|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
436-1154 |
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: 1358.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGARIY 595
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKHLTGARIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 596 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLAVLKQALNVVGF 675
Cdd:cd14878 161 TYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSLNREKLAVLKQALNVVGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 676 SNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 755
Cdd:cd14878 241 SSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 756 FFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHE 835
Cdd:cd14878 321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 836 QVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGNGNVA 915
Cdd:cd14878 401 QTECVQEGVTMETAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYSPMKDGNGNVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 916 LKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLsqtgslvsaypsfkfrghksalls 995
Cdd:cd14878 481 LKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL------------------------ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 996 kkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFD 1075
Cdd:cd14878 537 ---------------------------------------VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFD 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884518 1076 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQGWQMGVRKVFLK 1154
Cdd:cd14878 578 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
437-1154 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 668.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRS--ADLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAAS-------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQL 589
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSgssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF-DPTGRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 590 TGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-TMQDDVSTGERSLNREKLAVLKQ 668
Cdd:cd00124 159 VGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDyLNSSGCDRIDGVDDAEEFQELLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 669 ALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 746
Cdd:cd00124 239 ALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 747 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmqTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 826
Cdd:cd00124 319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAES--TSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 827 INEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAvysp 906
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDFPDNQD-CLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF---- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 907 lkdgngnVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqsklsqtgslvsaypsfkf 986
Cdd:cd00124 472 -------SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG---------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 987 rghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDIIGKLQKCTPHFIHCIRPN 1066
Cdd:cd00124 517 ----------------------------------------------------SQFRSQLDALMDTLNSTQPHFVRCIKPN 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1067 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFL-REKKEHLAAERCRLVLQQCKLQGWQ 1145
Cdd:cd00124 545 DEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATeKASDSKKAAVLALLLLLKLDSSGYQ 624
|
....*....
gi 1622884518 1146 MGVRKVFLK 1154
Cdd:cd00124 625 LGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
425-1164 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 611.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 425 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 504
Cdd:smart00242 9 EDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKY---RGKSRGELPPHVFAIADNAYRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 505 LFQEQRPQCFILSGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVM----CILEAFGHAKTTLNDLSSCFIKYFEL 580
Cdd:smart00242 86 MLNDKENQSIIISGESGAGKTENTKKIMQYLA--SVSGSNTEVGSVEDQIlesnPILEAFGNAKTLRNNNSSRFGKFIEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 581 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ------TMQDDVstg 654
Cdd:smart00242 164 HFDA-KGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQggcltvDGIDDA--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 655 erslnrEKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSA-FVSDLQLLEQVAGMLQVSTDELASAL 733
Cdd:smart00242 240 ------EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 734 TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQ 813
Cdd:smart00242 314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYF----IGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 814 LCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkkLQS 893
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDW-TFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTF---LEK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 894 LLESSNTNAVYSPLKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQ 973
Cdd:smart00242 466 LNQHHKKHPHFSKPK--------KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 974 TGslvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQ 1053
Cdd:smart00242 538 AG-------------------SKKR-----------------------------------FQTVGSQFKEQLNELMDTLN 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1054 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCR 1133
Cdd:smart00242 564 STNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTW-PPWGGDAKKACE 642
|
730 740 750
....*....|....*....|....*....|...
gi 1622884518 1134 LVLQQCKL--QGWQMGVRKVFLKYWHADQLNDL 1164
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 ... |
437-1154 |
1.36e-175 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 546.87 E-value: 1.36e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLY---RGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCeRKQQLTGARIYT 596
Cdd:cd01379 79 SGESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT-STGAVTGARISE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEK-HGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLAVLKQALNVVGF 675
Cdd:cd01379 158 YLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 676 SNLEVENLFVILAAILHLGDIRFTALTEG----NSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 751
Cdd:cd01379 238 TKEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 752 QIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 831
Cdd:cd01379 318 EEATDARDAMAKALYGRLFSWIVNRINS-LLKPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 832 FLHEQVECVQEGVTMET-AYSpgNQNGVLDFFFQKPSGFLTLLDEESQmiwsmesnFPKKL-QSLLESSNTNavyspLKD 909
Cdd:cd01379 397 FAWEQQEYLNEGIDVDLiEYE--DNRPLLDMFLQKPMGLLALLDEESR--------FPKATdQTLVEKFHNN-----IKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 910 GNgNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrgh 989
Cdd:cd01379 462 KY-YWRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 990 ksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSK 1069
Cdd:cd01379 517 ----------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSR 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1070 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtFLREKKEHLAAERCRLVLQQCKLQGWQMGVR 1149
Cdd:cd01379 551 QAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA--FKWNEEVVANRENCRLILERLKLDNWALGKT 628
|
....*
gi 1622884518 1150 KVFLK 1154
Cdd:cd01379 629 KVFLK 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
425-1154 |
1.44e-165 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 521.07 E-value: 1.44e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 425 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 504
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAY---RGKRRGELPPHIFAIADEAYRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 505 LFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC----ILEAFGHAKTTLNDLSSCFIKYFEL 580
Cdd:pfam00063 79 MLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILqsnpILEAFGNAKTVRNNNSSRFGKYIEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 581 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSlnr 660
Cdd:pfam00063 159 QF-DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 661 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 741 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTN 820
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSL---DVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 821 EKMHHYINEVLFLHEQVECVQEGVTmetaYSP---GNQNGVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKK-----LQ 892
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIE----WTFidfGDNQPCIDLIEKKPLGILSLLDE--------ECLFPKAtdqtfLD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 893 SLLESSNTNAVY-SPLKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkl 971
Cdd:pfam00063 460 KLYSTFSKHPHFqKPRLQGE---------THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD-- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 972 sqtGSLVSAYPSFKFRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGK 1051
Cdd:pfam00063 529 ---YETAESAAANESGKSTPKRTKKKR-----------------------------------FITVGSQFKESLGELMKT 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1052 LQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHlAAER 1131
Cdd:pfam00063 571 LNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGD-AKKG 649
|
730 740
....*....|....*....|....*
gi 1622884518 1132 CRLVLQQCKLQG--WQMGVRKVFLK 1154
Cdd:pfam00063 650 CEAILQSLNLDKeeYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
424-1256 |
1.65e-148 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 498.06 E-value: 1.65e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 424 NDDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFH 503
Cdd:COG5022 68 VDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY---SGKNRLELEPHVFAIAEEAYR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 504 QLFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFEL 580
Cdd:COG5022 145 NLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEKQILAtnpILEAFGNAKTVRNDNSSRFGKYIKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 581 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNR 660
Cdd:COG5022 225 EFDE-NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 661 EKLAvlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFvSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:COG5022 304 KITL---DALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIF-SDNSVLDKACYLLGIDPSLFVKWLVKRQIKT 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 741 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTN 820
Cdd:COG5022 380 GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNF----IGVLDIYGFEIFEKNSFEQLCINYTN 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 821 EKMHHYINEVLFLHEQVECVQEGVtmetAYSP----GNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLe 896
Cdd:COG5022 456 EKLQQFFNQHMFKLEQEEYVKEGI----EWSFidyfDNQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQRL- 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 897 SSNTNAVYSPLKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsqtgs 976
Cdd:COG5022 531 NKNSNPKFKKSRFRD---------NKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE------ 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 977 lvsaypsfkfrghksallskkmtassiigENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCT 1056
Cdd:COG5022 596 -----------------------------ENIE--------------------SKGRFPTLGSRFKESLNSLMSTLNSTQ 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1057 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR---EKKEHLAAERCR 1133
Cdd:COG5022 627 PHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWtgeYTWKEDTKNAVK 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1134 LVLQQCKL--QGWQMGVRKVFLKywhADQLNDLCLQ----LQRKIITCQKVIRGFLARQHLLQKISiRQQEVTS-INSFL 1206
Cdd:COG5022 707 SILEELVIdsSKYQIGNTKVFFK---AGVLAALEDMrdakLDNIATRIQRAIRGRYLRRRYLQALK-RIKKIQViQHGFR 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884518 1207 QNTE-DMGLKTYDALVIQNASDIA--RENDRLRSEMNAPYHKE---KLEVRNTQEE 1256
Cdd:COG5022 783 LRRLvDYELKWRLFIKLQPLLSLLgsRKEYRSYLACIIKLQKTikrEKKLRETEEV 838
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
437-1154 |
8.40e-148 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 471.74 E-value: 8.40e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLY---RNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTcrAASS------RAMLDSRfkhvmCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLT 590
Cdd:cd01381 79 SGESGAGKTESTKLILQYLA--AISGqhswieQQILEAN-----PILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV-IE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 591 GARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqtMQDDVSTGERSLNREKLAVLKQAL 670
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYL---TQGNCLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 671 NVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 748
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNldASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 749 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 828
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDS-SRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 829 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQmiwsmesnFPKKL-QSLLESSN----TNAV 903
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEFVDNQD-VLDLIALKPMNIMSLIDEESK--------FPKGTdQTMLEKLHsthgNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 904 YSPLKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsayps 983
Cdd:cd01381 458 YLKPK--------SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 984 fkfrghksallskkmtassiigenknylelskllkkkGTSTflqrleRGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCI 1063
Cdd:cd01381 520 -------------------------------------GSET------RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCI 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1064 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKE---HLAAERCRLVLQQCK 1140
Cdd:cd01381 557 KPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTdcrAATRKICCAVLGGDA 636
|
730
....*....|....
gi 1622884518 1141 LqgWQMGVRKVFLK 1154
Cdd:cd01381 637 D--YQLGKTKIFLK 648
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
437-1154 |
9.00e-148 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 471.10 E-value: 9.00e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVR--SQRPPHLFWIADQAYRRLLETGRNQCILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGARIYT 596
Cdd:cd14897 80 SGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE-NGQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL-NQTMQDDV--STGERSLNREKLAVLKQALNVV 673
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrDDNRNRPVfnDSEELEYYRQMFHDLTNIMKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 674 GFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 753
Cdd:cd14897 239 GFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 754 AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTL-DIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 832
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGpSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 833 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTnavYSPLKDGNg 912
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDD-VLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR---YVASPGNR- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 913 nvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsaypsfkfrghksa 992
Cdd:cd14897 474 --------VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 993 llskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPD 1072
Cdd:cd14897 521 ---------------------------------------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1073 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEHLAAERCRLVLQQCKLQGWQMGVRKVF 1152
Cdd:cd14897 556 KFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS--NKVRSDDLGKCQKILKTAGIKGYQFGKTKVF 633
|
..
gi 1622884518 1153 LK 1154
Cdd:cd14897 634 LK 635
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
438-1154 |
7.40e-146 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 467.08 E-value: 7.40e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLF----QEQRPQC 513
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKS---SLPPHIFAVADRAYQSMLgrlaRGPKNQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 514 FILSGERGSGKSEASKQIIRHLT--CRAASSramLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTG 591
Cdd:cd14889 80 IVISGESGAGKTESTKLLLRQIMelCRGNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF--RNGHVKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 592 ARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTM--QDDVSTGerslnREKLAVLKQA 669
Cdd:cd14889 155 AKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAgcKREVQYW-----KKKYDEVCNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 670 LNVVGFSNLEVENLFVILAAILHLGDIRFTaLTEGNSAFVSDLQ--LLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 747
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITFE-MDDDEALKVENDSngWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 748 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 827
Cdd:cd14889 309 HHTKQQAEDARDSIAKVAYGRVFGWIVSKINQ-LLAPKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 828 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVYSpl 907
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITYKDNKP-ILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG---NSYYG-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 908 KDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfr 987
Cdd:cd14889 462 KSRS-------KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPR------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 988 ghksallSKKMTASSiigenknylelskllkKKGTSTFLQrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNN 1067
Cdd:cd14889 528 -------AKLPQAGS----------------DNFNSTRKQ--------SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNH 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1068 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEHLAAERCRLVLQQCKLQGWQMG 1147
Cdd:cd14889 577 VKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKLVGWKCG 652
|
....*..
