd14875 240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLRECF--------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 627 dmIIRRHT--IQI------AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQL 698
Cdd:cd14875 310 --LVKSKTslVTIlankteAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGCKY--IGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 699 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSl 778
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECV-NMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWD- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 779 lESSNTNAVYSPLKDGNGNvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqt 858
Cdd:cd14875 464 -QWANKSPYFVLPKSTIPN--------QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIR---------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 859 gSLVSAYPSFKFRGHksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQK 938
Cdd:cd14875 525 -TLLSTEKGLARRKQ----------------------------------------------TVAIRFQRQLTDLRTELES 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 939 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFlSRY------KPLADTFlreKKEHLA 1012
Cdd:cd14875 558 TETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF-CRYfylimpRSTASLF---KQEKYS 633
|
730 740 750
....*....|....*....|....*....|.
gi 1622884521 1013 AERCRLVLQQCKLQGWQ-----MGVRKVFLK 1038
Cdd:cd14875 634 EAAKDFLAYYQRLYGWAkpnyaVGKTKVFLR 664
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
320-1038 |
1.06e-85 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 295.78 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMY---KGKKRTEMPPHLFSISDNAYHDMLMDRENQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTC------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQL 473
Cdd:cd14934 78 ITGESGAGKTENTKKVIQYFANiggtgkQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT-TGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 474 TGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLNQ--TMQDDVSTGErslnreKLAVL 550
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQgvTVVDNMDDGE------ELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 551 KQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 630
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 631 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 710
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTL----DTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 711 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNtnavY 788
Cdd:cd14934 387 FNHHMFVLEQEEYKREGIEWVFIDFGLDLQACID-LLEKPMGIFSILEEQCVFPKATDATFKAALydNHLGKSSN----F 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 789 SPLKDGNGnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvsaypsf 868
Cdd:cd14934 462 LKPKGGKG----KGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS-------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 869 kfrghksallSKKMTASSIIgenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIR 948
Cdd:cd14934 530 ----------KKQKRGSSFM-------------------------------TVSNFYREQLNKLMTTLHSTAPHFVRCIV 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 949 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKKehlAAErcrLVLQQC 1023
Cdd:cd14934 569 PNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLnpnviPQGFVDNKK---ASE---LLLGSI 642
|
730
....*....|....*..
gi 1622884521 1024 KLQ--GWQMGVRKVFLK 1038
Cdd:cd14934 643 DLDvnEYKIGHTKVFFR 659
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
320-1038 |
1.53e-84 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 292.70 E-value: 1.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAAS------------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFc 467
Cdd:cd14932 78 CTGESGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 468 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqtmqddvSTGERSL----N 543
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFL--------SNGNVTIpgqqD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 544 REKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 623
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 624 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 703
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 704 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSMESNFPKKLQSllES 781
Cdd:cd14932 386 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQ--EQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 782 SNTNAVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgsl 861
Cdd:cd14932 464 GNNPKFQKPKK-------LKDDAD-FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD-------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 862 vsaypsfkfrghksallskkmtASSIIGENKNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLTDIIGKLQKCTP 941
Cdd:cd14932 528 ----------------------VDRIVGLDKVAGMGESLHGAFKTRKGMFR-------TVGQLYKEQLMNLMTTLRNTNP 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 942 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQ 1021
Cdd:cd14932 579 NFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMVK 657
|
730
....*....|....*....
gi 1622884521 1022 QCKLQG--WQMGVRKVFLK 1038
Cdd:cd14932 658 ALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
321-1038 |
7.20e-84 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 290.41 E-value: 7.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASS----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERK 470
Cdd:cd14913 79 TGESGAGKTVNTKRVIQYFATIAATGdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 471 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREK 546
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITT-------NPYDYPFISQGEILVasidDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 547 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 626
Cdd:cd14913 231 LLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 627 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEK 706
Cdd:cd14913 311 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL---DTKLPRQHF-IGVLDIAGFEIFEYNSLEQLCINFTNEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 707 MHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNt 784
Cdd:cd14913 387 LQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 785 navYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsa 864
Cdd:cd14913 465 ---FQKPKVVKGRAE-----AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 865 ypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFI 944
Cdd:cd14913 526 -----FATADADSGKKKVAKKK-------------------GSSFQ---------TVSALFRENLNKLMSNLRTTHPHFV 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 945 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCK 1024
Cdd:cd14913 573 RCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASID 652
|
730
....*....|....*.
gi 1622884521 1025 LQ--GWQMGVRKVFLK 1038
Cdd:cd14913 653 IDhtQYKFGHTKVFFK 668
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
321-1038 |
2.70e-83 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 288.18 E-value: 2.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSR---SDNAPHIFSVADSAYQDMLHHEEPQHIIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLtCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 480
Cdd:cd14882 79 SGESYSGKTTNARLLIKHL-CYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTF-GSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEK-HGLHLNNLCAHRYLnqtmQDDVSTGERSL---------NREKLAVL 550
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYL----RIPPEVPPSKLkyrrddpegNVERYKEF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 551 KQALNVVGFSNLEVENLFVILAAILHLGDIRFTaltEGN-SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 629
Cdd:cd14882 233 EEILKDLDFNEEQLETVRKVLAAILNLGEIRFR---QNGgYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 630 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeqRSM--QTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 707
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFP---RAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 708 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQmiwSMESnfpkklqsllessnTNAV 787
Cdd:cd14882 387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAV-DQLMTKPDGLFYIIDDASR---SCQD--------------QNYI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 788 YSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLVSAYPS 867
Cdd:cd14882 449 MDRIKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--SQVRNMRTLAAT 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 868 FKFrghkSALLSKKMTAssiIGENknylelskllkKKGTstflqrlergdpvtiasqlrksltdiigklqkctpHFIHCI 947
Cdd:cd14882 527 FRA----TSLELLKMLS---IGAN-----------SGGT-----------------------------------HFVRCI 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 948 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEHLAAERCRLVLQQCKLQG 1027
Cdd:cd14882 554 RSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDF--DETVEMTKDNCRLLLIRLKMEG 631
|
730
....*....|.
gi 1622884521 1028 WQMGVRKVFLK 1038
Cdd:cd14882 632 WAIGKTKVFLK 642
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
320-1038 |
3.17e-81 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 282.75 E-value: 3.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAM-----LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLT 474
Cdd:cd14919 78 CTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 475 GARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLavlkQAL 554
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETM----EAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 555 NVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 634
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 635 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 714
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 715 LFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSMESNFPKKlqsLLESSNTNAVYSPLK 792
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEK---VVQEQGTHPKFQKPK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 793 DgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfrg 872
Cdd:cd14919 467 Q------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVA-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 873 hksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNS 952
Cdd:cd14919 532 --------GMSETALPGAFKT--------------------RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHE 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 953 KLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQCKLQG--WQM 1030
Cdd:cd14919 584 KKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRI 662
|
....*...
gi 1622884521 1031 GVRKVFLK 1038
Cdd:cd14919 663 GQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
320-1038 |
8.38e-81 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 281.57 E-value: 8.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAAS------------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFc 467
Cdd:cd15896 78 CTGESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 468 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKL 547
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 548 avlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 627
Cdd:cd15896 237 ----EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 628 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 707
Cdd:cd15896 313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 708 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLqsLLESSNTN 785
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKV--LQEQGTHP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 786 AVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsay 865
Cdd:cd15896 468 KFFKPKK-------LKDEAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 866 psfkfrghksalLSKKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIH 945
Cdd:cd15896 534 ------------LDKVSGMSEMPGAFKT--------------------RKGMFRTVGQLYKEQLSKLMATLRNTNPNFVR 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 946 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQCKL 1025
Cdd:cd15896 582 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMIKSLEL 660
|
730
....*....|....*
gi 1622884521 1026 QG--WQMGVRKVFLK 1038
Cdd:cd15896 661 DPnlYRIGQSKVFFR 675
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
321-999 |
2.10e-79 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 277.37 E-value: 2.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAA----------SSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErK 470
Cdd:cd14917 79 TGESGAGKTVNTKRVIQYFAVIAAigdrskkdqtPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA-T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 471 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREK 546
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-------NPYDYAFISQGETTVasidDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 547 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 626
Cdd:cd14917 231 LMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 627 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEK 706
Cdd:cd14917 311 EYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 707 MHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNT 784
Cdd:cd14917 387 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSNNF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 785 NavysplKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsa 864
Cdd:cd14917 466 Q------KPRNIKGKPEAH---FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 865 ypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFI 944
Cdd:cd14917 526 -----YAGADAPIEKGKGKAKK-------------------GSSFQ---------TVSALHRENLNKLMTNLRSTHPHFV 572
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884521 945 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 999
Cdd:cd14917 573 RCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
320-997 |
2.14e-79 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 278.90 E-value: 2.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-------FSSSGKLCSSLPPHLFSCVERAFHQLFQ 391
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqFGDRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 392 EQRPQCFILSGERGSGKSEASKQIIRH--LTCRAAS---------------SRAMLDSRFKHVMCILEAFGHAKTTLNDL 454
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYfaVHCGTGNnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 455 SSCFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDG----LSAEEKHGLHLN-NLCAHRYLNQ 529
Cdd:cd14899 161 SSRFGKFIELRFRDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSgGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 530 TMQDDVSTGERslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG--NSAFVSDLQLLEQVAG--- 604
Cdd:cd14899 241 SLCSKRRDGVK--DGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKgdDTVFADEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 605 -------MLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQ--------- 668
Cdd:cd14899 319 hftkaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 669 ----DEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQnGVLD 744
Cdd:cd14899 399 sdvdDEEDATDF--IGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNR-ACLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 745 FFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAVYSplkdgngNVALKDHGTAFTIMHYAGRVMYDVVGAI 824
Cdd:cd14899 476 LFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFR-------SAPLIQRTTQFVVAHYAGCVTYTIDGFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 825 EKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSAllsKKMTASsiigenknylelskllkkk 904
Cdd:cd14899 549 AKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRA---KSAIAA------------------- 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 905 gtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 984
Cdd:cd14899 607 --------------VSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFP 672
|
730
....*....|...
gi 1622884521 985 VRLSFSDFLSRYK 997
Cdd:cd14899 673 VRLTHKQFLGRYR 685
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
320-1038 |
3.38e-79 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 276.98 E-value: 3.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 320 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY---RGKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 471
Cdd:cd14930 78 CTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 472 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqTMQDDVSTG-ERSLNREKLavl 550
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGqERELFQETL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 551 kQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 630
Cdd:cd14930 232 -ESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 631 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 710
Cdd:cd14930 311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 711 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLQSllESSNTNAVY 788
Cdd:cd14930 388 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQ--EQGGHPKFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 789 SPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS-----KLSQTGSLVS 863
Cdd:cd14930 466 RPRH-------LRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 864 AYPSFKFRghksallskkmtassiigenknylelskllkkkgtstflqrleRGDPVTIASQLRKSLTDIIGKLQKCTPHF 943
Cdd:cd14930 538 GPPGGRPR-------------------------------------------RGMFRTVGQLYKESLSRLMATLSNTNPSF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 944 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQC 1023
Cdd:cd14930 575 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQAL 653
|
730
....*....|....*..
gi 1622884521 1024 KLQG--WQMGVRKVFLK 1038
Cdd:cd14930 654 ELDPnlYRVGQSKIFFR 670
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
326-1037 |
1.48e-77 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 270.83 E-value: 1.48e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 326 IQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERG 405
Cdd:cd14881 7 LQARFYAKEFFTNVGPILLSVNPYRDVG------NPLTLTSTRS--SPLAPQLLKVVQEAVRQQSETGYPQAIILSGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 406 SGKSEASKQIIRHLTCRAA---SSRAmldsrFKHV---MCILEAFGHAKTTLNDLSSCFIKYFELQFCErkQQLTGARIY 479
Cdd:cd14881 79 SGKTYASMLLLRQLFDVAGggpETDA-----FKHLaaaFTVLRSLGSAKTATNSESSRIGHFIEVQVTD--GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 480 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH--RYLNQtmqddvSTGERSLNREKLA--VLKQALN 555
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPAnlRYLSH------GDTRQNEAEDAARfqAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 556 VVGFSNLEVENlfvILAAILHLGDIRFTALTEGNSAFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 635
Cdd:cd14881 226 ILGIPFLDVVR---VLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 636 QIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLD--IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 713
Cdd:cd14881 302 NMSNMTRDALAKALYCRTVATIVRRANS-LKRLGSTLGTHATDgfIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 714 VLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESnFPKKLQslLESSNTNAVYSPlkd 793
Cdd:cd14881 381 HIFKSSIESCRDEGIQCEVEVDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTAES-YVAKIK--VQHRQNPRLFEA--- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 794 gngnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtsenvvinhlfqsklSQTGslvsaypSFKFRGH 873
Cdd:cd14881 455 ------KPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY---------------KQNC-------NFGFATH 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 874 ksallskkmtassiigenknylelskllkkkgTSTFLQRLErgdpvtiasqlrksltDIIGKLQKCTPHFIHCIRPNNSK 953
Cdd:cd14881 507 --------------------------------TQDFHTRLD----------------NLLRTLVHARPHFVRCIRSNTTE 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 954 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQ------- 1026
Cdd:cd14881 539 TPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILQFLEAQppsklss 618
|
730
....*....|....
gi 1622884521 1027 ---GWQMGVRKVFL 1037
Cdd:cd14881 619 vstSWALGKRHIFL 632
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
321-1038 |
3.47e-77 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 271.22 E-value: 3.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASS------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcE 468
Cdd:cd14912 79 TGESGAGKTVNTKRVIQYFATIAVTGekkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 469 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 544
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITT-------NPYDYPFVSQGEISVasidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 545 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 624
Cdd:cd14912 231 EELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 625 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 704
Cdd:cd14912 311 GNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 705 EKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 782
Cdd:cd14912 387 EKLQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 783 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLV 862
Cdd:cd14912 466 N----FQKPKVVKGKAE-----AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG--AQTAEGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 863 SAYPSFKFRGHKSAllskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 942
Cdd:cd14912 535 SAGGGAKKGGKKKG------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 943 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT------FLREKKehlAAERC 1016
Cdd:cd14912 576 FVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegqFIDSKK---ASEKL 652
|
730 740
....*....|....*....|..
gi 1622884521 1017 RLVLQQCKLQgWQMGVRKVFLK 1038
Cdd:cd14912 653 LASIDIDHTQ-YKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
321-1006 |
5.12e-77 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 270.39 E-value: 5.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAA-----------SSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 469
Cdd:cd14916 79 TGESGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 470 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NRE 545
Cdd:cd14916 158 TGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTN-------NPYDYAFVSQGEVSVasidDSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 546 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 625
Cdd:cd14916 231 ELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 626 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNE 705
Cdd:cd14916 311 NEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 706 KMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSN 783
Cdd:cd14916 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLydNHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 784 TNavysplKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqtgslVS 863
Cdd:cd14916 466 FQ------KPRNVKGKQEAH---FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-----AD 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 864 AYPSFKFRGHKSAllskkmtassiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHF 943
Cdd:cd14916 532 TGDSGKGKGGKKK-----------------------------GSSFQ---------TVSALHRENLNKLMTNLKTTHPHF 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884521 944 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1006
Cdd:cd14916 574 VRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 636
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
321-1006 |
1.10e-76 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 269.68 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASS------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcE 468
Cdd:cd14910 79 TGESGAGKTVNTKRVIQYFATIAVTGekkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 469 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 544
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITT-------NPYDYAFVSQGEITVpsidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 545 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 624
Cdd:cd14910 231 EELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 625 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 704
Cdd:cd14910 311 GNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 705 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 782
Cdd:cd14910 387 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 783 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLV 862
Cdd:cd14910 466 N----FQKPKPAKGKVE-----AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 863 SAYPSFKFRGhksallskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 942
Cdd:cd14910 537 GGKKGGKKKG----------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884521 943 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1006
Cdd:cd14910 574 FVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
321-1006 |
1.52e-75 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 266.21 E-value: 1.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRA---------ASSRAM---LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCE 468
Cdd:cd14915 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 469 rKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 544
Cdd:cd14915 159 -TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITT-------NPYDFAFVSQGEITVpsidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 545 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 624
Cdd:cd14915 231 EELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 625 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 704
Cdd:cd14915 311 GNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 705 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 782
Cdd:cd14915 387 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 783 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinHLFQSKLSQTgslv 862
Cdd:cd14915 466 N----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV------------GLYQKSGMKT---- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 863 sayPSFKFRGHKSAllSKKMTASSIIGENKNylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 942
Cdd:cd14915 521 ---LAFLFSGGQTA--EAEGGGGKKGGKKKG-------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884521 943 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1006
Cdd:cd14915 574 FVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
326-1038 |
5.36e-75 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 264.06 E-value: 5.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 326 IQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLC--SSLPPHLFSCVERAFHQLFQEQRPQCFILSG 402
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSRGfpSDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 403 ERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIYTYL 482
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL-LVGPDGGLKGGKITSYM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 483 LEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGErslNREKLAVLKQALNVVgFSNL 562
Cdd:cd14886 166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGID---DQKEFAPVRSQLEKL-FSKN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 563 EVENLFVILAAILHLGDIRFTALTEG---NSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 639
Cdd:cd14886 242 EIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 640 FFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVlFLH 718
Cdd:cd14886 322 VNIRAVAKDLYGALFELCVDTLNEIIQFDADARPW----IGILDIYGFEFFERNTYEQLLINYANERLQqYFINQV-FKS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 719 EQVECVQEGVTMETAYSPGNQNGVLdfFFQKPS-GFLTLLDEESQmiwsMESNFPKKLQSLLESSNTNAVYSPLKDGNGN 797
Cdd:cd14886 397 EIQEYEIEGIDHSMITFTDNSNVLA--VFDKPNlSIFSFLEEQCL----IQTGSSEKFTSSCKSKIKNNSFIPGKGSQCN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 798 valkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgslvsaypsfkfrghksal 877
Cdd:cd14886 471 ---------FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN----------------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 878 lskkMTASSIIGENKNYLelskllkkkgtSTFLqrlergdpvtiASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDT 957
Cdd:cd14886 513 ----KAFSDIPNEDGNMK-----------GKFL-----------GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 958 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL---ADTFLREKKEHLAAERCRLVLQQCKLQGWQMGVRK 1034
Cdd:cd14886 567 YETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTK 646
|
....
gi 1622884521 1035 VFLK 1038
Cdd:cd14886 647 VFLR 650
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
322-1038 |
1.59e-74 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 263.13 E-value: 1.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 322 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILS 401
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 402 GERGSGKSEASKQIIRHLTCRAASS----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 471
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGekkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 472 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREKL 547
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITT-------NPYDYAFVSQGEITVpsidDQEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 548 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 627
Cdd:cd14918 232 MATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 628 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 707
Cdd:cd14918 312 YVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 708 HHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNtn 785
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLydQHLGKSAN-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 786 avYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktseNVVINHLFQSKLSQTGSLVSAY 865
Cdd:cd14918 465 --FQKPKVVKGKAE-----AHFSLIHYAGTVDYNITGWLDKNKDPLN-----------DTVVGLYQKSAMKTLASLFSTY 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 866 PSFKfrGHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIH 945
Cdd:cd14918 527 ASAE--ADSGAKKGAKKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPHFVR 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 946 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT------FLREKKehlAAERCRLV 1019
Cdd:cd14918 574 CIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASaipegqFIDSKK---ASEKLLAS 650
|
730
....*....|....*....