gi 1622884518 1148 VRKVFLK 1154
Cdd:cd14889 653 KTRLFFK 659
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
1242-1587 |
1.06e-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: 444.60 E-value: 1.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1242 PYHKEKLEVRNTQEEGSKRTEDK---------SGPRHFHPSSMSVCMAVDGLG-QCLAGPSIWSPSLHSVFSMDDNSSLP 1311
Cdd:pfam15439 1 LYRKEKLEKRRRQEEGIKRSGEEvagkvrdisSEGRHFRMGFMTMPASQDRLPhPCAAGMSIRSQSLHSVGSGDEDGSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1312 SPRKQPPPKPKRDPNTRLSASYEAVSACLS-AAREAA--NEALARPRPHSDDYStmKKIPPRKPKRSPNTKLSGSYEEIS 1388
Cdd:pfam15439 81 SSRKQPPPKPKRDPSTKLSMSSEAVSAGLSaGAKETPseTEALSKPRPHSDEYS--RKIPPPKPKRSPNTQLSGSFDEIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1389 GSRPgdaRPPGAPGTAArvlTPGTPQCAlppatpPGDEDDGEPVYIEMLGHPAR-------PDSPDPGESVYEEMKCCLP 1461
Cdd:pfam15439 159 APYI---RPHGLLQRAS---SSDGPSPA------PLPDEEEEPVYIEMVGNVLRdfspttpDDDPDQSEAVYEEMKYPLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1462 DDGGPGAGSFLRASPPLL-----HGAPEDE--------AAGPPGDMCDIPPPFPNLLPHRPPLLVFPPTPVTCSPASDES 1528
Cdd:pfam15439 227 EDSGAANGPPPLASSPLLadphsPISPESDsalpssqcATPTKKDLCDIPAPFPNLLPHRPPLLVFPPAPVTCSPASDES 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884518 1529 PLTPLEVKKLPVLEtNLKYPVQSEgSSPLSPQYSKSQKGDGDRPASPGLALFNGSGRAS 1587
Cdd:pfam15439 307 PLTPLEVKKLPVLE-NVSYSKQPA-SSPLSPQESKHQREDKDRPSSPGLAVLTPSGRAR 363
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
442-1154 |
7.18e-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: 7.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 442 IQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERG 521
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESY---RGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 522 SGKSEASKQIIRHLTcrAASSRAMLD-SRFKHVM----CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 596
Cdd:cd01378 84 AGKTEASKRIMQYIA--AVSGGSESEvERVKDMLlasnPLLEAFGNAKTLRNDNSSRFGKYMEIQF-DFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStgerSLNREK-LAVLKQALNVVGF 675
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVD----GIDDAAdFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 676 SNLEVENLFVILAAILHLGDIRFTALTEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM---IIRRHTIQ 752
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEEGNAA-ISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 753 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLLS-QDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 831
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAkSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 832 FLHEQVECVQEGVTMETayspgnqngvLDFFF---------QKPSGFLTLLDEESqmiwsmesNFPKK------LQSLLE 896
Cdd:cd01378 392 LKAEQEEYVREGIEWTP----------IKYFNnkiicdlieEKPPGIFAILDDAC--------LTAGDatdqtfLQKLNQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 897 SSNTNAVYSPLKDgngnvALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgs 976
Cdd:cd01378 454 LFSNHPHFECPSG-----HFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 977 lvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQKCT 1056
Cdd:cd01378 527 ------------------SKKR-----------------------------------PPTAGTKFKNSANALVETLMKKQ 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1057 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAD-TFLRekKEHLAAERCRLV 1135
Cdd:cd01378 554 PSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPkTWPA--WDGTWQGGVESI 631
|
730 740
....*....|....*....|.
gi 1622884518 1136 LQQCKLQG--WQMGVRKVFLK 1154
Cdd:cd01378 632 LKDLNIPPeeYQMGKTKIFIR 652
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
436-1154 |
1.03e-136 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 442.59 E-value: 1.03e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSsgKLcSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNR--RL-GKLPPHIFAIADVAYHAMLRKKKNQCIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGA 592
Cdd:cd01385 78 ISGESGSGKTESTNFLLHHLT--ALSQKGYGSGVEQTILGagpVLEAFGNAKTAHNNNSSRFGKFIQVNYRE-NGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 593 RIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTGERSLNREKLAVLKQALNV 672
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQS---DCYTLEGEDEKYEFERLKQAMEM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 673 VGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 750
Cdd:cd01385 232 VGFLPETQRQIFSVLSAVLHLGNIEYKKKAYHRdeSVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 751 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 830
Cdd:cd01385 312 LPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 831 LFLHEQVECVQEGVTMETAYSPGNqNGVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKKL-QSLLE------SSNTNAV 903
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEYTDN-TGCLQLISKKPTGLLCLLDE--------ESNFPGATnQTLLAkfkqqhKDNKYYE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 904 YSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgSLVSAYPS 983
Cdd:cd01385 463 KPQVME-----------PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVR-----------ELIGIDPV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 984 FKFRghkSALLS---KKMTASSIIGEN--KNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQKCTPH 1058
Cdd:cd01385 521 AVFR---WAVLRaffRAMAAFREAGRRraQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPF 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1059 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQ 1138
Cdd:cd01385 598 FIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDR 677
|
730
....*....|....*.
gi 1622884518 1139 CKlqgWQMGVRKVFLK 1154
Cdd:cd01385 678 DN---YQIGKTKVFLK 690
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
437-1154 |
1.87e-136 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 440.99 E-value: 1.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFsssGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYF---GKRMGALPPHIFALAEAAYTNMQEDGKNQSVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLtCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 596
Cdd:cd14883 79 SGESGAGKTETTKLILQYL-CAVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCF-DASGHIKGAIIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDG--LSAEEKHGLHLNNLCAHRYLNQtmqDDVSTGERSLNREKLAVLKQALNVVG 674
Cdd:cd14883 157 YLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQ---SGCIRIDNINDKKDFDHLRLAMNVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 675 FSNLEVENLFVILAAILHLGDIRFTALtEGNSA--FVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQ 752
Cdd:cd14883 234 IPEEMQEGIFSVLSAILHLGNLTFEDI-DGETGalTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 753 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 832
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF----IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 833 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVY-SPLKdgn 911
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFTDNQE-CLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEK---HPYYeKPDR--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 912 gnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsAYPSfkfrghks 991
Cdd:cd14883 462 -----RRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELF------------TYPD-------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 992 alLSKKMTASSIIGENKNylelskllkKKGTStflqrleRGDPvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLP 1071
Cdd:cd14883 517 --LLALTGLSISLGGDTT---------SRGTS-------KGKP-TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1072 DTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLAAERCRLVLQQCKLQG--WQMGVR 1149
Cdd:cd14883 578 NVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL-DPRARSADHKETCGAVRALMGLGGLPEdeWQVGKT 656
|
....*
gi 1622884518 1150 KVFLK 1154
Cdd:cd14883 657 KVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
439-1154 |
4.04e-133 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 431.33 E-value: 4.04e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 439 LYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILS 517
Cdd:cd01384 4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQY---KGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 518 GERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVM---CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 594
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLesnPLLEAFGNAKTVRNNNSSRFGKFVEIQF-DDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 595 YTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ---DDVSTGErslnrEKLAVLKqALN 671
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCfelDGVDDAE-----EYRATRR-AMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 672 VVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSD---LQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 748
Cdd:cd01384 234 VVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 749 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 828
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL----IGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 829 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLqsllessntnavYSPLK 908
Cdd:cd01384 390 QHVFKMEQEEYTKEEIDWSYIEFVDNQD-VLDLIEKKPGGIIALLDEACMFPRSTHETFAQKL------------YQTLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 909 DGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKD---SLSQNLLfvmKTSENVVINHLFQSKLSQTGSlvsayPSFK 985
Cdd:cd01384 457 DHKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDyvvAEHQALL---NASKCPFVAGLFPPLPREGTS-----SSSK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 986 FrghksallskkmtaSSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLTDIIGKLQKCTPHFIHCIRP 1065
Cdd:cd01384 529 F--------------SS----------------------------------IGSRFKQQLQELMETLNTTEPHYIRCIKP 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1066 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLreKKEHLAAERCRLVLQQCKLQGWQ 1145
Cdd:cd01384 561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL--KGSDDEKAACKKILEKAGLKGYQ 638
|
....*....
gi 1622884518 1146 MGVRKVFLK 1154
Cdd:cd01384 639 IGKTKVFLR 647
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
437-1154 |
1.73e-132 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 429.94 E-value: 1.73e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQY---SGRALGELPPHLFAIANLAFAKMLDAKQNQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARIYT 596
Cdd:cd01387 79 SGESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF--EGGVIVGAITSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStGERSlnREKLAVLKQALNVVGFS 676
Cdd:cd01387 157 YLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIA-GKSD--ADDFRRLLAAMQVLGFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 677 NLEVENLFVILAAILHLGDIRF-----TALTEGNSaFVSDLQlLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 751
Cdd:cd01387 234 SEEQDSIFRILASVLHLGNVYFhkrqlRHGQEGVS-VGSDAE-IQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 752 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEqrsmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 831
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQ----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 832 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKKLQ-SLLESSNTNAVYSPLKDg 910
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAFADNQP-VINLISKKPVGILHILDD--------ECNFPQATDhSFLEKCHYHHALNELYS- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 911 ngnvALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsaypsfkfrgHK 990
Cdd:cd01387 458 ----KPRMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ---------------TD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 991 SALLSKkmtassiigenknylelskllkkkGTSTFLQRLERGDpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKL 1070
Cdd:cd01387 519 KAPPRL------------------------GKGRFVTMKPRTP--TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKE 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1071 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQG-WQMGVR 1149
Cdd:cd01387 573 PMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPKDmYRLGAT 652
|
....*
gi 1622884518 1150 KVFLK 1154
Cdd:cd01387 653 KVFLR 657
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
437-1154 |
4.44e-127 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 414.41 E-value: 4.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLcsSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY---RQKL--LDSPHVYAVADTAYREMMRDEINQSIII 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 596
Cdd:cd01383 77 SGESGAGKTETAKIAMQYLAALGGGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHF-DAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTGERSLNREKLAVLKQALNVVGFS 676
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQS---NCLTIDGVDDAKKFHELKEALDTVGIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 677 NLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEF 756
Cdd:cd01383 232 KEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 757 FRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQ--RSmqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 834
Cdd:cd01383 312 ARDALAKAIYASLFDWLVEQINKSLEVGKRRtgRS-----ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 835 EQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEesqmiwsmESNFPK--------KLQSLLessNTNAVYSp 906
Cdd:cd01383 387 EQEEYELDGIDWTKVDFEDNQE-CLDLIEKKPLGLISLLDE--------ESNFPKatdltfanKLKQHL---KSNSCFK- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 907 lkdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSEnvviNHLFQsklsqtgslvsaypsfkf 986
Cdd:cd01383 454 ----------GERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCS----CQLPQ------------------ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 987 rghksaLLSKKMTassiigenkNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPN 1066
Cdd:cd01383 502 ------LFASKML---------DASRKALPLTKASGSDSQKQ-------SVATKFKGQLFKLMQRLENTTPHFIRCIKPN 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1067 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAerCRLVLQQCKLQG--W 1144
Cdd:cd01383 560 NKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLST--SVAILQQFNILPemY 637
|
730
....*....|
gi 1622884518 1145 QMGVRKVFLK 1154
Cdd:cd01383 638 QVGYTKLFFR 647
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
437-1154 |
9.90e-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: 412.70 E-value: 9.90e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd01380 2 AVLHNLKVRFCQrNAIYTYCGIVLVAINPYEDLPIYGEDIIQAY---SGQNMGELDPHIFAIAEEAYRQMARDEKNQSII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAMlDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGA 592
Cdd:cd01380 79 VSGESGAGKTVSAKYAMRYFATVGGSSSGE-TQVEEKVLAsnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKN-YRIIGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 593 RIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ---TMQDDVStgerslNREKLAVLKQA 669
Cdd:cd01380 157 NMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQggsPVIDGVD------DAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 670 LNVVGFSNLEVENLFVILAAILHLGDIRFTAlTEGNSAFVS-DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 748
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKA-TRNDSASISpDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 749 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 828
Cdd:cd01380 310 LTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 829 EVLFLHEQVECVQEGVTMETAYSPGNQnGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL-QSLLESSntNAVYSPL 907
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDFYDNQ-PCID-LIEGKLGILDLLDEECRLPKGSDENWAQKLyNQHLKKP--NKHFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 908 KDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvvinhlfqsklsqtgslvsaypsfkfr 987
Cdd:cd01380 464 RFSN---------TAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 988 gHKSallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNN 1067
Cdd:cd01380 508 -RKK--------------------------------------------TVGSQFRDSLILLMETLNSTTPHYVRCIKPND 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1068 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA---DTFLREKKEHLAAERCRLVLQQCKlqgW 1144
Cdd:cd01380 543 EKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLpskEWLRDDKKKTCENILENLILDPDK---Y 619
|
730
....*....|
gi 1622884518 1145 QMGVRKVFLK 1154
Cdd:cd01380 620 QFGKTKIFFR 629
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
436-1147 |
1.04e-123 |
|
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: 1.04e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPK---EMPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 595
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG-VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF-DNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 596 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLhlNNLCAHRYLNQTMQDDVSTGERSLNREKLavlKQALNVVGF 675
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSLSGCIEVEGVDDVADFEEV---VLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 676 SNLEVENLFVILAAILHLGDIRFTALTEGNSAF---VSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG--DMIIRRHT 750
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 751 IQiAEFFRDLLAKSLYSRLFSFLVNTMNsclLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 830
Cdd:cd14872 311 AQ-ATDACDALAKAAYSRLFDWLVKKIN---ESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 831 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQsllessNTNAVYSPLKDG 910
Cdd:cd14872 387 TFKLEEALYQSEGVKFEHIDFIDNQP-VLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN------QTHAAKSTFVYA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 911 NgnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsayPSFKFRghk 990
Cdd:cd14872 460 E----VRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------PPSEGD--- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 991 sallskkmtassiigenknylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKL 1070
Cdd:cd14872 519 ---------------------------------------QKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1071 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREKKehLAAERCRLVLQ---QCKlQGWQM 1146
Cdd:cd14872 560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvKTIAKRVGP--DDRQRCDLLLKslkQDF-SKVQV 636
|
.