gi 1622884521 1020 LQQCKLQgWQMGVRKVFLK 1038
Cdd:cd14918 651 IDIDHTQ-YKFGHTKVFFK 668
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
321-1000 |
5.11e-74 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 261.32 E-value: 5.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRP--QC 397
Cdd:cd14880 2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQP--QKLKPHIFTVGEQTYRNVKSLIEPvnQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 398 FILSGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcER 469
Cdd:cd14880 80 IVVSGESGAGKTWTSRCLMKFYAVVAASPTSWeshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL-NR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 470 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqddvstgERSLNREKLAV 549
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP--------ERNLEEDCFEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 550 LKQALNVVGFSNLEVENLFVILAAILHLGDIRFTA---------LTEGNSAFVSDLQLLeqvagmLQVSTDELASALTT- 619
Cdd:cd14880 231 TREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADsedeaqpcqPMDDTKESVRTSALL------LKLPEDHLLETLQIr 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 620 DIQYFKGDMIIRRHTIQI-AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDeqrSMQTLDIGILDIFGFEEFQKNEFEQL 698
Cdd:cd14880 305 TIRAGKQQQVFKKPCSRAeCDTRRDCLAKLIYARLFDWLVSVINSSICADT---DSWTTFIGLLDVYGFESFPENSLEQL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 699 CVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsMESNFPKKLQS 777
Cdd:cd14880 382 CINYANEKLqQHFVAHYL-RAQQEEYAVEGLEWSFINYQDNQT-CLDLIEGSPISICSLINEECRL---NRPSSAAQLQT 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 778 LLESSNTNavySPLKdGNGNVALKdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsq 857
Cdd:cd14880 457 RIESALAG---NPCL-GHNKLSRE---PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN--- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 858 tgslvsaypsfkfrghksallSKKMTASSIIGENknylelskllkkkgtstflqrleRGDPVTIASQLRKSLTDIIGKLQ 937
Cdd:cd14880 527 ---------------------PEEKTQEEPSGQS-----------------------RAPVLTVVSKFKASLEQLLQVLH 562
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884521 938 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1000
Cdd:cd14880 563 STTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
321-1006 |
1.06e-72 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 257.69 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 400
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASS-----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 469
Cdd:cd14923 79 TGESGAGKTVNTKRVIQYFATIAVTGdkkkeqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 470 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NRE 545
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIST-------NPFDFPFVSQGEVTVasidDSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 546 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 625
Cdd:cd14923 231 ELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 626 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNE 705
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 706 KMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSN 783
Cdd:cd14923 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 784 tnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvS 863
Cdd:cd14923 466 ----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-----------S 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 864 AYpsfkfrghksallskkmtASSIIGENknylelskllkkkGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQKCTPHF 943
Cdd:cd14923 526 NY------------------AGAEAGDS-------------GGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHF 574
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884521 944 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1006
Cdd:cd14923 575 VRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
321-1002 |
6.95e-71 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 249.81 E-value: 6.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsslpPHLFSCVERAFHQLFQEQRpQCFIL 400
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE------PHVYDVAEASVQDLLVHGN-QTIVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcerKQQLTGARIYT 480
Cdd:cd14898 75 SGESGSGKTENAKLVIKYLVERTASTTS-IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF---DGKITGAKFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 481 YLLEKSRLVSQPLGQSNFLIFSLLmdglsaeekhglhlnnlCAHRYLNQTmQDDVSTGERSLNREKLAVLKQ-------A 553
Cdd:cd14898 151 YLLEKSRVTHHEKGERNFHIFYQF-----------------CASKRLNIK-NDFIDTSSTAGNKESIVQLSEkykmtcsA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 554 LNVVGFSNL-EVENLfviLAAILHLGDIRFTalTEGNSAFVSDlQLLEQVAGMLQVSTDELASALTT-DIQYfKGDMIIR 631
Cdd:cd14898 213 MKSLGIANFkSIEDC---LLGILYLGSIQFV--NDGILKLQRN-ESFTEFCKLHNIQEEDFEESLVKfSIQV-KGETIEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 632 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEqrsmqtLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 711
Cdd:cd14898 286 FNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGE------RSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 712 NEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDffFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLessntnavyspl 791
Cdd:cd14898 360 IKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRD--FEKPCGLMDLISEESFNAWGNVKNLLVKIKKYL------------ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 792 kdgNGNVALKdHGTAFTIMHYAGRVMYDVVGAIEKNKDSlsqnllfvmktsenvvinhlfqsklsqtGSLvsaypsfkfR 871
Cdd:cd14898 426 ---NGFINTK-ARDKIKVSHYAGDVEYDLRDFLDKNREK----------------------------GQL---------L 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 872 GHKSALLSKKMTASSIIGENKNylelskllkkkgtstflqrlergdpvtiasqlrkSLTDIIGKLQKCTPHFIHCIRPNN 951
Cdd:cd14898 465 IFKNLLINDEGSKEDLVKYFKD----------------------------------SMNKLLNSINETQAKYIKCIRPNE 510
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622884521 952 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT 1002
Cdd:cd14898 511 ECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
333-1006 |
2.40e-70 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 252.26 E-value: 2.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 333 NQIYTFIGDILLLVNPYKELPIYS-SMVSQLYFSSSgklcSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGKSEA 411
Cdd:cd14887 22 NCIYTYTGTLLIAVNPYRFFNLYDrQWISRFDTEAN----SRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTET 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 412 SKQIIRHLTC----RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKqQLTGARIYTYLLEKSR 487
Cdd:cd14887 98 SKHVLTYLAAvsdrRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG-KLTRASVATYLLANER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 488 LVSQPLGQSNFLIFSllmdglsaeekhglhlnNLCAHRYLNQTMqdDVSTGERSLNREKLAVLKQALNVVGFSNLEVENL 567
Cdd:cd14887 177 VVRIPSDEFSFHIFY-----------------ALCNAAVAAATQ--KSSAGEGDPESTDLRRITAAMKTVGIGGGEQADI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 568 FVILAAILHLGDIRFTALTE--------------GNSAFVSDL-QLLE--------QVAGMLQVSTDELASALTTDIQYF 624
Cdd:cd14887 238 FKLLAAILHLGNVEFTTDQEpetskkrkltsvsvGCEETAADRsHSSEvkclssglKVTEASRKHLKTVARLLGLPPGVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 625 KGDMI-----IRR-------HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL----------LSQDEQRSMQTLDIGIL 682
Cdd:cd14887 318 GEEMLrlalvSRSvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdSDEDTPSTTGTQTIGIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 683 DIFGFEEFQ---KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVL-DFFFQKPSGFLTLLD 758
Cdd:cd14887 398 DLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLaSTLTSSPSSTSPFSP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 759 EESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGNGNV----------------------ALKDHGTAFTIMHYAGRV 816
Cdd:cd14887 478 TPSFRSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSdlfyeklnkniinsakyknitpALSRENLEFTVSHFACDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 817 MYDVVGAIEKNKDSLSQNLlfvmktsenvvinhlfqsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKNyle 896
Cdd:cd14887 558 TYDARDFCRANREATSDEL---------------------------------------ERLFLACSTYTRLVGSKKN--- 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 897 lskllkkKGTSTFLQRLErgdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMV 976
Cdd:cd14887 596 -------SGVRAISSRRS-----TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663
|
730 740 750
....*....|....*....|....*....|
gi 1622884521 977 KIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1006
Cdd:cd14887 664 RVMADGFPCRLPYVELWRRYETKLPMALRE 693
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
322-999 |
2.31e-69 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 246.71 E-value: 2.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 322 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgklcsslppHLFSCVERAFHQLFQ-EQRPQCFIL 400
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC-------------HISGVAENALDRIKSmSSNAESIVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 401 SGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARI-Y 479
Cdd:cd14874 70 GGESGSGKSYNAFQVFKYLT--SQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLkY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 480 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-----TMQDDVstgerslnrEKLAVLKQAL 554
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQgnsteNIQSDV---------NHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 555 NVVGFSNLEVENLFVILAAILHLGDIRFTAL----TEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQyfKGDMIi 630
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTKrnpnVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSE--DGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 631 rrhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdeQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 710
Cdd:cd14874 294 ---DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL-----KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 711 INEVLFLHEQVECVQEGVTMETAYSPGNQNG-VLDFFFQKPSGFLTLLDEESQmiwsmesnFPK-KLQSLLESSNTNAVY 788
Cdd:cd14874 366 FVKHSFHDQLVDYAKDGISVDYKVPNSIENGkTVELLFKKPYGLLPLLTDECK--------FPKgSHESYLEHCNLNHTD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 789 splKDGNGNVALKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVsaypsf 868
Cdd:cd14874 438 ---RSSYGKARNKER-LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMI------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 869 kfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIR 948
Cdd:cd14874 508 --------------------------------------------------VSQAQFILRGAQEIADKINGSHAHFVRCIK 537
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622884521 949 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 999
Cdd:cd14874 538 SNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
321-997 |
4.58e-66 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 238.65 E-value: 4.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS----LPPHLFSCVERAFHQLFQEQRP 395
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAASaapfPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 396 QCFILSGERGSGKSEASKQIIRHLT-CRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQ-- 472
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHyIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTqk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 473 ------LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL--------NQTMQDDVSTG 538
Cdd:cd14884 162 nmfngcFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLlnpdeshqKRSVKGTLRLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 539 ERSLNREKLAVLK---------QALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAgMLQVS 609
Cdd:cd14884 242 SDSLDPSEEEKAKdeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKAAAECLQIEEEDLENVIKYK-NIRVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 610 TDelasalttdiqyfkgdmIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLD--------IG 680
Cdd:cd14884 321 HE-----------------VIRTErRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDiysineaiIS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 681 ILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVLFlHEQVECVQEGVTMETAYSPgNQNGVLDFffqkPSGFLTLLDE 759
Cdd:cd14884 384 ILDIYGFEELSGNDFDQLCINLANEKLNnYYINNEIE-KEKRIYARENIICCSDVAP-SYSDTLIF----IAKIFRRLDD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 760 ESQM-----------IWSMESNFPKKLQslLESSNTNAVYSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNK 828
Cdd:cd14884 458 ITKLknqgqkktddhFFRYLLNNERQQQ--LEGKVSYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 829 DSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrghksallskkmtasSIIGENKNYLelskllkkkgtst 908
Cdd:cd14884 536 DKIETSIETLISCSSNRFLRE------------------------------------ANNGGNKGNF------------- 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 909 flqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 988
Cdd:cd14884 567 ----------LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
....*....
gi 1622884521 989 FSDFLSRYK 997
Cdd:cd14884 637 KKETAAALK 645
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
321-996 |
1.00e-65 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 237.30 E-value: 1.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcssLPPHLFSCVERAFHQLFQEQRPQCFI 399
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRG-----LPPHLFALAAKAISDMQDFRRDQLIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 400 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIY 479
Cdd:cd14905 77 IGGESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEM-FYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 480 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVST--GERSLNReklavLKQALNVV 557
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDR-----LKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 558 GFSNLEVENLFVILAAILHLGDIRFtaLTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDiqyfkgdmiiRRHTIQI 637
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTF--FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 638 AEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdeQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 717
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL-----KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 718 HEQVECVQEGVTMETAYS-PGNQNGVldfffQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTnavysplkdgng 796
Cdd:cd14905 374 QEQREYQTERIPWMTPISfKDNEESV-----EMMEKIINLLDQESKNINSSDQIFLEKLQNFLSRHHL------------ 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 797 nvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtseNVVINHLFQS----KLSQTGSLVSAYPSFKFRG 872
Cdd:cd14905 437 ---FGKKPNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHK---NSITKYLFSRdgvfNINATVAELNQMFDAKNTA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 873 HKSALLSKK--MTASSIIGENKNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDiigklQKCTPHFIHCIRPN 950
Cdd:cd14905 511 KKSPLSIVKvlLSCGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINN-----SNCDFHFIRCIKPN 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1622884521 951 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 996
Cdd:cd14905 586 SKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRF 631
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
321-1038 |
3.74e-63 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 229.89 E-value: 3.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgKLCSS--LPPHLFSCVERAFHQLFQEQRPQCF 398
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMF-----KGCRRedMPPHIYASAQSAYRAMLMSRRDQSI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 399 ILSGERGSGKSEASKQIIRHLTCRAASS---------RAMLDsrfkhvmcILEAFGHAKTTLNDLSSCFIKYFELQFcER 469
Cdd:cd01386 77 VLLGRSGSGKTTNCRHILEYLVTAAGSVggvlsveklNAALT--------VLEAFGNVRTALNGNATRFSQLFSLDF-DQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 470 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLC--AHRYLNQTM-QDDVSTGERSLNRek 546
Cdd:cd01386 148 AGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAesNSFGIVPLQkPEDKQKAAAAFSK-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 547 lavLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASAL--------- 617
Cdd:cd01386 226 ---LQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 618 ---TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeQRSMQTldIGILDIFGFE--EFQK 692
Cdd:cd01386 303 qqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSS--HHSTSS--ITIVDTPGFQnpAHSG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 693 NE----FEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPS--------------GFL 754
Cdd:cd01386 379 SQrgatFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedrrGLL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 755 TLLDEESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGngnvalkDHGTAFTIMHYAGR--VMYDVVGaieknkdsls 832
Cdd:cd01386 459 WLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRS-------EGPLQFVLGHLLGTnpVEYDVSG---------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 833 qnllFVMKTSENVvinhlfqSKLSQTGSLVSaypsfkfrghksallSKKMTAssiiGENKNYlelskllkkkgtstflqr 912
Cdd:cd01386 522 ----WLKAAKENP-------SAQNATQLLQE---------------SQKETA----AVKRKS------------------ 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 913 lergdpvtIASQLRKSLTDIIGKLQKCTPHFIHCIRPN------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFR 980
Cdd:cd01386 554 --------PCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkderstssPAAGDELLDVPLLRSQLRGSQLLDALRLYR 625
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884521 981 YGYPVRLSFSDFLSRYKPLADTFLRE-------KKEHLAAERcrlVLQQCKLQ--GWQMGVRKVFLK 1038
Cdd:cd01386 626 QGFPDHMPLGEFRRRFQVLAPPLTKKlglnsevADERKAVEE---LLEELDLEksSYRIGLSQVFFR 689
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
322-997 |
1.32e-59 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 220.61 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 322 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKL-------CSSLPPHLFSCVERAFHQLFQEQR 394
Cdd:cd14893 3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 395 PQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDS------------RFKHVMCILEAFGHAKTTLNDLSSCFIKYF 462
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSegasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 463 ELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEE--KHGLHLNNLCAHRYLNQTMQDDVstGER 540
Cdd:cd14893 163 SVEF-SKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNKCVNEFVMLKQADPLA--TNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 541 SLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG-------NSAFVSDLQ--------LLEQVAGM 605
Cdd:cd14893 240 ALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGgksvggaNSTTVSDAQscalkdpaQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 606 LQVSTDELASALTTDiQYFKGD-----MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL---LSQDEQRSM--Q 675
Cdd:cd14893 320 LEVEPVVLDNYFRTR-QFFSKDgnktvSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggiFDRYEKSNIviN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 676 TLDIGILDIFGFEEF--QKNEFEQLCVNMTNEKMHH-YINEVL-----FLHEQVECVQEGVTMETAYS-PGNQNGVLDFF 746
Cdd:cd14893 399 SQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHfYVQNTLainfsFLEDESQQVENRLTVNSNVDiTSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 747 FQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLE-----------SSNTNAVYSPLKDGNgnvalkdhgTAFTIMHYAGR 815
Cdd:cd14893 479 EDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEavgglsrpnmgADTTNEYLAPSKDWR---------LLFIVQHHCGK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 816 VMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAyPSFKFRGHKSALLSKKMTASSiigENKNyl 895
Cdd:cd14893 550 VTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAA-KQTEERGSTSSKFRKSASSAR---ESKN-- 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 896 elskllkkKGTSTFLQRLERGDPVTIAsqlrksltdiigkLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEM 975
Cdd:cd14893 624 --------ITDSAATDVYNQADALLHA-------------LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVEL 682
|
730 740
....*....|....*....|..
gi 1622884521 976 VKIFRYGYPVRLSFSDFLSRYK 997
Cdd:cd14893 683 MQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
329-1038 |
9.03e-59 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 215.65 E-value: 9.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 329 RFGNNQIYTFIGDILLLVNPYKELPIYSSmvsqlyfSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGK 408
Cdd:cd14937 10 RYKKNYIYTIAEPMLISINPYQVIDVDIN-------EYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGSGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 409 SEASKQIIRHLTCRAAS----SRAMLDSRFkhvmcILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGARIYTYLLE 484
Cdd:cd14937 83 TEASKLVIKYYLSGVKEdneiSNTLWDSNF-----ILEAFGNAKTLKNNNSSRYGKYIKIELDEY-QNIVSSSIEIFLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 485 KSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL-NQTMQ----DDVSTGER---SLNREKLAVLKqalnv 556
Cdd:cd14937 157 NIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIvNKNVVipeiDDAKDFGNlmiSFDKMNMHDMK----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 557 vgfsnlevENLFVILAAILHLGDIRFTALTEGNSAFVSDL-----QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 631
Cdd:cd14937 232 --------DDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELdknnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 632 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 711
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNY----IGILDIFGFEIFSKNSLEQLLINIANEEIHSIY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 712 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfffqkpsgfltLLDEESQMIWSMESNF--PKKLQSLLESSNTNAvYS 789
Cdd:cd14937 380 LYIVYEKETELYKAEDILIESVKYTTNES-IID-----------LLRGKTSIISILEDSClgPVKNDESIVSVYTNK-FS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 790 plKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkLSQTGSLvsaypsfk 869
Cdd:cd14937 447 --KHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-VEVSESL-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 870 frGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLTDIIGKLQKCTPHFIHCIRP 949
Cdd:cd14937 516 --GRKNLITFKYL--------------------------------------------KNLNNIISYLKSTNIYFIKCIKP 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 950 NNSKLPDTFDNFYVSAQLQYIGVLEMVKI---FRYGYpvrlSFSDFLSRYKPL-----ADTFLREKkehlaaERCRLVLQ 1021
Cdd:cd14937 550 NENKEKNNFNQKKVFPQLFSLSIIETLNIsffFQYKY----TFDVFLSYFEYLdystsKDSSLTDK------EKVSMILQ 619
|
730
....*....|....*...
gi 1622884521 1022 Q-CKLQGWQMGVRKVFLK 1038
Cdd:cd14937 620 NtVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
321-1037 |
8.75e-40 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 159.62 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 321 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgkLCSSLPPHL----FSCVERAFHQLFQEQRPQ 396
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY------KCIDCIEDLslneYHVVHNALKNLNELKRNQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 397 CFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSR-----------------------FKHVMCILEAFGHAKTTLND 453
Cdd:cd14938 76 SIIISGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLndqeednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 454 LSSCFIKYFELQFceRKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNqtmqD 533
Cdd:cd14938 156 NSSRFSKFCTIHI--ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLN----N 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 534 DVSTGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF---------------VSDLQL 598
Cdd:cd14938 230 EKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLmgknqcgqninyetiLSELEN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 599 LEQVAGMLQVSTDELASAL-----TTDIQYFKGDMI------IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNsCLLS 667
Cdd:cd14938 310 SEDIGLDENVKNLLLACKLlsfdiETFVKYFTTNYIfndsilIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 668 QDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFF 747
Cdd:cd14938 389 QLQNININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 748 QKPSGFL-TLLDEESQMIWSMESNFpkkLQSLLESSNTNAVYSPLKDGNGNvalkdhGTAFTIMHYAGRVMYDVVGAIEK 826
Cdd:cd14938 469 GPTEGSLfSLLENVSTKTIFDKSNL---HSSIIRKFSRNSKYIKKDDITGN------KKTFVITHSCGDIIYNAENFVEK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 827 NKDSLSQNLLFVMKTSENVVINHLFQsklsqtgslvsaypSFKFRghksallskkmTASSIIGENKNYLELSKLlkkkgt 906
Cdd:cd14938 540 NIDILTNRFIDMVKQSENEYMRQFCM--------------FYNYD-----------NSGNIVEEKRRYSIQSAL------ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 907 STFLQRLERGDPVTIaSQLRKSLTDIIGKLQKCTPHFIHCIRPNNSK-LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 985
Cdd:cd14938 589 KLFKRRYDTKNQMAV-SLLRNNLTELEKLQETTFCHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPH 667
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1622884521 986 RLSFSDFLSRYKpladtflreKKEHLAAERCRLVLQQCKL--QGWQMGVRKVFL 1037
Cdd:cd14938 668 KFTLNEFLSIFD---------IKNEDLKEKVEALIKSYQIsnYEWMIGNNMIFL 712
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-219 |
3.35e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 148.56 E-value: 3.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 6 ARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyl 85
Cdd:COG0666 95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA------------ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 86 dENGVDLtslrqmklqrpmsmltdVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLH 165
Cdd:COG0666 163 -NGNLEI-----------------VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622884521 166 LAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAASEFIEEMLLKAEIAWEEK 219
Cdd:COG0666 225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-238 |
3.62e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 148.18 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 6 ARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyl 85
Cdd:COG0666 62 ALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY------------ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 86 dENGVDLtslrqmklqrpmsmltdVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLH 165
Cdd:COG0666 130 -NGNLEI-----------------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884521 166 LAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAASEF---IEEMLLKAEIAWEEKMKEPLSVSTLAQEEPYEEI 238
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGnleIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
440-1006 |
2.42e-23 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 107.91 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 440 ILEAFGHAKTTLNDLSSCFIKYFELQFC----ERKQQLTGARIYTYLLEKSRLVSQPLGQS------NFLIFSLLMDGLS 509
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVAfglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 510 AEE-----KHGLHLNNL-CA---------HRYLNQTMQDDvsTGERSLNREKLAVlkQALNVVGFSNLEVENLFVILAAI 574
Cdd:cd14894 335 AFPfmrllAKELHLDGIdCSaltylgrsdHKLAGFVSKED--TWKKDVERWQQVI--DGLDELNVSPDEQKTIFKVLSAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 575 LHLGDIRFTALTEGNSAFVSD---LQLLEQVAGMLQV-STDELASALTTDIQYFKGDMIIRRHTIQIAEF--FRDLLAKS 648
Cdd:cd14894 411 LWLGNIELDYREVSGKLVMSStgaLNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVnhVRDTLARL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 649 LYSRLFSFLVNTMNSCL----LSQDEQRSMQTLD---------IGILDIFGFEEFQKNEFEQLCVNMTNEKMhhYINEvl 715
Cdd:cd14894 491 LYQLAFNYVVFVMNEATkmsaLSTDGNKHQMDSNasapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKL--YARE-- 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 716 flhEQVecvqegvtMETAYSP-------GNQNGVLdFFFQKPSGF------LTLLDEESQMIWSMESNFPKKLQSLLESS 782
Cdd:cd14894 567 ---EQV--------IAVAYSSrphltarDSEKDVL-FIYEHPLGVfasleeLTILHQSENMNAQQEEKRNKLFVRNIYDR 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 783 NTNAVYSP---LKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvviNHLfqSKLSQTG 859
Cdd:cd14894 635 NSSRLPEPprvLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNS---SHF--CRMLNES 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 860 SLVSAYPSfkfrghksallskkmTASSIIGENKNylelskllKKKGTSTFLqrlergdpvtiaSQLRKSLTDIIGKLQKC 939
Cdd:cd14894 710 SQLGWSPN---------------TNRSMLGSAES--------RLSGTKSFV------------GQFRSHVNVLTSQDDKN 754
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884521 940 TPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG----YPVRLSFSDFLSRYKPLadtfLRE 1006
Cdd:cd14894 755 MPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSsssySAIDISKSTLLTRYGSL----LRE 821
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
7-209 |
1.31e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 99.74 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 7 RYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACAC-----DNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSIL 81
Cdd:PHA03100 44 EARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 82 LTYLDENGVDLTSLR-------QMKLQRPMSMLTDVKHFLSSGGNVNEKNdegvtllhmacasgykeVVSLILEHGGDLN 154
Cdd:PHA03100 124 VEYLLDNGANVNIKNsdgenllHLYLESNKIDLKILKLLIDKGVDINAKN-----------------RVNYLLSYGVPIN 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884521 155 IVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAASEFIEEML 209
Cdd:PHA03100 187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
346-464 |
4.99e-20 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 88.94 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 346 VNPYKELPIYSSmvSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAAS 425
Cdd:cd01363 5 VNPFKELPIYRD--SKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFN 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622884521 426 SRAMLDSRFK---------------HVMCILEAFGHAKTTLNDLSSCFIKYFEL 464
Cdd:cd01363 83 GINKGETEGWvylteitvtledqilQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
45-212 |
8.61e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 88.86 E-value: 8.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 45 DIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLRQMKLQRPMSMLTDVKHFLSSGGNVNEKN 124
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 125 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAASE- 203
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANg 164
|
170
....*....|.