gi 1622884518 1147 G 1147
Cdd:cd14872 637 G 637
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
436-1154 |
1.92e-123 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 404.18 E-value: 1.92e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCF 514
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQY---SRRHLGELPPHIFAIANECYRCLWKRHDNQCI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 515 ILSGERGSGKSEASKQIIRHLT----------CRAASSR---AMLDSRfkhvmCILEAFGHAKTTLNDLSSCFIKYFELQ 581
Cdd:cd14873 78 LISGESGAGKTESTKLILKFLSvisqqslelsLKEKTSCveqAILESS-----PIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 582 FCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQT--MQDDVSTGERSLN 659
Cdd:cd14873 153 ICQ-KGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSgcVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 660 ReklaVLKqALNVVGFSNLEVENLFVILAAILHLGDIRFtaLTEGnSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 739
Cdd:cd14873 232 E----VIT-AMEVMQFSKEEVREVSRLLAGILHLGNIEF--ITAG-GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 740 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmqtldIGILDIFGFEEFQKNEFEQLCVNMT 819
Cdd:cd14873 304 LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS-----IGILDIFGFENFEVNHFEQFNINYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 820 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSlleSSN 899
Cdd:cd14873 379 NEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGE-CLD-LIEKKLGLLALINEESHFPQATDSTLLEKLHS---QHA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 900 TNAVYSPLKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvs 979
Cdd:cd14873 454 NNHFYVKPRVAVNN---------FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQ--- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 980 aypsfkfrghksallSKKMTASsiigenknylelskllkkkgtstflqrlERGDPvTIASQLRKSLTDIIGKLQKCTPHF 1059
Cdd:cd14873 522 ---------------DTLKCGS----------------------------KHRRP-TVSSQFKDSLHSLMATLSSSNPFF 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1060 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKkehlaaerCRL 1134
Cdd:cd14873 558 VRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmrnlaLPEDVRGK--------CTS 629
|
730 740
....*....|....*....|..
gi 1622884518 1135 VLQQCKLQG--WQMGVRKVFLK 1154
Cdd:cd14873 630 LLQLYDASNseWQLGKTKVFLR 651
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
437-1154 |
5.97e-122 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 400.30 E-value: 5.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKY---KGKRREEMPPHIFAIADNAYRNMLQDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKH-------VMC--ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQ 587
Cdd:cd01377 79 TGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledqiLQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGS-TG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 588 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ------TMQDDVstgerslnrE 661
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltiDGVDDA---------E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 662 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIqyFK 741
Cdd:cd01377 229 EFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPR--IK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 742 -GDMIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMT 819
Cdd:cd01377 307 vGREWVTKGqNKEQVVFSVGALAKALYERLFLWLVKRINKTL---DTKSKRQYF-IGVLDIAGFEIFEFNSFEQLCINYT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 820 NEKMHHYINEVLFLHEQVECVQEGVTMEtayspgnqngVLDF---------FFQKPS-GFLTLLDEESQMIWSMESNFPK 889
Cdd:cd01377 383 NEKLQQFFNHHMFVLEQEEYKKEGIEWT----------FIDFgldlqptidLIEKPNmGILSILDEECVFPKATDKTFVE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 890 KLQSLLESSNTN-AVYSPLKDGNGnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ 968
Cdd:cd01377 453 KLYSNHLGKSKNfKKPKPKKSEAH----------FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 969 SKLSQTGSlvsaypSFKFRGHKSALLskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDI 1048
Cdd:cd01377 523 DYEESGGG------GGKKKKKGGSFR-----------------------------------------TVSQLHKEQLNKL 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1049 IGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLA 1128
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGK 635
|
730 740
....*....|....*....|....*...
gi 1622884518 1129 AErCRLVLQQCKL--QGWQMGVRKVFLK 1154
Cdd:cd01377 636 AA-CEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
437-1154 |
1.73e-119 |
|
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: 393.67 E-value: 1.73e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcsSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSI----SKSPHVFSTASSAYQGMCNNKKSQTIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASS---RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQ----- 587
Cdd:cd14888 78 ISGESGAGKTESTKYVMKFLACAGSEDikkRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKSkrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 588 ---QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL--NNLCAHR-YLNQTMQDDVSTGERSLNRE 661
Cdd:cd14888 158 drgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYeeNDEKLAKgADAKPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 662 KLAV-----------LKQ------ALNVVGFSNLEVENLFVILAAILHLGDIRFT---ALTEGNSAFVSDLQLLEQVAGM 721
Cdd:cd14888 238 YLTKsschelpdvddLEEfestlyAMQTVGISPEEQNQIFSIVAAILYLGNILFEnneACSEGAVVSASCTDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 722 LQVSTDELASALTTDiqyfkgdMIIRRH-------TIQIAEFFRDLLAKSLYSRLFSFLVNTMNScllSQDEQRSMQTLD 794
Cdd:cd14888 318 LGVDAEDLLNALCYR-------TIKTAHefytkplRVDEAEDVRDALARALYSCLFDKVVERTNE---SIGYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 795 IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLD 874
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCV-DLLQEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 875 EESQmiwsmesnFPK-KLQSLlessnTNAVYSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLF 953
Cdd:cd14888 467 EECF--------VPGgKDQGL-----CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 954 VMKTSENVVINHLFQSKLSqtgslvsaypsfkfRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergd 1033
Cdd:cd14888 534 VIKNSKNPFISNLFSAYLR--------------RGTDGNTKKKKF----------------------------------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1034 pVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYK 1113
Cdd:cd14888 565 -VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYR 643
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1622884518 1114 PLADTFLREkkehlaaercrlvlqqcKLQGWQMGVRKVFLK 1154
Cdd:cd14888 644 ILLNGEGKK-----------------QLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
438-1112 |
5.53e-119 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 392.09 E-value: 5.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFS-----SSGKLCSSLPPHLFSCVERAFHQLFQEQRP 511
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiiqnGEYFDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 512 QCFILSGERGSGKSEASKQIIRHLT-------------CRAASSRAMLDSRF----KHVMC--ILEAFGHAKTTLNDLSS 572
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTqlsqqeqnseevlTLTSSIRATSKSTKsieqKILSCnpILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 573 CFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCA---HRYLNQTMQD 649
Cdd:cd14907 163 RFGKYVSILVDKKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 650 DVSTgersLNREKL-AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRF--TALTEGNSAFVSDLQLLEQVAGMLQVST 726
Cdd:cd14907 243 EVDT----INDEKLfKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGIDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 727 DELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLL--SQDEQRSMQ--TLDIGILDIFG 802
Cdd:cd14907 319 EELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMpkDEKDQQLFQnkYLSIGLLDIFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 803 FEEFQKNEFEQLCVNMTNEKMHH-YINEVlFLHEQVECVQEGVT---METAYsPGNQNgVLDFFFQKPSGFLTLLDEESQ 878
Cdd:cd14907 399 FEVFQNNSFEQLCINYTNEKLQQlYISYV-FKAEEQEFKEEGLEdylNQLSY-TDNQD-VIDLLDKPPIGIFNLLDDSCK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 879 MIWSMESNFPKKLQSLLESSNTNAVYSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTS 958
Cdd:cd14907 476 LATGTDEKLLNKIKKQHKNNSKLIFPNKINK-----------DTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 959 ENVVINHLF----QSKLSQTGSLVSAYPSFKFRGHKsallskkmtassiigenknylelskllkkkgtstflqrlergdp 1034
Cdd:cd14907 545 KNRIISSIFsgedGSQQQNQSKQKKSQKKDKFLGSK-------------------------------------------- 580
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884518 1035 vtiasqLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1112
Cdd:cd14907 581 ------FRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQY 652
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
437-1154 |
3.99e-115 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 380.28 E-value: 3.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14896 2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASY---HPRKALNTTPHIFAIAASAYRLSQSTGQDQCILL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqfCERKQQLTGARIYT 596
Cdd:cd14896 79 SGHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRL--HLQHGVIVGASVSH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSlnrEKLAVLKQALNVVGFS 676
Cdd:cd14896 157 YLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDA---QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 677 NLEVENLFVILAAILHLGDIRFTAlTEGNS---AFVSDLQLLEQVAGMLQVSTDELASALT---TDIQYfkgDMIIRRHT 750
Cdd:cd14896 234 AEELTAIWAVLAAILQLGNICFSS-SERESqevAAVSSWAEIHTAARLLQVPPERLEGAVThrvTETPY---GRVSRPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 751 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 830
Cdd:cd14896 310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAT--IGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 831 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkkLQSLLESSNTNAVYS----P 906
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIPQPPRES-CLDLLVDQPHSLLSILDDQTWLSQATDHTF---LQKCHYHHGDHPSYAkpqlP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 907 LKdgngnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkf 986
Cdd:cd14896 464 LP-------------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYG----------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 987 rghksallskkmtassiigenknylelskllkkkgtstflqrLERGDPvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPN 1066
Cdd:cd14896 520 ------------------------------------------LGQGKP-TLASRFQQSLGDLTARLGRSHVYFIHCLNPN 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1067 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADtflREKKEHLAAERCRLVLQQckLQG--- 1143
Cdd:cd14896 557 PGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS---ERQEALSDRERCGAILSQ--VLGaes 631
|
730
....*....|...