gi 1622884521 204 FIE--EMLLKA 212
Cdd:COG0666 165 NLEivKLLLEA 175
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
110-190 |
6.64e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 110 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHgGDLNIVDDQyWTPLHLAAKYGQANLVKLLLMHQANPHLV 189
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90
|
.
gi 1622884521 190 N 190
Cdd:pfam12796 91 D 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
6-164 |
2.17e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 84.62 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 6 ARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyl 85
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE------------ 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884521 86 dengvdltslrqmklqrpMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPL 164
Cdd:COG0666 229 ------------------NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
8-184 |
6.47e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 83.57 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 8 YDNAFIaEILIDRGVNVNHQDEDFWTPMHIACACD-NPDIVLLLVLAGANVLLQDVNGNIPLDYAveGTESSSILLTYLD 86
Cdd:PHA02876 319 YDTENI-RTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA--AVRNNVVIINTLL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 87 ENGVDLTSLRQmKLQRPMSM-------LTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYK-EVVSLILEHGGDLNIVDD 158
Cdd:PHA02876 396 DYGADIEALSQ-KIGTALHFalcgtnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINI 474
|
170 180
....*....|....*....|....*.
gi 1622884521 159 QYWTPLHLAAKYgqANLVKLLLMHQA 184
Cdd:PHA02876 475 QNQYPLLIALEY--HGIVNILLHYGA 498
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
9-196 |
9.31e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.85 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 9 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVllQDVNGNIPLDYAVEGTESSSILLTYLDEN 88
Cdd:PHA02874 13 DIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADI--NHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 89 GVDLTSLRQMKLQRPMsmltdVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAA 168
Cdd:PHA02874 91 GVDTSILPIPCIEKDM-----IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
|
170 180
....*....|....*....|....*...
gi 1622884521 169 KYGQANLVKLLLMHQANPHLVNCNEEKP 196
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
6-190 |
1.23e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 75.45 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 6 ARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMH--IACACDN-PDIVLLLVLAGANVLLQDVNGNIPLDYavegtesssi 80
Cdd:PHA03095 20 LNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCGFTPLHL---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 81 lltYLdENGvdlTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKNDEGVTLLHmACASGY---KEVVSLILEHGGDLNIVD 157
Cdd:PHA03095 90 ---YL-YNA---TTLDVIKL------------LIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALD 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1622884521 158 DQYWTPLHLAAKYGQAN--LVKLLLMHQANPHLVN 190
Cdd:PHA03095 150 LYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVD 184
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
7-192 |
2.43e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.23 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 7 RYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLqdvngnIPLDyAVEGTESSSILLTYLD 86
Cdd:PHA02874 44 RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIP-CIEKDMIKTILDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 87 ENGVDLTSLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHL 166
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180
....*....|....*....|....*.
gi 1622884521 167 AAKYGQANLVKLLLMHQANPhLVNCN 192
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHI-MNKCK 221
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
9-159 |
3.03e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.93 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 9 DNAFIAEILIDRGVNVNHQDEDFWTPMHIA-CACDN-PDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLD 86
Cdd:PHA03100 84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKSNsYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 87 ENGVDLTSLRQMKLQRPMSMLTD---------------------VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSL 145
Cdd:PHA03100 164 DKGVDINAKNRVNYLLSYGVPINikdvygftplhyavynnnpefVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
|
170
....*....|....
gi 1622884521 146 ILEHGGDLNIVDDQ 159
Cdd:PHA03100 244 LLNNGPSIKTIIET 257
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
131-182 |
2.01e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 2.01e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1622884521 131 LHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMH 182
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
127-180 |
1.20e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.14 E-value: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884521 127 GVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLL 180
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
10-189 |
2.21e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 68.13 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 10 NAFIAEILIDRGVNVNHQDEDFWTPMHI-----ACacdNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTY 84
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLAVllksrNA---NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 85 LDENGVDLTSLRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVD 157
Cdd:PHA03095 208 LIRAGCDPAATDMLGNTPLHSMATgssckrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287
|
170 180 190
....*....|....*....|....*....|..
gi 1622884521 158 DQYWTPLHLAAKYGQANLVKLLLMHQANPHLV 189
Cdd:PHA03095 288 SDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
13-208 |
8.57e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.44 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 13 IAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILltyldengvdl 92
Cdd:PHA02878 183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDIL----------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 93 tslrqmklqrpmsmltdvKHFLSSGGNVNEKND-EGVTLLHMACASgyKEVVSLILEHGGDLNIVDDQYWTPLHLAAK-Y 170
Cdd:PHA02878 252 ------------------KLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqY 311
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622884521 171 GQANLVKLLLMHqanphlVNCNEEKPSDIAASE-FIEEM 208
Cdd:PHA02878 312 LCINIGRILISN------ICLLKRIKPDIKNSEgFIDNM 344
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
17-215 |
9.34e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.14 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 17 LIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtESSSILLTYLDENGVDLtSLR 96
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK--HNFFDIIKLLLEKGAYA-NVK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 97 QMKLQRPMSMLTD------VKHFLSSGGNVNEKNDEGVTLLHMACAsgYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKY 170
Cdd:PHA02874 187 DNNGESPLHNAAEygdyacIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINP 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622884521 171 G-QANLVKLLLMHQANPHLVNCNEEKPSDIAASEFIEEMLLKAEIA 215
Cdd:PHA02874 265 PcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIA 310
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
9-201 |
1.48e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 66.24 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 9 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSI-------- 80
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaiidnrs 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 81 ---------------------LLTYldENGVDLTSLRQMK-------LQRPmSMLTDVKHFLSSGGNVNEKNDEGVTLLH 132
Cdd:PHA02876 236 ninkndlsllkairnedletsLLLY--DAGFSVNSIDDCKntplhhaSQAP-SLSRLVPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884521 133 MACASGY-KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQ-ANLVKLLLMHQANPHLVNCNEEKPSDIAA 201
Cdd:PHA02876 313 LMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAA 383
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
5-157 |
3.14e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.59 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 5 CARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLvlaganvllqdvngnipLDYAvegtesssillty 84
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-----------------LEHA------------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884521 85 ldengvdltslrqmklqrpmsmltdvkhflssggNVNEKnDEGVTLLHMACASGYKEVVSLILEHGGDLNIVD 157
Cdd:pfam12796 54 ----------------------------------DVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1275-1552 |
1.92e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.03 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1275 RPGDARPPGAPGTAARVLTPGTPQCALPPatPPG--------DEDDGEPVYIEML--------------GHPARPDSPD- 1331
Cdd:PHA03247 2482 RPAEARFPFAAGAAPDPGGGGPPDPDAPP--APSrlapailpDEPVGEPVHPRMLtwirgleelasddaGDPPPPLPPAa 2559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1332 ----PGESVYEEMkcCLPDDGGPGAGSflRASPPllhGAPEDEAAGP-PGDMCDIP--PPFPNLLPHRPPllvfPPTPVT 1404
Cdd:PHA03247 2560 ppaaPDRSVPPPR--PAPRPSEPAVTS--RARRP---DAPPQSARPRaPVDDRGDPrgPAPPSPLPPDTH----APDPPP 2628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1405 CSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSP-------LSPQYSKSQKGDGDRPASPGLALFNGSGRASPPStpp 1477
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP--- 2705
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884521 1478 ppppgPPPAPFRPCAHLAFPPEPAPVSLGKAGPSTEAPKVHPKPNSA---PGAGSCSSFPKIPYSPVKAARVDARKAG 1552
Cdd:PHA03247 2706 -----PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpatPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
10-211 |
7.85e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 60.28 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 10 NAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLV-------LAGANVLLQDV--NGNIPLdyavegteSSSI 80
Cdd:PHA02878 49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrsinkcsVFYTLVAIKDAfnNRNVEI--------FKII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 81 LLTYLDEN-GVDLTSLRQMKLQRPMSMLTdVKHFLSSGGNVNEKN-DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDD 158
Cdd:PHA02878 121 LTNRYKNIqTIDLVYIDKKSKDDIIEAEI-TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622884521 159 QYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAASEFIEEMLLK 211
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILK 252
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
17-71 |
1.13e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 52.73 E-value: 1.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884521 17 LIDRG-VNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYA 71
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
110-187 |
1.64e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 1.64e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884521 110 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPH 187
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
17-185 |
2.35e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 58.92 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 17 LIDRGVNVNHQDedfwtpMHIACACDNPDI--VLLLVLAGANVLLQDVNGNIPLDYAVEgTESSSILLTYLDENGVDLTS 94
Cdd:PHA02876 230 IIDNRSNINKND------LSLLKAIRNEDLetSLLLYDAGFSVNSIDDCKNTPLHHASQ-APSLSRLVPKLLERGADVNA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 95 lRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKNDEGVTLLHMACA-SGYKEVVSLILEHGGDLNIVDDQYWTPLHL 166
Cdd:PHA02876 303 -KNIKGETPLYLMAkngydteNIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHY 381
|
170
....*....|....*....
gi 1622884521 167 AAKYGQANLVKLLLMHQAN 185
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGAD 400
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1238-1529 |
4.25e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1238 PRPHSDDYStmkkIPPRKPKRSPNTKLSGSYEEISGSRPGDARP--PGAPGTAARVLTPGTPqcaLPPATPPGDEDDGEP 1315
Cdd:PHA03247 2559 APPAAPDRS----VPPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSP 2631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1316 vyiemlghPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLR-----ASPPLLHGAPED-------EAAGPPGDMCDIPP 1383
Cdd:PHA03247 2632 --------SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRrarrlGRAAQASSPPQRprrraarPTVGSLTSLADPPP 2703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1384 PFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDRPASPGLAL 1463
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL 2783
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884521 1464 FNGSGRA---------SPPSTPPPPPPGPPPAPFRPCAHLAFPPEPAPVSLGKAGPSTEAPkvhPKPNSAPGAGS 1529
Cdd:PHA03247 2784 TRPAVASlsesreslpSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG---PPPPSLPLGGS 2855
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
13-171 |
4.29e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 57.73 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 13 IAEILIDRGVNVNHQDEDFWTPMHI-ACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVD 91
Cdd:PHA03095 65 IVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPKVIRLLLRKGAD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 92 LTSlRQMKLQRPMSMLTD--------VKHFLSSGGNVNEKNDEGVTLLHMACAS--GYKEVVSLILEHGGDLNIVDDQYW 161
Cdd:PHA03095 145 VNA-LDLYGMTPLAVLLKsrnanvelLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGN 223
|
170
....*....|
gi 1622884521 162 TPLHLAAKYG 171
Cdd:PHA03095 224 TPLHSMATGS 233
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
13-165 |
1.63e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 56.46 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 13 IAEILIDRGVNVNHQDEDFWTPMHIACACDN--PDIVLLLVLAGANVLLQDVNGNIP-LDYAVE----GTESSSILLTYL 85
Cdd:PHA02716 194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPiMTYIINidniNPEITNIYIESL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 86 DENGVD-----LTSLRQMKLQRPMSMltdVKHFLSSGGNVNEKNDEGVTLLHMACASGY--KEVVSLILEHGGDLNIVDD 158
Cdd:PHA02716 274 DGNKVKnipmiLHSYITLARNIDISV---VYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDN 350
|
....*..
gi 1622884521 159 QYWTPLH 165
Cdd:PHA02716 351 IGNTVLH 357
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
119-167 |
2.83e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 2.83e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622884521 119 NVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLA 167
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
35-202 |
3.57e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 35 MHIACACD-----NPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILL-----TYLDENGVDLTSLRQMKLQRpm 104
Cdd:PHA02875 1 MDQVALCDailfgELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLlmkhgAIPDVKYPDIESELHDAVEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 105 SMLTDVKHFLSSGGNVNEK-NDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQ 183
Cdd:PHA02875 79 GDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
170
....*....|....*....
gi 1622884521 184 ANPHLVNCNEEKPSDIAAS 202
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMA 177
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1230-1565 |
7.17e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.41 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1230 AANEALARPRPHSDDYSTMKKIPPRKPKRSPNTklsgsyeeiSGSRPGDARPPGAPGTAARvlTPGTPQCALPPATPPGD 1309
Cdd:PHA03307 133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVASD---------AASSRQAALPLSSPEETAR--APSSPPAEPPPSTPPAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1310 EDDGEPVYIEMLGHPARPDSPDPGESvyeemkcclpDDGGPGAGSFLRASPPllhgaPEDEAAGPPgDMCDIPPPFPNLL 1389
Cdd:PHA03307 202 ASPRPPRRSSPISASASSPAPAPGRS----------AADDAGASSSDSSSSE-----SSGCGWGPE-NECPLPRPAPITL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1390 PHRPPLLVFP-PTPVTCSPASDESPLTPLEVKKLPvletnlkypvQSEGSSPLSPQYSKSQKGDGDRPASPGLALFNGSG 1468
Cdd:PHA03307 266 PTRIWEASGWnGPSSRPGPASSSSSPRERSPSPSP----------SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSES 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1469 RASppstppppppgpppapfrpcahLAFPPEPAPVSLGKAGPSTEAPKVHPK---PNSAPGAGSCSSFPKIPYSPVKAAR 1545
Cdd:PHA03307 336 SRG----------------------AAVSPGPSPSRSPSPSRPPPPADPSSPrkrPRPSRAPSSPAASAGRPTRRRARAA 393
|
330 340
....*....|....*....|
gi 1622884521 1546 VDARKAGSSASPPAPYSPPS 1565
Cdd:PHA03307 394 VAGRARRRDATGRFPAGRPR 413
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1214-1429 |
7.69e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 54.11 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1214 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDA-RPPGAPGTAARVl 1292
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASArGPGGAPAPAPAP- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1293 tPGTPQCALPPAT----PPGDEDDGEPVYIEMLGHPAR-PDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLHGAP 1367
Cdd:PRK12323 455 -AAAPAAAARPAAagprPVAAAAAAAPARAAPAAAPAPaDDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATAD 533
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622884521 1368 EDEAAGPPGDMcdiPPPFPNLLPHRPPLLVFPPTPvtcsPASDESPLTPLEVKKLPVLETNL 1429
Cdd:PRK12323 534 PDDAFETLAPA---PAAAPAPRAAAATEPVVAPRP----PRASASGLPDMFDGDWPALAARL 588
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1213-1552 |
7.93e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.41 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1213 LSASYEAVSACLSAAREAANealaRPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAArvl 1292
Cdd:PHA03307 44 VSDSAELAAVTVVAGAAACD----RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1293 TPGTPQCALPPATPPgdeddgePVYIEML------GHPARPDSPDPGESvyeemKCCLPDDGGPGAGSFLRASPPllhga 1366
Cdd:PHA03307 117 PPPTPPPASPPPSPA-------PDLSEMLrpvgspGPPPAASPPAAGAS-----PAAVASDAASSRQAALPLSSP----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1367 PEDEAAGPPGDMCDIPPPFPNLLPHRPPllvfPPTPVTCSPASDESPLTP--LEVKKLPVLETNLKYPVQSEGSSPL--- 1441
Cdd:PHA03307 180 EETARAPSSPPAEPPPSTPPAAASPRPP----RRSSPISASASSPAPAPGrsAADDAGASSSDSSSSESSGCGWGPEnec 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1442 -----SPQYSKSQKGDGDRPASPGLALFNGSGRASPPSTPPPPPPGPPPAPFRPCAH-------------LAFPPEPAPV 1503
Cdd:PHA03307 256 plprpAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPrasssssssressSSSTSSSSES 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622884521 1504 SLGKAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPySPVKAARVDARKAG 1552
Cdd:PHA03307 336 SRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP-RPSRAPSSPAASAG 383
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
42-195 |
1.01e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 42 DNP--DIVLLLVLAGANVLLQDVNGNIPLdyavegtesSSILLTYLDENgvdltslrqmklqrpmSMLTDVKHFLSSGGN 119
Cdd:PHA02798 47 DSPstDIVKLFINLGANVNGLDNEYSTPL---------CTILSNIKDYK----------------HMLDIVKILIENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 120 VNEKNDEGVTLLHMACASGY---KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG---QANLVKLLLMHQANPHLVNcNE 193
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHN-NK 180
|
..
gi 1622884521 194 EK 195
Cdd:PHA02798 181 EK 182
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
8-192 |
2.04e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 8 YDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGA--NVLLQDVNGniPLDYAVE-----GTESSSI 80
Cdd:PHA02875 12 FGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEegdvkAVEELLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 81 LLTYLDE----NGvdLTSLRQMKLQRPMSMLtdvKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIV 156
Cdd:PHA02875 90 LGKFADDvfykDG--MTPLHLATILKKLDIM---KLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622884521 157 DDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCN 192
Cdd:PHA02875 165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
146-200 |
2.31e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 2.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884521 146 ILEHGG-DLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIA 200
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
1202-1543 |
2.49e-06 |
|
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.
Pssm-ID: 434857 [Multi-domain] Cd Length: 668 Bit Score: 52.46 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1202 PPKPKRDPNTRLSASYE-AVSACLSAAREAANEALARPRPHSDDYS-----TMKKIPPRKPKRSpntklSGSYEEISGSR 1275
Cdd:pfam15685 198 SATSPTDSQAKHIAEGKtAGGACGGAPPQAGEGEMARFAASESGLSllckvTFKSAAPLCPAAA-----SGPLAAKASLG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1276 PGDARPPGAPGTA---ARVLTPG--TPQCALPPATPP-------GDEDDGEPVYiemlGHPARPDS-----PDPGESVYE 1338
Cdd:pfam15685 273 GGGGGGLFAASGAiscAEVLKQGplAPGAARPLGEVPraaleteGGEGDGEGCS----GGPAAPASharalPPPAYTTFP 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1339 EMKCCL----PDDG--------GPGAGSflrasppllhGAPEDEAAGPPGDMCDIPPP----FPNLLPHRP-PLLVFPPT 1401
Cdd:pfam15685 349 GSKPKFdwvsPPDGperhfrfnGAGGGI----------GAPRRRAAALSGPWGSPPPPpgkaHPIPGPRRPaPALLAPPM 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1402 PVTCSPASDESPLT-PLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQKGD--GDRPASPGlalfNGSGRASPpstppp 1478
Cdd:pfam15685 419 FIFPAPTNGEPVRPgPPAPQALLPRPPPPTPPATPPPVPPPIPQLPALQPMPlaAARPPTPR----PCPGHGES------ 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884521 1479 pppgpppapfrpcahlAFPPEP-APVSLGKAGPSTEAPKVH--PKPNSAPGAGSCSSFPKIPySPVKA 1543
Cdd:pfam15685 489 ----------------ALAPAPtAPLPPALAADQAPAPALAaaPAPSPAPAPATADPLPPAP-APIKA 539
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1212-1543 |
4.95e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1212 RLSASYEAVSACLSAAREAANEALARPRPHSddysTMKKIP-PRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAAR 1290
Cdd:PHA03247 2684 RRRAARPTVGSLTSLADPPPPPPTPEPAPHA----LVSATPlPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1291 VLTPGTPQCALPPATPPGDEDDGEPVYIEMLGHPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLHGAPede 1370
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQP--- 2836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1371 AAGPPGdmcdiPPPFPNLLPhrPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQK 1450
Cdd:PHA03247 2837 TAPPPP-----PGPPPPSLP--LGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1451 gdgdRPASPGLALFNGSGRASPPSTPPPPPPGPPPAPFRPCAHLAFPPEPAPVS----LGKAGPS-TEAPKVHPKPNSAP 1525
Cdd:PHA03247 2910 ----QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVpqpwLGALVPGrVAVPRFRVPQPAPS 2985
|
330
....*....|....*...