gi 1622884518 1144 --WQMGVRKVFLK 1154
Cdd:cd14896 632 plYHLGATKVLLK 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
437-1154 |
8.32e-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: 8.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRP---- 511
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLY---HGTTAGELPPHVFAIADHAYTQLIQSGVLdpsn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 512 QCFILSGERGSGKSEASKQIIRHLTcRAASSRA-------------------MLDSRFKHVMCILEAFGHAKTTLNDLSS 572
Cdd:cd14890 79 QSIIISGESGAGKTEATKIIMQYLA-RITSGFAqgasgegeaaseaieqtlgSLEDRVLSSNPLLESFGNAKTLRNDNSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 573 CFIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQtmQDDVS 652
Cdd:cd14890 158 RFGKFIEIQF-DHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRG--ECSSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 653 TGERslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG-NSAFVSDLQLLEQVAGMLQVSTDELAS 731
Cdd:cd14890 235 PSCD--DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTtVLEDATTLQSLKLAAELLGVNEDALEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 732 ALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEF 811
Cdd:cd14890 313 ALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGF----IGVLDIYGFEKFEWNTF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 812 EQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQN-GVLDFFFQKPSG----FLTLLDeesqmIWSMESN 886
Cdd:cd14890 389 EQLCINYANEKLQRHFNQHMFEVEQVEYSNEGI--DWQYITFNDNqACLELIEGKVNGkpgiFITLDD-----CWRFKGE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 887 FP-KKLQSLLESSntnavYSPLKDGNGNVALK-----------DHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFV 954
Cdd:cd14890 462 EAnKKFVSQLHAS-----FGRKSGSGGTRRGSsqhphfvhpkfDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKEL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 955 MKTSEnvvinhlfqsklsqtgslvsaypsfkfrghksallskkmtaSSIigenknylelskllkkkgtstflqrleRGdp 1034
Cdd:cd14890 537 IKQSR-----------------------------------------RSI---------------------------RE-- 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1035 VTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKP 1114
Cdd:cd14890 547 VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQV 626
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1622884518 1115 LADTflREKKEHLAAERCRLvLQQCKLQgWQMGVRKVFLK 1154
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 ... |
438-1154 |
1.33e-113 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 376.41 E-value: 1.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQ----EQRPQC 513
Cdd:cd14892 3 LLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASSPPPHVFSIAERAYRAMKGvgkgQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 514 FILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVM------C------ILEAFGHAKTTLNDLSSCFIKYFELQ 581
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAhesieeCvllsnlILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 582 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStgERSLNRE 661
Cdd:cd14892 163 Y-NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVD--GVDDATE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 662 kLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALT--EGNSAFVSDLQLLEQVAGMLQVSTDELASALTTD-IQ 738
Cdd:cd14892 240 -FKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENAddEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQtTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 739 YFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSC---LLSQDEQRSM---QTLDIGILDIFGFEEFQKNEFE 812
Cdd:cd14892 319 TARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqQTSGVTGGAAsptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 813 QLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQNG-VLDFFFQKPSGFLTLLDEesQMIWSMESNfPKKL 891
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGI--DVSAIEFQDNQdCLDLIQKKPLGLLPLLEE--QMLLKRKTT-DKQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 892 QSLLESSN--TNAVYSPLKDGNgnvalkDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqs 969
Cdd:cd14892 474 LTIYHQTHldKHPHYAKPRFEC------DE---FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS----------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 970 klsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDII 1049
Cdd:cd14892 534 ---------------------------------------------------------------------SKFRTQLAELM 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1050 GKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA------DTFLREK 1123
Cdd:cd14892 545 EVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvAASPDAC 624
|
730 740 750
....*....|....*....|....*....|..
gi 1622884518 1124 KEHLAAERCR-LVLQQCKLQGWQMGVRKVFLK 1154
Cdd:cd14892 625 DATTARKKCEeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
437-1154 |
4.75e-110 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 366.41 E-value: 4.75e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLcsSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14903 2 AILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKE--ELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLtcrAASSRAMLDSRFK---HVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGAR 593
Cdd:cd14903 80 SGESGAGKTETTKILMNHL---ATIAGGLNDSTIKkiiEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF-DKNGTLVGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 594 IYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHrylnqTMQDDVSTGERSLNREKLAVLKQALNVV 673
Cdd:cd14903 156 CRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAY-----TGANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 674 GFSNLEVENLFVILAAILHLGDIRFTALT--EGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 751
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPndDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 752 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 831
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASL--GNDAKMANH--IGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 832 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKpSGFLTLLDEESQMIWSMESNFPKKLQSLLEsSNTNAVYSPlkdgn 911
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDFADNQD-VLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHK-DEQDVIEFP----- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 912 gnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKS 991
Cdd:cd14903 459 -----RTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 992 ALLSKkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLP 1071
Cdd:cd14903 534 ALTTT---------------------------------------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSP 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1072 DTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYkplaDTFLREKKEHL--AAERCRLVLQQCKLQG---WQM 1146
Cdd:cd14903 575 TELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKF----WLFLPEGRNTDvpVAERCEALMKKLKLESpeqYQM 650
|
....*...
gi 1622884518 1147 GVRKVFLK 1154
Cdd:cd14903 651 GLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
436-1154 |
3.49e-107 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 357.71 E-value: 3.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCF 514
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSY---QGKSLGTLPPHVFAIADKAYRDMKVLKQSQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 515 ILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 594
Cdd:cd01382 78 IVSGESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF-NEKSSVVGGFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 595 YTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLhlnnlcahryLNQTMQDDVstgerslnrEKLAVLKQALNVVG 674
Cdd:cd01382 157 SHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------LKDPLLDDV---------GDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 675 FSNLEVENLFVILAAILHLGDIRFTALTEGNSA----FVSDLQLLEQVAGMLQVSTDELASALTTDIQY-----FKGDMI 745
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgcnvKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQttrggAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 746 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeqRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 825
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE---TSSYF--IGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 826 YINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkklqsllessnTNAVYS 905
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEYVDNQD-CIDLIEAKLVGILDLLDEESKLPKPSDQHF------------TSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 906 PLKDgNGNVA------LKDHGT-----AFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 974
Cdd:cd01382 440 KHKN-HFRLSiprkskLKIHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 975 GSLVSAypsfkfrghksallSKKMTASSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLTDIIGKLQK 1054
Cdd:cd01382 519 KDSKQK--------------AGKLSFIS----------------------------------VGNKFKTQLNLLMDKLRS 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1055 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladTFLREKKEHLAAER-CR 1133
Cdd:cd01382 551 TGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYK----KYLPPKLARLDPRLfCK 626
|
730 740
....*....|....*....|...
gi 1622884518 1134 LVLQQCKLQG--WQMGVRKVFLK 1154
Cdd:cd01382 627 ALFKALGLNEndFKFGLTKVFFR 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
437-1154 |
9.95e-107 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 358.50 E-value: 9.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvsQLY----FSSSGKLCSSLPPHLFSCVERAF-------HQL 505
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYdlhkYREEMPGWTALPPHVFSIAEGAYrslrrrlHEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 506 FQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC---------ILEAFGHAKTTLNDLSSCFIK 576
Cdd:cd14895 75 GASKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISgsellsanpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 577 Y----FELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH--RYLNQTM--- 647
Cdd:cd14895 155 FvrmfFEGHELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQefQYISGGQcyq 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 648 -QDDVStgerslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN---------------SAFVSD 711
Cdd:cd14895 235 rNDGVR------DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 712 L---QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlSQDEQR 788
Cdd:cd14895 309 LtvqQHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS-PQRQFA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 789 SMQTLD--------IGILDIFGFEEFQKNEFEQLCVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNqNGVL 859
Cdd:cd14895 388 LNPNKAankdttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLqYQFIQDIL-LTEQQAHIEEGIKWNAVDYEDN-SVCL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 860 DFFFQKPSGFLTLLDEESQMIWSMESNFPKKL-QSLLESSNTNAVYSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVG 938
Cdd:cd14895 466 EMLEQRPSGIFSLLDEECVVPKGSDAGFARKLyQRLQEHSNFSASRTDQAD-----------VAFQIHHYAGAVRYQAEG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 939 AIEKNKDSLSQNLLFVMKTSENVVINHLFQS-KLSQTGSLVSAYPsfKFRGHKSALLSkkmtassiigenknylelskll 1017
Cdd:cd14895 535 FCEKNKDQPNAELFSVLGKTSDAHLRELFEFfKASESAELSLGQP--KLRRRSSVLSS---------------------- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1018 kkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 1097
Cdd:cd14895 591 -----------------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQ 653
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884518 1098 GYPVRLSFSDFLSRYKPLADTflREKKEHLAAErcrlVLQQCKLQGWQMGVRKVFLK 1154
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 ... |
437-1153 |
1.72e-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: 1.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGK---LCSSLPPHLFSCVERAFHQLFQEQRP-- 511
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGERraaGERKLPPHVYAVADKAFRAMLFASRGqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 512 --QCFILSGERGSGKSEASKQIIRHLTC--------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQ 581
Cdd:cd14901 82 cdQSILVSGESGAGKTETTKIIMNYLASvssatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 582 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGerSLNRE 661
Cdd:cd14901 162 F-ASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDG--VDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 662 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF-VSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFsMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 741 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTN 820
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASRF--IGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 821 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLeSSNT 900
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDA-CVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLL-AKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 901 NAVYSPLKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVInhlfqsklsqtgslvsa 980
Cdd:cd14901 475 SFSVSKLQQGKRQ---------FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL----------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 981 ypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQKCTPHFI 1060
Cdd:cd14901 529 -----------------------------------------------------SSTVVAKFKVQLSSLLEVLNATEPHFI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1061 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTfLREKKEHL--AAERCRLVLQQ 1138
Cdd:cd14901 556 RCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPD-GASDTWKVneLAERLMSQLQH 634
|
730 740
....*....|....*....|
gi 1622884518 1139 CKLQG-----WQMGVRKVFL 1153
Cdd:cd14901 635 SELNIehlppFQVGKTKVFL 654
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
437-1112 |
2.75e-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: 349.63 E-value: 2.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRD---KLQPHVYATSTAAYKHMLTNEMNQSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 595
Cdd:cd14904 79 VSGESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF-DGRGKLIGAKCE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 596 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGersLNREKL-AVLKQALNVVG 674
Cdd:cd14904 158 TYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPG---LDDAKLfASTQKSLSLIG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 675 FSNLEVENLFVILAAILHLGDIRFTALTEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 754
Cdd:cd14904 235 LDNDAQRTLFKILSGVLHLGEVMFDKSDENGSR-ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 755 EFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 834
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ---IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 835 EQVECVQEGVTMETAYSPGNQnGVLDFFFQKpSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntnavysplKDGNGNV 914
Cdd:cd14904 391 VEEEYIREGLQWDHIEYQDNQ-GIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQT----------KKDNESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 915 AL-KDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvSAYPSfkfrghksal 993
Cdd:cd14904 459 DFpKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---------SEAPS---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 994 lSKKMTASsiiGENKNylelskllkkkgtstflqrlergDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDT 1073
Cdd:cd14904 520 -ETKEGKS---GKGTK-----------------------APKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE 572
|
650 660 670
....*....|....*....|....*....|....*....
gi 1622884518 1074 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1112
Cdd:cd14904 573 FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
437-1122 |
1.25e-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: 338.11 E-value: 1.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVsqLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLI--LNEYKDINQNKSPIPHIYAVALRAYQSMVSEKKNQSII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAML-------DSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCER 585
Cdd:cd14906 80 ISGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnNSIEKDILTsnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 586 KQQLTGARIYTYLLEKSRLVSQP-LGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLN-----------QTMQDDVS 652
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDarddvissfksQSSNKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 653 TGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNS-AFVSD--LQLLEQVAGMLQVSTDEL 729
Cdd:cd14906 240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKyAYQKDkvTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 730 ASALTTdiQYFK----GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQ-------TLDIGIL 798
Cdd:cd14906 320 KQALLN--RNLKaggrGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAggsnkknNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 799 DIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQ 878
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKE-CIELIEKKSDGILSLLDDECI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 879 MiwsmesnfPK-KLQSLLES-----SNTNAVYS-PLKDGngnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNL 951
Cdd:cd14906 477 M--------PKgSEQSLLEKynkqyHNTNQYYQrTLAKG-----------TLGIKHFAGDVTYQTDGWLEKNRDSLYSDV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 952 LFVMKTSENVVINHLFQSKLSQTGSlvsaypsfkfrghksalLSKKMTASsiigenknylelskllkkkgtstflqrler 1031
Cdd:cd14906 538 EDLLLASSNFLKKSLFQQQITSTTN-----------------TTKKQTQS------------------------------ 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1032 gdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSR 1111
Cdd:cd14906 571 ---NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSR 647
|
730
....*....|.
gi 1622884518 1112 YKPLADTFLRE 1122
Cdd:cd14906 648 YKCIVDMYNRK 658
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
433-1157 |
7.10e-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: 327.97 E-value: 7.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 433 LNDGSLLYEIQKRFGNNQIYTFIGD-ILLLVNPYKELPIYS--SM---VSQLYFSSSGKLcSSLPPHLFSCVERAFHQLF 506
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSdaSLgeyGSEYYDTTSGSK-EPLPPHAYDLAARAYLRMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 507 QEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSR--AMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCE 584
Cdd:cd14879 80 RRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkgTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 585 RKQqLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLA 664
Cdd:cd14879 160 RGR-LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGCHPLPLGPGSDDAEGFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 665 VLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 742
Cdd:cd14879 239 ELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGeeSAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVRK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 743 DmiirRHTI----QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQtldIGILDIFGFEEF---QKNEFEQLC 815
Cdd:cd14879 319 E----LCTVfldpEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATF---ISLLDFPGFQNRsstGGNSLDQFC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 816 VNMTNEKMHHYINEVLFLHEQVECVQEGVTM-ETAYsPGNQnGVLDFFFQKPSGFLTLLDEESqmiwsmeSNFPKKL-QS 893
Cdd:cd14879 392 VNFANERLHNYVLRSFFERKAEELEAEGVSVpATSY-FDNS-DCVRLLRGKPGGLLGILDDQT-------RRMPKKTdEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 894 LLES-SNTNAVYSPLKDGNGNVALKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktsenvvinhlfqskls 972
Cdd:cd14879 463 MLEAlRKRFGNHSSFIAVGNFATRSGSAS-FTVNHYAGEVTYSVEGFLERNGDVLS------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 973 qtGSLVSAypsfkFRGhksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLTDIIGKL 1052
Cdd:cd14879 518 --PDFVNL-----LRG-------------------------------------------------ATQLNAALSELLDTL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1053 QKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEHLAAERC 1132
Cdd:cd14879 542 DRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKST----LRGSAAERIRQCA 617
|
730 740
....*....|....*....|....*..
gi 1622884518 1133 RLVLQQCKLQGWqMGVRKVFLKY--WH 1157
Cdd:cd14879 618 RANGWWEGRDYV-LGNTKVFLSYaaWR 643
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
437-1136 |
1.00e-94 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 323.77 E-value: 1.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-----FSSSGKLCSSLPPHLFSCVERAFHQLFQEQR 510
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtSTSPVSQLSELPPHVFAIGGKAFGGLLKPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 511 P-QCFILSGERGSGKSEASKQIIRHLTC---------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFEL 580
Cdd:cd14902 82 RnQSILVSGESGSGKTESTKFLMQFLTSvgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 581 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ---TMQDDVSTGERS 657
Cdd:cd14902 162 QF-GANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 658 LNREKLAVlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF-VSDLQL--LEQVAGMLQVSTDELASALT 734
Cdd:cd14902 241 AQLYVETV--RAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATaVTAASRfhLAKCAELMGVDVDKLETLLS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 735 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLV----NTMN---SCLLSQDEQRSMQTldIGILDIFGFEEFQ 807
Cdd:cd14902 319 SREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVrrlsDEINyfdSAVSISDEDEELAT--IGILDIFGFESLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 808 KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsmesnf 887
Cdd:cd14902 397 RNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDDKSNGLFSLLDQECLM-------- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 888 PKKLQsllESSNTNAVYSPLKDGNgnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVInhlf 967
Cdd:cd14902 468 PKGSN---QALSTKFYRYHGGLGQ-----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 968 qsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKnylelskllkkkgtstflQRLERGDPVTIAS---QLRKS 1044
Cdd:cd14902 530 -----------------------VAIGADENRDSPGADNGA------------------AGRRRYSMLRAPSvsaQFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1045 LTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADT 1118
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFkcflstRDR 648
|
730
....*....|....*...
gi 1622884518 1119 FLREKKEHLAAERCRLVL 1136
Cdd:cd14902 649 AAKMNNHDLAQALVTVLM 666
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
438-1116 |
2.27e-94 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 320.45 E-value: 2.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFG--NNQIYTFIGDILLLVNPYKELPiySSMVSqLYFSSSGKLCsslPPHLFSCVERAFHQLF---QEQRPQ 512
Cdd:cd14891 3 ILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPDKS-DYINTPLDPC---PPHPYAIAEMAYQQMClgsGRMQNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 513 CFILSGERGSGKSEASKQIIRHLTCRAASSRAM------------------LDSRFKHVMCILEAFGHAKTTLNDLSSCF 574
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFLTTRAVGGKKAsgqdieqsskkrklsvtsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 575 IKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTG 654
Cdd:cd14891 157 GKFMKLQFTKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQS---GCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 655 ERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRF----TALTEGNSAFVSDLQLLEQVAGMLQVSTDELA 730
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 731 SALTT-DIQYFKGDMIIRRhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQ-K 808
Cdd:cd14891 314 KVITQrEIVTRGETFTIKR-NAREAVYSRDAIAKSIYERLFLWIVQQINTSL----GHDPDPLPYIGVLDIFGFESFEtK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 809 NEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwSMESNfp 888
Cdd:cd14891 389 NDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRE-CLDLIASKPNGILPLLDNEARN--PNPSD-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 889 KKLQSLLESSNTNAVYSPLKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLlfvmktsENVVinhlfq 968
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHP------KDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDF-------EDLL------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 969 sklsqtgslvsaypsfkfrgHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLTDi 1048
Cdd:cd14891 525 --------------------ASSAKFSDQM--------------------------------------------QELVD- 539
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884518 1049 igKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1116
Cdd:cd14891 540 --TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVL 605
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
437-1124 |
5.63e-94 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 320.70 E-value: 5.63e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFS---------SSGKlcsSLPPHLFSCVERAFHQLFQ 507
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqgiESPQ---ALGPHVFAIADRSYRQMMS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 508 EQRP-QCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDS-----------RFKHVMCILEAFGHAKTTLNDLSSCFI 575
Cdd:cd14908 79 EIRAsQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimdRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 576 KYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH-----RYLNQTMQDD 650
Cdd:cd14908 159 KFIELGF-NRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpNEFHYTGQGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 651 VSTGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF---VSDLQLLEQVAGMLQVSTD 727
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEiaeEGNEKCLARVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 728 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLL--SQDEQRSmqtlDIGILDIFGFEE 805
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRS----SVGVLDIFGFEC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 806 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQM-IWSME 884
Cdd:cd14908 394 FAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQD-CLDTIQAKKKGILTMLDDECRLgIRGSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 885 SNFPKKLqsllessntNAVYSPLKDGNGNVALKDHGTA-------FTIMHYAGRVMYDV-VGAIEKNKDSLSqnllfvmK 956
Cdd:cd14908 473 ANYASRL---------YETYLPEKNQTHSENTRFEATSiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIP-------L 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 957 TSENvvinhLFQSklsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvt 1036
Cdd:cd14908 537 TADS-----LFES------------------------------------------------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1037 iASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1116
Cdd:cd14908 545 -GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLL 623
|
....*...
gi 1622884518 1117 DTFLREKK 1124
Cdd:cd14908 624 PLIPEVVL 631
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
437-1154 |
1.35e-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: 1.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14929 2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRA-----MLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLTG 591
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESkkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM-LSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 592 ARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDG--------LSAEEKHGLHLnnlCAHRYLNQTMQDDVstgerslnrEKL 663
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGkkelrdllLVSANPSDFHF---CSCGAVAVESLDDA---------EEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 664 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 744 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 823
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVL---DAKLSRQFF-IGILDITGFEILDYNSLEQLCINFTNEKL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 824 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSMESNFPKKLqslLESSNTNAV 903
Cdd:cd14929 382 QQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKL---FDNHFGKSV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 904 Y--SPLKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqTGSlvsay 981
Cdd:cd14929 458 HfqKPKPDK------KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIS-TDS----- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 982 psfkfrghksallskkmtaSSIIGENKNylelskllkKKGTSTFLqrlergdpvtIASQLRKSLTDIIGKLQKCTPHFIH 1061
Cdd:cd14929 526 -------------------AIQFGEKKR---------KKGASFQT----------VASLHKENLNKLMTNLKSTAPHFVR 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1062 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREK--KEHLAAERCRLVLQQ 1138
Cdd:cd14929 568 CINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILnPRTFPKSKfvSSRKAAEELLGSLEI 647
|
730
....*....|....*.
gi 1622884518 1139 CKLQgWQMGVRKVFLK 1154
Cdd:cd14929 648 DHTQ-YRFGITKVFFK 662
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
425-1192 |
1.19e-91 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 317.74 E-value: 1.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 425 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQ 504
Cdd:PTZ00014 99 GDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDS--DKLPPHVFTTARRALEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 505 LFQEQRPQCFILSGERGSGKSEASKQIIRHLtcrAASSRAMLDSRF-KHVMC---ILEAFGHAKTTLNDLSSCFIKYFEL 580
Cdd:PTZ00014 177 LHGVKKSQTIIVSGESGAGKTEATKQIMRYF---ASSKSGNMDLKIqNAIMAanpVLEAFGNAKTIRNNNSSRFGRFMQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 581 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTGE 655
Cdd:PTZ00014 254 QL-GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLdvpgiDDVKDFE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 656 RSLnreklavlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG---NSAFVSD--LQLLEQVAGMLQVSTDELA 730
Cdd:PTZ00014 333 EVM---------ESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDesLEVFNEACELLFLDYESLK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 731 SALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNE 810
Cdd:PTZ00014 404 KELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVF----IGMLDIFGFEVFKNNS 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 811 FEQLCVNMTNEKMH-HYINeVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPK 889
Cdd:PTZ00014 480 LEQLFINITNEMLQkNFVD-IVFERESKLYKDEGISTEELEYTSNES-VIDLLCGKGKSVLSILEDQCLAPGGTDEKFVS 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 890 KLQSLLESsntNAVYSPLK-DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ 968
Cdd:PTZ00014 558 SCNTNLKN---NPKYKPAKvDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 969 SKLSQTGSlvsaypsfkfrghksalLSKKMtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDI 1048
Cdd:PTZ00014 626 GVEVEKGK-----------------LAKGQ-------------------------------------LIGSQFLNQLDSL 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1049 IGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLA 1128
Cdd:PTZ00014 652 MSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL-DLAVSNDSSLDP 730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 1129 AERCRLVLQQCKL--QGWQMGVRKVFLKYWHADQLNdlclQLQRKIITCQK--------VIRGFLARQHLLQKI 1192
Cdd:PTZ00014 731 KEKAEKLLERSGLpkDSYAIGKTMVFLKKDAAKELT----QIQREKLAAWEplvsvleaLILKIKKKRKVRKNI 800
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
437-1143 |
2.41e-89 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 305.31 E-value: 2.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS--------LPPHLFSCVERAFHQ--- 504
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLLSFEARSSStrnkgsdpMPPHIYQVAGEAYKAmml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 505 -LFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCI----------LEAFGHAKTTLNDLSSC 573
Cdd:cd14900 82 gLNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIaakvlqtnilLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 574 FIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGlSAEEKHGLHLnnlcahryLNQTMqddvst 653
Cdd:cd14900 162 FGKFIKLHF-TSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG-ASEAARKRDM--------YRRVM------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 654 gerslnreklavlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDL-----QLLEQVAGMLQVST 726
Cdd:cd14900 226 --------------DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrlGQLKSDLapssiWSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 727 DELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLD-IGILDIFGFEE 805
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHfIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 806 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMES 885
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQD-CVNLISQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 886 NFPKKLQSLLEsSNTNAVYSPLKDGNGnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinH 965
Cdd:cd14900 451 TLASKLYRACG-SHPRFSASRIQRARG---------LFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------D 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 966 LFQSKLsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiasQLRKSL 1045
Cdd:cd14900 509 LFVYGL--------------------------------------------------------------------QFKEQL 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1046 TDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtflREKKE 1125
Cdd:cd14900 521 TTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLA----RAKNR 596
|
730
....*....|....*...
gi 1622884518 1126 HLAAERCRLVLQQCKLQG 1143
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 ... |
437-1154 |
3.95e-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: 3.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASS-----------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFE 579
Cdd:cd14911 79 TGESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 580 LQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTG 654
Cdd:cd14911 159 INF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLpvpgvDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 655 ERSLNreklavlkqALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALT 734
Cdd:cd14911 238 QATVK---------SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 735 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQL 814
Cdd:cd14911 309 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL---DRTKRQGASFIGILDMAGFEIFELNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 815 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSl 894
Cdd:cd14911 386 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKLVS- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 895 LESSNTNAVYSPLKdgngnvalkdhGTA-FTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsq 973
Cdd:cd14911 464 AHSMHPKFMKTDFR-----------GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD---- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 974 tgslvsaypsfkfrghksallskkmtaSSIIGenknylelsKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQ 1053
Cdd:cd14911 529 ---------------------------AEIVG---------MAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLR 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1054 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT-----FLREKKEhla 1128
Cdd:cd14911 573 NTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNvipkgFMDGKKA--- 649
|
730 740
....*....|....*....|....*...