gi 1622884521 1526 GAGSCSSFPKIPYSPVKA 1543
Cdd:PHA03247 2986 REAPASSTPPLTGHSLSR 3003
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
4-51 |
1.35e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 1.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622884521 4 KCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLV 51
Cdd:pfam13637 7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1253-1459 |
2.01e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1253 PRKPK--RSPNTKLSGSYEEisgSRPGDARPPGA--PGTAARVLTPGTPQCALPPATPPGDEDDGEPVYIEMLGHPARPD 1328
Cdd:PTZ00449 588 PKDPEepKKPKRPRSAQRPT---RPKSPKLPELLdiPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPK 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1329 SP-DPG--ESVYE----------EMKCCLPDDggPGAGSFLRASPPLLHGAPEDEaagppgdmcdiPPPFPNLLPHRPPL 1395
Cdd:PTZ00449 665 PPfDPKfkEKFYDdyldaaakskETKTTVVLD--ESFESILKETLPETPGTPFTT-----------PRPLPPKLPRDEEF 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1396 LVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYP-------------VQSEGSSPLSPQ------YSKSQKGDGDRP 1456
Cdd:PTZ00449 732 PFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPlpdilaeefkeedIHAETGEPDEAMkrpdspSEHEDKPPGDHP 811
|
...
gi 1622884521 1457 ASP 1459
Cdd:PTZ00449 812 SLP 814
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
13-180 |
2.05e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 49.06 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 13 IAEILIDRGVNVNHQDEDFWTPM-----HIACACDNPDIVLLLVLAGANVLLQDVNGNIPLdYAV--EGTESSSILLTYL 85
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLlsNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 86 DENGVDLTSLRQMKlqrpmsmLTDVKHFLSSGGNVNekndegvtllhmacasgyKEVVSLILEHGGDLNIVDDQY-WTPL 164
Cdd:PHA02798 132 IENGADTTLLDKDG-------FTMLQVYLQSNHHID------------------IEIIKLLLEKGVDINTHNNKEkYDTL 186
|
170 180
....*....|....*....|
gi 1622884521 165 HLAAKYG----QANLVKLLL 180
Cdd:PHA02798 187 HCYFKYNidriDADILKLFV 206
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
14-73 |
2.32e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 2.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 14 AEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVE 73
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1238-1548 |
3.07e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 48.91 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1238 PRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYE----EISGSRPGDARPPGAPGTAARvltpgTPQCALPPATPPGdeddg 1313
Cdd:PHA03378 659 ITPYKPTWTQIGHIPYQPSPTGANTMLPIQWApgtmQPPPRAPTPMRPPAAPPGRAQ-----RPAAATGRARPPA----- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1314 epvyiemlGHPARPDSPDPGesvyeemkcclPDDGGPGAGSFLRASPPLLHGAPEDEAAGPPGDMCDIPPP--------F 1385
Cdd:PHA03378 729 --------AAPGRARPPAAA-----------PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPqappapqqR 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1386 PNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEvkklPVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDRPaSPglalfn 1465
Cdd:PHA03378 790 PRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTK----QILRQLLTGGVKRGRPSLKKPAALERQAAAGPTP-SP------ 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1466 GSGRASPPSTppppppgpppapfrpcAHLAFPPEPAPVSL-GKAGPSTE--APKVHPKPNSAPG---AGSCSSFPKIPys 1539
Cdd:PHA03378 859 GSGTSDKIVQ----------------APVFYPPVLQPIQVmRQLGSVRAaaASTVTQAPTEYTGerrGVGPMHPTDIP-- 920
|
....*....
gi 1622884521 1540 PVKAARVDA 1548
Cdd:PHA03378 921 PSKRAKTDA 929
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
1226-1416 |
3.26e-05 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 48.80 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1226 AAREAANEAlarPRPHSDDYSTMKKIPPRKPKRSPntklsgsyeeisgsRPGDARPPGAPGTAARVLTPGTPQcaLPPAT 1305
Cdd:PHA03321 486 AAPPPEPAA---APSPATYYTRMGGGPPRLPPRNR--------------ATETLRPDWGPPAAAPPEQMEDPY--LEPDD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1306 PPGDEDDGEPVYIEmlGHPARPDSPDpGESVYEEMKcclpDDGGPGAGSF--LRASPPLLhGAPEDEAAGPPgdmcDIPP 1383
Cdd:PHA03321 547 DRFDRRDGAAAAAT--SHPREAPAPD-DDPIYEGVS----DSEEPVYEEIptPRVYQNPL-PRPMEGAGEPP----DLDA 614
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622884521 1384 PFPNLLPH--------RPPLLVFPPTPVTCSPASDESPLTP 1416
Cdd:PHA03321 615 PTSPWVEEenpiygwgDSPLFSPPPAARFPPPDPALSPEPP 655
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
161-190 |
3.50e-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: 3.50e-05
10 20 30
....*....|....*....|....*....|.
gi 1622884521 161 WTPLHLAA-KYGQANLVKLLLMHQANPHLVN 190
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
126-155 |
8.36e-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: 41.03 E-value: 8.36e-05
10 20 30
....*....|....*....|....*....|
gi 1622884521 126 EGVTLLHMACASGYKEVVSLILEHGGDLNI 155
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
159-188 |
1.02e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|
gi 1622884521 159 QYWTPLHLAAKYGQANLVKLLLMHQANPHL 188
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1213-1540 |
1.43e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 46.68 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1213 LSASYEAVSACLSAAREAANEALARPRPHSddystmkkiPPRKPKRSPNTKLSgSYEEISGSRPGDARPPGAPGTAARVL 1292
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSA---------PSVPPQGSPATSQP-PNQTQSTAAPHTLIQQTPTLHPQRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1293 TPGTPQCALPPATPPgDEDDGEPVYIEMLgHPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLhgaPEDEAA 1372
Cdd:pfam03154 244 SPHPPLQPMTQPPPP-SQVSPQPLPQPSL-HGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPG---PSPAAP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1373 GPPGDMCDIPPPFPNLLPHRPPL-LVFPPTPVTCsPASDESPLTPleVKKLPVLETNlKYPVQSEGSSPLSPqysksqkg 1451
Cdd:pfam03154 319 GQSQQRIHTPPSQSQLQSQQPPReQPLPPAPLSM-PHIKPPPTTP--IPQLPNPQSH-KHPPHLSGPSPFQM-------- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1452 DGDRPASPGLALFngsgraSPPSTPPPPPPGPPPAPFRPCAHLAFPPEPAPVSLGKAGPSTEAPKVHPKPNSAPGAGSCS 1531
Cdd:pfam03154 387 NSNLPPPPALKPL------SSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQS 460
|
....*....
gi 1622884521 1532 SFPKIPYSP 1540
Cdd:pfam03154 461 PFPQHPFVP 469
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
126-158 |
1.74e-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: 40.35 E-value: 1.74e-04
10 20 30
....*....|....*....|....*....|....
gi 1622884521 126 EGVTLLHMACAS-GYKEVVSLILEHGGDLNIVDD 158
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
126-155 |
2.11e-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: 39.93 E-value: 2.11e-04
10 20 30
....*....|....*....|....*....|
gi 1622884521 126 EGVTLLHMACASGYKEVVSLILEHGGDLNI 155
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1214-1500 |
2.44e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1214 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISG---SRPGDARPPGA-PGT-- 1287
Cdd:PHA03247 2800 SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAkPAApa 2879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1288 ---AARVLTPGTPQCALPPATPPgdeDDGEPvyiemlghPARPDSPDPGESVYEEMKCCLPDDGGPGAGsflRASPPLlh 1364
Cdd:PHA03247 2880 rppVRRLARPAVSRSTESFALPP---DQPER--------PPQPQAPPPPQPQPQPPPPPQPQPPPPPPP---RPQPPL-- 2943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1365 gAPEDEAAGPPGDMCDIPPP-FPNLLPHR---PPLLVFPPTPVTCSPASDESPLTPLEVKKL----------------PV 1424
Cdd:PHA03247 2944 -APTTDPAGAGEPSGAVPQPwLGALVPGRvavPRFRVPQPAPSREAPASSTPPLTGHSLSRVsswasslalheetdppPV 3022
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884521 1425 -LETNLKYPVQSEGSSPLSPQYSKSQKGDGDRP-ASPGlalfngsgrASPPSTPPPPPPGPPPAPFRPCAHLAFPPEP 1500
Cdd:PHA03247 3023 sLKQTLWPPDDTEDSDADSLFDSDSERSDLEALdPLPP---------EPHDPFAHEPDPATPEAGARESPSSQFGPPP 3091
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1228-1545 |
3.50e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.44 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1228 REAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYeeisgsrPGDARPPGAPGTAARVLTPGTP---------- 1297
Cdd:PHA03378 433 KKAARTEQPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQA-------PLEPWQPLPHPQVTPVILHQPPaqgvqahgsm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1298 ----------------QCALPPATP-PGDEDDGEPVYIEMLGhpARPDSPDPGESVYEEMkccLPDDG-GP--------G 1351
Cdd:PHA03378 506 ldllekddedmeqrvmATLLPPSPPqPRAGRRAPCVYTEDLD--IESDEPASTEPVHDQL---LPAPGlGPlqiqpltsP 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1352 AGSFLRASPPLLHGAP-----EDEAAGPPGDMCDIPP---PFPNLLPHRP-PLLVFPPTPVTCSPASDESPLTPLEVKKL 1422
Cdd:PHA03378 581 TTSQLASSAPSYAQTPwpvphPSQTPEPPTTQSHIPEtsaPRQWPMPLRPiPMRPLRMQPITFNVLVFPTPHQPPQVEIT 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1423 PVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDR----PASPGLA----LFNGSGRASPPSTPPPPPPGPPPAPFRPCAHL 1494
Cdd:PHA03378 661 PYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTmqppPRAPTPMrppaAPPGRAQRPAAATGRARPPAAAPGRARPPAAA 740
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622884521 1495 AFPPEPAPVSLGKAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPYSPVKAAR 1545
Cdd:PHA03378 741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPR 791
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1251-1552 |
3.75e-04 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 45.05 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1251 IPPRKPKRSPNT---KLSGSYEEISGSRPGDARPPGAPGTAARvltPGTPQCALPPAT-PPGDEDDGEPVYIEMLGHPAR 1326
Cdd:COG5180 84 LDPAPPKSSPDTpeeQLGAPAGDLLVLPAAKTPELAAGALPAP---AAAAALPKAKVTrEATSASAGVALAAALLQRSDP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1327 PDSPDPGEsvyeemkccLPDDGGPGAGSFLR--ASPPLLHGAPEDEAAgppgdmcDIPPPfpnllPHRPPLLVFPPTPVT 1404
Cdd:COG5180 161 ILAKDPDG---------DSASTLPPPAEKLDkvLTEPRDALKDSPEKL-------DRPKV-----EVKDEAQEEPPDLTG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1405 CS-----PASDESPLTPLEvkklPVLETNLKYPVQSEG-SSPLSPQYSKSQKGDGDRPAS--PGL-ALFNGSGRASPPST 1475
Cdd:COG5180 220 GAdhprpEAASSPKVDPPS----TSEARSRPATVDAQPeMRPPADAKERRRAAIGDTPAAepPGLpVLEAGSEPQSDAPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1476 PPPPPPGPPPAPFRPcahlafPPEPAPVSLG---------KAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPYSPVKAARV 1546
Cdd:COG5180 296 AETARPIDVKGVASA------PPATRPVRPPggardpgtpRPGQPTERPAGVPEAASDAGQPPSAYPPAEEAVPGKPLEQ 369
|
....*.