gi 1622884518 1129 aerCRLVLQQCKLQG--WQMGVRKVFLK 1154
Cdd:cd14911 650 ---CEKMIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
437-1154 |
7.06e-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: 7.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY---RGKKRHEMPPHIYAISESAYRCMLQDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQ 588
Cdd:cd14920 79 TGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 589 LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-----TMQDDvstgerslnREKL 663
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNgyipiPGQQD---------KDNF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 664 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd14920 229 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 744 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 823
Cdd:cd14920 309 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 824 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLQSllESSNTN 901
Cdd:cd14920 386 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 902 AVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG-SLVSA 980
Cdd:cd14920 464 KFQKPRQ-------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGlDQVTG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 981 YPSFKFrghKSALLSKKmtassiigenknylelskllkkkgtstflqrlerGDPVTIASQLRKSLTDIIGKLQKCTPHFI 1060
Cdd:cd14920 536 MTETAF---GSAYKTKK----------------------------------GMFRTVGQLYKESLTKLMATLRNTNPNFV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1061 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA-----DTFLREKkehlaaERCRLV 1135
Cdd:cd14920 579 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpnaipKGFMDGK------QACERM 652
|
730 740
....*....|....*....|.
gi 1622884518 1136 LQQCKLQG--WQMGVRKVFLK 1154
Cdd:cd14920 653 IRALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
445-1154 |
8.50e-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: 8.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 445 RFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGK 524
Cdd:cd14876 10 RYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPD--LTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 525 SEASKQIIRHLtcrAASSRAMLDSRF-KHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGArIYTYLLE 600
Cdd:cd14876 88 TEATKQIMRYF---ASAKSGNMDLRIqTAIMAanpVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS-VVAFLLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 601 KSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTGERslnreklavLKQALNVVGF 675
Cdd:cd14876 164 KSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLdvpgiDDVADFEE---------VLESLKSMGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 676 SNLEVENLFVILAAILHLGDIRFTALTEG---NSAFVS--DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 750
Cdd:cd14876 235 TEEQIDTVFSIVSGVLLLGNVKITGKTEQgvdDAAAISneSLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 751 IQIAEFFRDLLAKSLYSRLFSFLVNTMNScllSQDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINe 829
Cdd:cd14876 315 KDDAEMLKLSLAKAMYDKLFLWIIRNLNS---TIEPPGGFKNF-MGMLDIFGFEVFKNNSLEQLFINITNEMLQkNFID- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 830 VLFLHEQVECVQEGV-TMETAYSPGNQngVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVYSPLK 908
Cdd:cd14876 390 IVFERESKLYKDEGIpTAELEYTSNAE--VIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS---NGKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 909 -DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkfr 987
Cdd:cd14876 465 vDSNIN---------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG------------ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 988 ghksallskKMTASSIIGenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDIIGKLQKCTPHFIHCIRPNN 1067
Cdd:cd14876 524 ---------KIAKGSLIG---------------------------------SQFLKQLESLMGLINSTEPHFIRCIKPNE 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1068 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLAAERCRLVLQQCKL--QGWQ 1145
Cdd:cd14876 562 TKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL-DLGIANDKSLDPKVAALKLLESSGLseDEYA 640
|
....*....
gi 1622884518 1146 MGVRKVFLK 1154
Cdd:cd14876 641 IGKTMVFLK 649
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
437-1154 |
1.45e-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: 1.45e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAM--------------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQF 582
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPgkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 583 CErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLN-NLCAHRYLNQ--TMQDDVSTGErsln 659
Cdd:cd14927 159 GP-TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQgvTTVDNMDDGE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 660 reKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 739
Cdd:cd14927 234 --ELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 740 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 819
Cdd:cd14927 312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFF----IGVLDIAGFEIFEFNSFEQLCINFT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 820 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLES 897
Cdd:cd14927 388 NEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACID-LIEKPLGILSILEEECMFPKASDASFKAKLydNHLGKS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 898 SNTNavySPLKDGNgnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgsl 977
Cdd:cd14927 467 PNFQ---KPRPDKK-----RKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSD--- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 978 vSAYPsfkfrgHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpvTIASQLRK-SLTDIIGKLQKCT 1056
Cdd:cd14927 536 -STED------PKSGVKEKRKKAASF--------------------------------QTVSQLHKeNLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1057 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADTFLREKKehlAAE 1130
Cdd:cd14927 577 PHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILnpsaipDDKFVDSRK---ATE 653
|
730 740
....*....|....*....|....
gi 1622884518 1131 RCRLVLQQCKLQgWQMGVRKVFLK 1154
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 ... |
437-1154 |
4.02e-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: 302.91 E-value: 4.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14909 2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMY---RGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASS--------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQ 588
Cdd:cd14909 79 TGESGAGKTENTKKVIAYFATVGASKktdeaaksKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP-TGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 589 LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLNQ--TMQDDVSTGErslnreKLAV 665
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQgkVTVPNVDDGE------EFSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 666 LKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 745
Cdd:cd14909 232 TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 746 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 825
Cdd:cd14909 312 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL---DTQQKRQHF-IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 826 YINEVLFLHEQVECVQEGVtmETAYspgnqngvLDF---------FFQKPSGFLTLLDEESQMIWSMESNFPKKLQSL-L 895
Cdd:cd14909 388 FFNHHMFVLEQEEYKREGI--DWAF--------IDFgmdllacidLIEKPMGILSILEEESMFPKATDQTFSEKLTNThL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 896 ESSNTNAVYSPLKDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG 975
Cdd:cd14909 458 GKSAPFQKPKPPKPGQ-------QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 976 SLVSAYPSfkfRGHKSALLSkkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKC 1055
Cdd:cd14909 531 GGEQAKGG---RGKKGGGFA----------------------------------------TVSSAYKEQLNSLMTTLRST 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1056 TPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR-EKKEHLAAERCrl 1134
Cdd:cd14909 568 QPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQgEEDPKKAAEII-- 645
|
730 740
....*....|....*....|..
gi 1622884518 1135 vLQQCKL--QGWQMGVRKVFLK 1154
Cdd:cd14909 646 -LESIALdpDQYRLGHTKVFFR 666
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
436-1154 |
1.37e-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: 1.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDS--------RFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 587
Cdd:cd14921 78 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 588 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLavlk 667
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 668 QALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 747
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 748 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 827
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 828 NEVLFLHEQVECVQEGV-------------TMETAYSPGNqngvldfffqkPSGFLTLLDEESQMIWSMESNFPKKLQSl 894
Cdd:cd14921 390 NHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCT- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 895 lESSNTNAVYSPLKdgngnvaLKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 974
Cdd:cd14921 458 -EQGNHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 975 GSLVSAypsfkfrghksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQK 1054
Cdd:cd14921 529 GLDQMA----------------KMTESSLPSASKT--------------------KKGMFRTVGQLYKEQLGKLMTTLRN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1055 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRL 1134
Cdd:cd14921 573 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACIL 651
|
730 740
....*....|....*....|..
gi 1622884518 1135 VLQQCKLQG--WQMGVRKVFLK 1154
Cdd:cd14921 652 MIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
437-1154 |
2.57e-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: 297.49 E-value: 2.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLF-QEQRPQCF 514
Cdd:cd14875 2 TLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDP--RLLPPHIWQVAHKAFNAIFvQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 515 ILSGERGSGKSEASKQII------RHLTCRAASSRAM---LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCER 585
Cdd:cd14875 80 VISGESGSGKTENAKMLIaylgqlSYMHSSNTSQRSIadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 586 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGL-HLNNLCAHRYLN--QTMQDDVSTGERSLNREK 662
Cdd:cd14875 160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNggNTFVRRGVDGKTLDDAHE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 663 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTAlTEGNSAFVSDLQLLEQVAGMLQVSTDELASALttdiqyfkg 742
Cdd:cd14875 240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLRECF--------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 743 dmIIRRHT--IQI------AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQL 814
Cdd:cd14875 310 --LVKSKTslVTIlankteAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGCKY--IGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 815 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSl 894
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECV-NMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWD- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 895 lESSNTNAVYSPLKDGNGNvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqt 974
Cdd:cd14875 464 -QWANKSPYFVLPKSTIPN--------QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIR---------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 975 gSLVSAYPSFKFRGHksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQK 1054
Cdd:cd14875 525 -TLLSTEKGLARRKQ----------------------------------------------TVAIRFQRQLTDLRTELES 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1055 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFlSRY------KPLADTFlreKKEHLA 1128
Cdd:cd14875 558 TETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF-CRYfylimpRSTASLF---KQEKYS 633
|
730 740 750
....*....|....*....|....*....|.
gi 1622884518 1129 AERCRLVLQQCKLQGWQ-----MGVRKVFLK 1154
Cdd:cd14875 634 EAAKDFLAYYQRLYGWAkpnyaVGKTKVFLR 664
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
436-1154 |
1.17e-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: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMY---KGKKRTEMPPHLFSISDNAYHDMLMDRENQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTC------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQL 589
Cdd:cd14934 78 ITGESGAGKTENTKKVIQYFANiggtgkQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT-TGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 590 TGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLNQ--TMQDDVSTGErslnreKLAVL 666
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQgvTVVDNMDDGE------ELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 667 KQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 746
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 747 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 826
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTL----DTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 827 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNtnavY 904
Cdd:cd14934 387 FNHHMFVLEQEEYKREGIEWVFIDFGLDLQACID-LLEKPMGIFSILEEQCVFPKATDATFKAALydNHLGKSSN----F 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 905 SPLKDGNGnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvsaypsf 984
Cdd:cd14934 462 LKPKGGKG----KGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS-------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 985 kfrghksallSKKMTASSIIgenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIR 1064
Cdd:cd14934 530 ----------KKQKRGSSFM-------------------------------TVSNFYREQLNKLMTTLHSTAPHFVRCIV 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1065 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKKehlAAErcrLVLQQC 1139
Cdd:cd14934 569 PNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLnpnviPQGFVDNKK---ASE---LLLGSI 642
|
730
....*....|....*..
gi 1622884518 1140 KLQ--GWQMGVRKVFLK 1154
Cdd:cd14934 643 DLDvnEYKIGHTKVFFR 659
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
436-1154 |
1.77e-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: 1.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAAS------------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFc 583
Cdd:cd14932 78 CTGESGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 584 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqtmqddvSTGERSL----N 659
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFL--------SNGNVTIpgqqD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 660 REKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 739
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 740 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 819
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 820 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSMESNFPKKLQSllES 897
Cdd:cd14932 386 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQ--EQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 898 SNTNAVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgsl 977
Cdd:cd14932 464 GNNPKFQKPKK-------LKDDAD-FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD-------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 978 vsaypsfkfrghksallskkmtASSIIGENKNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLTDIIGKLQKCTP 1057
Cdd:cd14932 528 ----------------------VDRIVGLDKVAGMGESLHGAFKTRKGMFR-------TVGQLYKEQLMNLMTTLRNTNP 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1058 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQ 1137
Cdd:cd14932 579 NFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMVK 657
|
730
....*....|....*....
gi 1622884518 1138 QCKLQG--WQMGVRKVFLK 1154
Cdd:cd14932 658 ALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
437-1154 |
7.98e-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: 7.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASS----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERK 586
Cdd:cd14913 79 TGESGAGKTVNTKRVIQYFATIAATGdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 587 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREK 662
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITT-------NPYDYPFISQGEILVasidDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 663 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 742
Cdd:cd14913 231 LLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 743 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEK 822
Cdd:cd14913 311 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL---DTKLPRQHF-IGVLDIAGFEIFEYNSLEQLCINFTNEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 823 MHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNt 900
Cdd:cd14913 387 LQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 901 navYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsa 980
Cdd:cd14913 465 ---FQKPKVVKGRAE-----AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 981 ypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFI 1060
Cdd:cd14913 526 -----FATADADSGKKKVAKKK-------------------GSSFQ---------TVSALFRENLNKLMSNLRTTHPHFV 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1061 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCK 1140
Cdd:cd14913 573 RCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASID 652
|
730
....*....|....*.