gi 1622884521 1547 DARKAG 1552
Cdd:COG5180 370 GAPRPG 375
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
128-200 |
5.25e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 5.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884521 128 VTLLHMAcASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIA 200
Cdd:PTZ00322 84 VELCQLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
160-187 |
7.33e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.39 E-value: 7.33e-04
10 20
....*....|....*....|....*...
gi 1622884521 160 YWTPLHLAAKYGQANLVKLLLMHQANPH 187
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1221-1413 |
1.63e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1221 SACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQCA 1300
Cdd:PHA03307 227 SAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1301 LPPATPPGDEDDGEPvyiemlgHPARPDSPDPGESVyeemkcclpdDGGPGAGSflrasppllhGAPEDEAAGPPGDMCD 1380
Cdd:PHA03307 307 PAPSSPRASSSSSSS-------RESSSSSTSSSSES----------SRGAAVSP----------GPSPSRSPSPSRPPPP 359
|
170 180 190
....*....|....*....|....*....|...
gi 1622884521 1381 IPPPFPnllPHRPPLLVFPPTPVTcSPASDESP 1413
Cdd:PHA03307 360 ADPSSP---RKRPRPSRAPSSPAA-SAGRPTRR 388
|
|
| PHA03325 |
PHA03325 |
nuclear-egress-membrane-like protein; Provisional |
1276-1418 |
1.97e-03 |
|
nuclear-egress-membrane-like protein; Provisional
Pssm-ID: 223044 Cd Length: 418 Bit Score: 42.56 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1276 PGDARPPGAPGTAARVLTPGTPQCALPPATPPGDEDDGEPVyiemlgHPARPDSPDPGESVYEEMkcclpDDGGPGAGSF 1355
Cdd:PHA03325 282 AMRAAAGETADLADDDGSEHSDPEPLPASLPPPPVRRPRVK------HPEAGKEEPDGARNAEAK-----EPAQPATSTS 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1356 LRASPpllHGAPEDEAAGPPGDMC-------DIPPPFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLE 1418
Cdd:PHA03325 351 SKGSS---SAQNKDSGSTGPGSSLaaassflEDDDFGSPPLDLTTSLRHMPSPSVTSAPEPPSIPLTYLS 417
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
32-61 |
2.40e-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: 37.27 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|.
gi 1622884521 32 WTPMHIACA-CDNPDIVLLLVLAGANVLLQD 61
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
119-193 |
3.17e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 42.38 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 119 NVNEKNDEGVTLLHMAcASGYKEVVSLILEH-------GGDLNIVDDQYW-------TPLHLAAKYGQANLVKLLLMHQA 184
Cdd:TIGR00870 74 NLSCRGAVGDTLLHAI-SLEYVDAVEAILLHllaafrkSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGA 152
|
90
....*....|
gi 1622884521 185 NPHL-VNCNE 193
Cdd:TIGR00870 153 SVPArACGDF 162
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
1249-1459 |
3.55e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 42.22 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1249 KKIPPRKPKRS--PNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQCALPPATPP------------------- 1307
Cdd:PLN03209 326 QRVPPKESDAAdgPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPiptppssspassksvdava 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1308 -GDEDDGEPVYIEMLGHP-----------ARPDSPdpgESVYEEMK-CCLPDDGGPGAGSFLRASPPLLHGAPEDEAAGP 1374
Cdd:PLN03209 406 kPAEPDVVPSPGSASNVPevepaqveakkTRPLSP---YARYEDLKpPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1375 PGDMCDIPPPFPNllPHRPPL----LVFPPTPVTCSPASDESPLTPLEVKKL--------PVLETNLKYPVQsegsSPLS 1442
Cdd:PLN03209 483 ATDAAAPPPANMR--PLSPYAvyddLKPPTSPSPAAPVGKVAPSSTNEVVKVgnsapptaLADEQHHAQPKP----RPLS 556
|
250
....*....|....*..
gi 1622884521 1443 PqYSKSQkgDGDRPASP 1459
Cdd:PLN03209 557 P-YTMYE--DLKPPTSP 570
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1259-1445 |
3.59e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 42.12 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1259 SPNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQC-ALPPATP--PGDEDDGEP-----------VYIEMLGHP 1324
Cdd:PRK14086 96 APPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQdQLPTARPayPAYQQRPEPgawpraaddygWQQQRLGFP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1325 ARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPpllHGaPEDEAAGPPGDMCDIPPPFPNllPHRPPLLVFPPTPVT 1404
Cdd:PRK14086 176 PRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDY---DH-PRPDWDRPRRDRTDRPEPPPG--AGHVHRGGPGPPERD 249
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622884521 1405 CSPASDESPLTPLEVKKLPvlETNlkyPVQSEGSSPLSPQY 1445
Cdd:PRK14086 250 DAPVVPIRPSAPGPLAAQP--APA---PGPGEPTARLNPKY 285
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
1242-1431 |
3.65e-03 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 42.35 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1242 SDDYSTMKKipPRKPKRSPNT--KLSGSYEEI--------SGSRPGDARPPGA--PGTAARVLTPGT--PQCALPPATPP 1307
Cdd:PHA03377 520 TEEEESVTQ--PAKPHRKVQDgfQRSGRRQKRatppkvspSDRGPPKASPPVMapPSTGPRVMATPStgPRDMAPPSTGP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1308 GDE---DDGEPVYIEMLGHP--ARPDSPDPgeSVYEEM--KCCLPDDGGPGAGSF--LRAS--------PPLLHGAPEDE 1370
Cdd:PHA03377 598 RQQakcKDGPPASGPHEKQPpsSAPRDMAP--SVVRMFlrERLLEQSTGPKPKSFweMRAGrdgsgiqqEPSSRRQPATQ 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884521 1371 AAgppgdmcdipPPFPNLLphrPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKY 1431
Cdd:PHA03377 676 ST----------PPRPSWL---PSVFVLPSVDAGRAQPSEESHLSSMSPTQPISHEEQPRY 723
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1240-1374 |
3.93e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1240 PHS-DDYSTMKKIPPRKP-----------KRSPNTKLSGSYEEISGSRPGDARPP--GAPGTAARVltPGTPQCALPPAT 1305
Cdd:PHA03247 362 PSSlEDLSAGRHHPKRASlptrkrrsarhAATPFARGPGGDDQTRPAAPVPASVPtpAPTPVPASA--PPPPATPLPSAE 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884521 1306 PPGDEDDGEPVYiemlGHPARPDSPDPGESvyeemkcclPDDGGPGAGSFLRASPPllhgaPEDEAAGP 1374
Cdd:PHA03247 440 PGSDDGPAPPPE----RQPPAPATEPAPDD---------PDDATRKALDALRERRP-----PEPPGADL 490
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
30-57 |
4.01e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 4.01e-03
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
164-214 |
4.25e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.17 E-value: 4.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884521 164 LHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAAS----EFIEEMLLKAEI 214
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKnghlEIVKLLLEHADV 55
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
32-57 |
4.56e-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: 4.56e-03
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1279-1551 |
7.77e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1279 ARPPGAPGTAARVLTPGTPQCALPPatpPGDEDDGEPVYIEMLGHPARPDSPDPGESVYEEmkcclpDDGGPGAGSFLRA 1358
Cdd:PHA03307 22 PRPPATPGDAADDLLSGSQGQLVSD---SAELAAVTVVAGAAACDRFEPPTGPPPGPGTEA------PANESRSTPTWSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1359 SPPLLHGAPEDEAAGPPGdmcdipppfpnllphRPPLLVFPPTPVTCSPASDESPLTPlevkklPVLETNLKYPVQSEGS 1438
Cdd:PHA03307 93 STLAPASPAREGSPTPPG---------------PSSPDPPPPTPPPASPPPSPAPDLS------EMLRPVGSPGPPPAAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 1439 SPLSPqySKSQKGDGDRPASPGLALFNGSGRASPPSTPPPPPpgpppapfrpcahlAFPPEPAPVSLGKAGPSTEAPKVH 1518
Cdd:PHA03307 152 PPAAG--ASPAAVASDAASSRQAALPLSSPEETARAPSSPPA--------------EPPPSTPPAAASPRPPRRSSPISA 215
|
250 260 270
....*....|....*....|....*....|...
gi 1622884521 1519 PKPNSAPGAGSCSSFPKIPYSPVKAARVDARKA 1551
Cdd:PHA03307 216 SASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
13-100 |
9.03e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 39.42 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884521 13 IAEILIDRGVNVNHQDEDFWTPMHI-ACACD-NPDIVLLLVLAGANVLLQDVNGNIPLdYAVEGTESSSILLTYLDENGV 90
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLLIDSGVSFLNKDFDNNNIL-YSYILFHSDKKIFDFLTSLGI 183
|
90
....*....|
gi 1622884521 91 DLTSLRQMKL 100
Cdd:PHA02859 184 DINETNKSGY 193
|
|
| |