gi 1622884518 1141 LQ--GWQMGVRKVFLK 1154
Cdd:cd14913 653 IDhtQYKFGHTKVFFK 668
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
437-1154 |
6.01e-83 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 287.02 E-value: 6.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSR---SDNAPHIFSVADSAYQDMLHHEEPQHIIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLtCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 596
Cdd:cd14882 79 SGESYSGKTTNARLLIKHL-CYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTF-GSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEK-HGLHLNNLCAHRYLnqtmQDDVSTGERSL---------NREKLAVL 666
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYL----RIPPEVPPSKLkyrrddpegNVERYKEF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 667 KQALNVVGFSNLEVENLFVILAAILHLGDIRFTaltEGN-SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 745
Cdd:cd14882 233 EEILKDLDFNEEQLETVRKVLAAILNLGEIRFR---QNGgYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 746 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeqRSM--QTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 823
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFP---RAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 824 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQmiwSMESnfpkklqsllessnTNAV 903
Cdd:cd14882 387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAV-DQLMTKPDGLFYIIDDASR---SCQD--------------QNYI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 904 YSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLVSAYPS 983
Cdd:cd14882 449 MDRIKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--SQVRNMRTLAAT 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 984 FKFrghkSALLSKKMTAssiIGENknylelskllkKKGTstflqrlergdpvtiasqlrksltdiigklqkctpHFIHCI 1063
Cdd:cd14882 527 FRA----TSLELLKMLS---IGAN-----------SGGT-----------------------------------HFVRCI 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1064 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEHLAAERCRLVLQQCKLQG 1143
Cdd:cd14882 554 RSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDF--DETVEMTKDNCRLLLIRLKMEG 631
|
730
....*....|.
gi 1622884518 1144 WQMGVRKVFLK 1154
Cdd:cd14882 632 WAIGKTKVFLK 642
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
436-1154 |
3.88e-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: 3.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAM-----LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLT 590
Cdd:cd14919 78 CTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 591 GARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLavlkQAL 670
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETM----EAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 671 NVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 750
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 751 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 830
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 831 LFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSMESNFPKKlqsLLESSNTNAVYSPLK 908
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEK---VVQEQGTHPKFQKPK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 909 DgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfrg 988
Cdd:cd14919 467 Q------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVA-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 989 hksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNS 1068
Cdd:cd14919 532 --------GMSETALPGAFKT--------------------RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHE 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1069 KLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQCKLQG--WQM 1146
Cdd:cd14919 584 KKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRI 662
|
....*...
gi 1622884518 1147 GVRKVFLK 1154
Cdd:cd14919 663 GQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
436-1154 |
9.33e-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: 9.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAAS------------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFc 583
Cdd:cd15896 78 CTGESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 584 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKL 663
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 664 avlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd15896 237 ----EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 744 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 823
Cdd:cd15896 313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 824 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLqsLLESSNTN 901
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKV--LQEQGTHP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 902 AVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsay 981
Cdd:cd15896 468 KFFKPKK-------LKDEAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 982 psfkfrghksalLSKKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIH 1061
Cdd:cd15896 534 ------------LDKVSGMSEMPGAFKT--------------------RKGMFRTVGQLYKEQLSKLMATLRNTNPNFVR 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1062 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQCKL 1141
Cdd:cd15896 582 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMIKSLEL 660
|
730
....*....|....*
gi 1622884518 1142 QG--WQMGVRKVFLK 1154
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 ... |
437-1115 |
1.90e-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: 277.75 E-value: 1.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAA----------SSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErK 586
Cdd:cd14917 79 TGESGAGKTVNTKRVIQYFAVIAAigdrskkdqtPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA-T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 587 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREK 662
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-------NPYDYAFISQGETTVasidDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 663 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 742
Cdd:cd14917 231 LMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 743 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEK 822
Cdd:cd14917 311 EYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 823 MHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNT 900
Cdd:cd14917 387 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSNNF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 901 NavysplKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsa 980
Cdd:cd14917 466 Q------KPRNIKGKPEAH---FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 981 ypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFI 1060
Cdd:cd14917 526 -----YAGADAPIEKGKGKAKK-------------------GSSFQ---------TVSALHRENLNKLMTNLRSTHPHFV 572
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884518 1061 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 1115
Cdd:cd14917 573 RCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
436-1113 |
2.67e-79 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 278.52 E-value: 2.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-------FSSSGKLCSSLPPHLFSCVERAFHQLFQ 507
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqFGDRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 508 EQRPQCFILSGERGSGKSEASKQIIRH--LTCRAAS---------------SRAMLDSRFKHVMCILEAFGHAKTTLNDL 570
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYfaVHCGTGNnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 571 SSCFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDG----LSAEEKHGLHLN-NLCAHRYLNQ 645
Cdd:cd14899 161 SSRFGKFIELRFRDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSgGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 646 TMQDDVSTGERslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG--NSAFVSDLQLLEQVAG--- 720
Cdd:cd14899 241 SLCSKRRDGVK--DGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKgdDTVFADEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 721 -------MLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQ--------- 784
Cdd:cd14899 319 hftkaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 785 ----DEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQnGVLD 860
Cdd:cd14899 399 sdvdDEEDATDF--IGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNR-ACLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 861 FFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAVYSplkdgngNVALKDHGTAFTIMHYAGRVMYDVVGAI 940
Cdd:cd14899 476 LFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFR-------SAPLIQRTTQFVVAHYAGCVTYTIDGFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 941 EKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSAllsKKMTASsiigenknylelskllkkk 1020
Cdd:cd14899 549 AKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRA---KSAIAA------------------- 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1021 gtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 1100
Cdd:cd14899 607 --------------VSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFP 672
|
730
....*....|...
gi 1622884518 1101 VRLSFSDFLSRYK 1113
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 ... |
436-1154 |
3.72e-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: 3.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 436 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY---RGKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 587
Cdd:cd14930 78 CTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 588 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqTMQDDVSTG-ERSLNREKLavl 666
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGqERELFQETL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 667 kQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 746
Cdd:cd14930 232 -ESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 747 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 826
Cdd:cd14930 311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 827 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLQSllESSNTNAVY 904
Cdd:cd14930 388 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQ--EQGGHPKFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 905 SPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS-----KLSQTGSLVS 979
Cdd:cd14930 466 RPRH-------LRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 980 AYPSFKFRghksallskkmtassiigenknylelskllkkkgtstflqrleRGDPVTIASQLRKSLTDIIGKLQKCTPHF 1059
Cdd:cd14930 538 GPPGGRPR-------------------------------------------RGMFRTVGQLYKESLSRLMATLSNTNPSF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1060 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQC 1139
Cdd:cd14930 575 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQAL 653
|
730
....*....|....*..
gi 1622884518 1140 KLQG--WQMGVRKVFLK 1154
Cdd:cd14930 654 ELDPnlYRVGQSKIFFR 670
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
442-1153 |
1.62e-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: 1.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 442 IQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERG 521
Cdd:cd14881 7 LQARFYAKEFFTNVGPILLSVNPYRDVG------NPLTLTSTRS--SPLAPQLLKVVQEAVRQQSETGYPQAIILSGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 522 SGKSEASKQIIRHLTCRAA---SSRAmldsrFKHV---MCILEAFGHAKTTLNDLSSCFIKYFELQFCErkQQLTGARIY 595
Cdd:cd14881 79 SGKTYASMLLLRQLFDVAGggpETDA-----FKHLaaaFTVLRSLGSAKTATNSESSRIGHFIEVQVTD--GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 596 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH--RYLNQtmqddvSTGERSLNREKLA--VLKQALN 671
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPAnlRYLSH------GDTRQNEAEDAARfqAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 672 VVGFSNLEVENlfvILAAILHLGDIRFTALTEGNSAFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 751
Cdd:cd14881 226 ILGIPFLDVVR---VLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 752 QIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLD--IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 829
Cdd:cd14881 302 NMSNMTRDALAKALYCRTVATIVRRANS-LKRLGSTLGTHATDgfIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 830 VLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESnFPKKLQslLESSNTNAVYSPlkd 909
Cdd:cd14881 381 HIFKSSIESCRDEGIQCEVEVDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTAES-YVAKIK--VQHRQNPRLFEA--- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 910 gngnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtsenvvinhlfqsklSQTGslvsaypSFKFRGH 989
Cdd:cd14881 455 ------KPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY---------------KQNC-------NFGFATH 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 990 ksallskkmtassiigenknylelskllkkkgTSTFLQRLErgdpvtiasqlrksltDIIGKLQKCTPHFIHCIRPNNSK 1069
Cdd:cd14881 507 --------------------------------TQDFHTRLD----------------NLLRTLVHARPHFVRCIRSNTTE 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1070 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQ------- 1142
Cdd:cd14881 539 TPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILQFLEAQppsklss 618
|
730
....*....|....
gi 1622884518 1143 ---GWQMGVRKVFL 1153
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 ... |
437-1154 |
3.93e-77 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 270.84 E-value: 3.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASS------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcE 584
Cdd:cd14912 79 TGESGAGKTVNTKRVIQYFATIAVTGekkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 585 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 660
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITT-------NPYDYPFVSQGEISVasidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 661 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:cd14912 231 EELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 741 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 820
Cdd:cd14912 311 GNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 821 EKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 898
Cdd:cd14912 387 EKLQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 899 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLV 978
Cdd:cd14912 466 N----FQKPKVVKGKAE-----AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG--AQTAEGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 979 SAYPSFKFRGHKSAllskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 1058
Cdd:cd14912 535 SAGGGAKKGGKKKG------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1059 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT------FLREKKehlAAERC 1132
Cdd:cd14912 576 FVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegqFIDSKK---ASEKL 652
|
730 740
....*....|....*....|..
gi 1622884518 1133 RLVLQQCKLQgWQMGVRKVFLK 1154
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 ... |
437-1122 |
5.63e-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: 5.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAA-----------SSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 585
Cdd:cd14916 79 TGESGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 586 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NRE 661
Cdd:cd14916 158 TGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTN-------NPYDYAFVSQGEVSVasidDSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 662 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 741
Cdd:cd14916 231 ELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 742 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNE 821
Cdd:cd14916 311 NEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 822 KMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSN 899
Cdd:cd14916 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLydNHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 900 TNavysplKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqtgslVS 979
Cdd:cd14916 466 FQ------KPRNVKGKQEAH---FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-----AD 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 980 AYPSFKFRGHKSAllskkmtassiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHF 1059
Cdd:cd14916 532 TGDSGKGKGGKKK-----------------------------GSSFQ---------TVSALHRENLNKLMTNLKTTHPHF 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884518 1060 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1122
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 ... |
437-1122 |
1.08e-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: 1.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASS------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcE 584
Cdd:cd14910 79 TGESGAGKTVNTKRVIQYFATIAVTGekkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 585 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 660
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITT-------NPYDYAFVSQGEITVpsidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 661 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:cd14910 231 EELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 741 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 820
Cdd:cd14910 311 GNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 821 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 898
Cdd:cd14910 387 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 899 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLV 978
Cdd:cd14910 466 N----FQKPKPAKGKVE-----AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 979 SAYPSFKFRGhksallskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 1058
Cdd:cd14910 537 GGKKGGKKKG----------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 1059 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1122
Cdd:cd14910 574 FVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
437-1122 |
1.74e-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: 1.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRA---------ASSRAM---LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCE 584
Cdd:cd14915 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 585 rKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 660
Cdd:cd14915 159 -TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITT-------NPYDFAFVSQGEITVpsidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 661 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 740
Cdd:cd14915 231 EELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 741 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 820
Cdd:cd14915 311 GNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 821 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 898
Cdd:cd14915 387 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 899 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinHLFQSKLSQTgslv 978
Cdd:cd14915 466 N----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV------------GLYQKSGMKT---- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 979 sayPSFKFRGHKSAllSKKMTASSIIGENKNylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 1058
Cdd:cd14915 521 ---LAFLFSGGQTA--EAEGGGGKKGGKKKG-------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 1059 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1122
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 ... |
442-1154 |
5.88e-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: 5.88e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 442 IQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLC--SSLPPHLFSCVERAFHQLFQEQRPQCFILSG 518
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSRGfpSDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 519 ERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIYTYL 598
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL-LVGPDGGLKGGKITSYM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 599 LEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGErslNREKLAVLKQALNVVgFSNL 678
Cdd:cd14886 166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGID---DQKEFAPVRSQLEKL-FSKN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 679 EVENLFVILAAILHLGDIRFTALTEG---NSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 755
Cdd:cd14886 242 EIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 756 FFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVlFLH 834
Cdd:cd14886 322 VNIRAVAKDLYGALFELCVDTLNEIIQFDADARPW----IGILDIYGFEFFERNTYEQLLINYANERLQqYFINQV-FKS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 835 EQVECVQEGVTMETAYSPGNQNGVLdfFFQKPS-GFLTLLDEESQmiwsMESNFPKKLQSLLESSNTNAVYSPLKDGNGN 913
Cdd:cd14886 397 EIQEYEIEGIDHSMITFTDNSNVLA--VFDKPNlSIFSFLEEQCL----IQTGSSEKFTSSCKSKIKNNSFIPGKGSQCN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 914 valkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgslvsaypsfkfrghksal 993
Cdd:cd14886 471 ---------FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN----------------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 994 lskkMTASSIIGENKNYLelskllkkkgtSTFLqrlergdpvtiASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDT 1073
Cdd:cd14886 513 ----KAFSDIPNEDGNMK-----------GKFL-----------GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1074 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL---ADTFLREKKEHLAAERCRLVLQQCKLQGWQMGVRK 1150
Cdd:cd14886 567 YETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTK 646
|
....
gi 1622884518 1151 VFLK 1154
Cdd:cd14886 647 VFLR 650
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
438-1154 |
1.08e-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: 263.52 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILS 517
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 518 GERGSGKSEASKQIIRHLTCRAASS----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 587
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGekkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 588 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREKL 663
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITT-------NPYDYAFVSQGEITVpsidDQEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 664 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 743
Cdd:cd14918 232 MATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 744 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 823
Cdd:cd14918 312 YVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 824 HHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNtn 901
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLydQHLGKSAN-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 902 avYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktseNVVINHLFQSKLSQTGSLVSAY 981
Cdd:cd14918 465 --FQKPKVVKGKAE-----AHFSLIHYAGTVDYNITGWLDKNKDPLN-----------DTVVGLYQKSAMKTLASLFSTY 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 982 PSFKfrGHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIH 1061
Cdd:cd14918 527 ASAE--ADSGAKKGAKKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPHFVR 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1062 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT------FLREKKehlAAERCRLV 1135
Cdd:cd14918 574 CIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASaipegqFIDSKK---ASEKLLAS 650
|
730
....*....|....*....
gi 1622884518 1136 LQQCKLQgWQMGVRKVFLK 1154
Cdd:cd14918 651 IDIDHTQ-YKFGHTKVFFK 668
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
437-1116 |
5.71e-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: 5.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRP--QC 513
Cdd:cd14880 2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQP--QKLKPHIFTVGEQTYRNVKSLIEPvnQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 514 FILSGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcER 585
Cdd:cd14880 80 IVVSGESGAGKTWTSRCLMKFYAVVAASPTSWeshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL-NR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 586 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqddvstgERSLNREKLAV 665
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP--------ERNLEEDCFEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 666 LKQALNVVGFSNLEVENLFVILAAILHLGDIRFTA---------LTEGNSAFVSDLQLLeqvagmLQVSTDELASALTT- 735
Cdd:cd14880 231 TREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADsedeaqpcqPMDDTKESVRTSALL------LKLPEDHLLETLQIr 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 736 DIQYFKGDMIIRRHTIQI-AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDeqrSMQTLDIGILDIFGFEEFQKNEFEQL 814
Cdd:cd14880 305 TIRAGKQQQVFKKPCSRAeCDTRRDCLAKLIYARLFDWLVSVINSSICADT---DSWTTFIGLLDVYGFESFPENSLEQL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 815 CVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsMESNFPKKLQS 893
Cdd:cd14880 382 CINYANEKLqQHFVAHYL-RAQQEEYAVEGLEWSFINYQDNQT-CLDLIEGSPISICSLINEECRL---NRPSSAAQLQT 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 894 LLESSNTNavySPLKdGNGNVALKdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsq 973
Cdd:cd14880 457 RIESALAG---NPCL-GHNKLSRE---PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN--- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 974 tgslvsaypsfkfrghksallSKKMTASSIIGENknylelskllkkkgtstflqrleRGDPVTIASQLRKSLTDIIGKLQ 1053
Cdd:cd14880 527 ---------------------PEEKTQEEPSGQS-----------------------RAPVLTVVSKFKASLEQLLQVLH 562
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884518 1054 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1116
Cdd:cd14880 563 STTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
437-1122 |
1.14e-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: 1.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASS-----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 585
Cdd:cd14923 79 TGESGAGKTVNTKRVIQYFATIAVTGdkkkeqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 586 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NRE 661
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIST-------NPFDFPFVSQGEVTVasidDSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 662 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 741
Cdd:cd14923 231 ELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 742 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNE 821
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 822 KMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSN 899
Cdd:cd14923 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 900 tnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvS 979
Cdd:cd14923 466 ----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-----------S 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 980 AYpsfkfrghksallskkmtASSIIGENknylelskllkkkGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQKCTPHF 1059
Cdd:cd14923 526 NY------------------AGAEAGDS-------------GGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHF 574
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884518 1060 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1122
Cdd:cd14923 575 VRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
437-1118 |
1.56e-70 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 249.04 E-value: 1.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsslpPHLFSCVERAFHQLFQEQRpQCFIL 516
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE------PHVYDVAEASVQDLLVHGN-QTIVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcerKQQLTGARIYT 596
Cdd:cd14898 75 SGESGSGKTENAKLVIKYLVERTASTTS-IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF---DGKITGAKFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 597 YLLEKSRLVSQPLGQSNFLIFSLLmdglsaeekhglhlnnlCAHRYLNQTmQDDVSTGERSLNREKLAVLKQ-------A 669
Cdd:cd14898 151 YLLEKSRVTHHEKGERNFHIFYQF-----------------CASKRLNIK-NDFIDTSSTAGNKESIVQLSEkykmtcsA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 670 LNVVGFSNL-EVENLfviLAAILHLGDIRFTalTEGNSAFVSDlQLLEQVAGMLQVSTDELASALTT-DIQYfKGDMIIR 747
Cdd:cd14898 213 MKSLGIANFkSIEDC---LLGILYLGSIQFV--NDGILKLQRN-ESFTEFCKLHNIQEEDFEESLVKfSIQV-KGETIEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 748 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEqrsmqtLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 827
Cdd:cd14898 286 FNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGE------RSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 828 NEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDffFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLessntnavyspl 907
Cdd:cd14898 360 IKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRD--FEKPCGLMDLISEESFNAWGNVKNLLVKIKKYL------------ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 908 kdgNGNVALKdHGTAFTIMHYAGRVMYDVVGAIEKNKDSlsqnllfvmktsenvvinhlfqsklsqtGSLvsaypsfkfR 987
Cdd:cd14898 426 ---NGFINTK-ARDKIKVSHYAGDVEYDLRDFLDKNREK----------------------------GQL---------L 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 988 GHKSALLSKKMTASSIIGENKNylelskllkkkgtstflqrlergdpvtiasqlrkSLTDIIGKLQKCTPHFIHCIRPNN 1067
Cdd:cd14898 465 IFKNLLINDEGSKEDLVKYFKD----------------------------------SMNKLLNSINETQAKYIKCIRPNE 510
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622884518 1068 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT 1118
Cdd:cd14898 511 ECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
449-1122 |
2.15e-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: 252.65 E-value: 2.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 449 NQIYTFIGDILLLVNPYKELPIYS-SMVSQLYFSSSgklcSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGKSEA 527
Cdd:cd14887 22 NCIYTYTGTLLIAVNPYRFFNLYDrQWISRFDTEAN----SRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTET 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 528 SKQIIRHLTC----RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKqQLTGARIYTYLLEKSR 603
Cdd:cd14887 98 SKHVLTYLAAvsdrRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG-KLTRASVATYLLANER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 604 LVSQPLGQSNFLIFSllmdglsaeekhglhlnNLCAHRYLNQTMqdDVSTGERSLNREKLAVLKQALNVVGFSNLEVENL 683
Cdd:cd14887 177 VVRIPSDEFSFHIFY-----------------ALCNAAVAAATQ--KSSAGEGDPESTDLRRITAAMKTVGIGGGEQADI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 684 FVILAAILHLGDIRFTALTE--------------GNSAFVSDL-QLLE--------QVAGMLQVSTDELASALTTDIQYF 740
Cdd:cd14887 238 FKLLAAILHLGNVEFTTDQEpetskkrkltsvsvGCEETAADRsHSSEvkclssglKVTEASRKHLKTVARLLGLPPGVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 741 KGDMI-----IRR-------HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL----------LSQDEQRSMQTLDIGIL 798
Cdd:cd14887 318 GEEMLrlalvSRSvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdSDEDTPSTTGTQTIGIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 799 DIFGFEEFQ---KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVL-DFFFQKPSGFLTLLD 874
Cdd:cd14887 398 DLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLaSTLTSSPSSTSPFSP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 875 EESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGNGNV----------------------ALKDHGTAFTIMHYAGRV 932
Cdd:cd14887 478 TPSFRSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSdlfyeklnkniinsakyknitpALSRENLEFTVSHFACDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 933 MYDVVGAIEKNKDSLSQNLlfvmktsenvvinhlfqsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKNyle 1012
Cdd:cd14887 558 TYDARDFCRANREATSDEL---------------------------------------ERLFLACSTYTRLVGSKKN--- 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1013 lskllkkKGTSTFLQRLErgdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMV 1092
Cdd:cd14887 596 -------SGVRAISSRRS-----TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663
|
730 740 750
....*....|....*....|....*....|
gi 1622884518 1093 KIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1122
Cdd:cd14887 664 RVMADGFPCRLPYVELWRRYETKLPMALRE 693
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
438-1115 |
3.62e-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: 246.32 E-value: 3.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgklcsslppHLFSCVERAFHQLFQ-EQRPQCFIL 516
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC-------------HISGVAENALDRIKSmSSNAESIVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARI-Y 595
Cdd:cd14874 70 GGESGSGKSYNAFQVFKYLT--SQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLkY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 596 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-----TMQDDVstgerslnrEKLAVLKQAL 670
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQgnsteNIQSDV---------NHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 671 NVVGFSNLEVENLFVILAAILHLGDIRFTAL----TEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQyfKGDMIi 746
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTKrnpnVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSE--DGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 747 rrhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdeQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 826
Cdd:cd14874 294 ---DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL-----KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 827 INEVLFLHEQVECVQEGVTMETAYSPGNQNG-VLDFFFQKPSGFLTLLDEESQmiwsmesnFPK-KLQSLLESSNTNAVY 904
Cdd:cd14874 366 FVKHSFHDQLVDYAKDGISVDYKVPNSIENGkTVELLFKKPYGLLPLLTDECK--------FPKgSHESYLEHCNLNHTD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 905 splKDGNGNVALKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVsaypsf 984
Cdd:cd14874 438 ---RSSYGKARNKER-LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMI------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 985 kfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIR 1064
Cdd:cd14874 508 --------------------------------------------------VSQAQFILRGAQEIADKINGSHAHFVRCIK 537
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622884518 1065 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 1115
Cdd:cd14874 538 SNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
437-1112 |
1.20e-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: 236.91 E-value: 1.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcssLPPHLFSCVERAFHQLFQEQRPQCFI 515
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRG-----LPPHLFALAAKAISDMQDFRRDQLIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 516 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIY 595
Cdd:cd14905 77 IGGESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEM-FYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 596 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVST--GERSLNReklavLKQALNVV 673
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDR-----LKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 674 GFSNLEVENLFVILAAILHLGDIRFtaLTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDiqyfkgdmiiRRHTIQI 753
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTF--FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 754 AEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdeQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 833
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL-----KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 834 HEQVECVQEGVTMETAYS-PGNQNGVldfffQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTnavysplkdgng 912
Cdd:cd14905 374 QEQREYQTERIPWMTPISfKDNEESV-----EMMEKIINLLDQESKNINSSDQIFLEKLQNFLSRHHL------------ 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 913 nvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtseNVVINHLFQS----KLSQTGSLVSAYPSFKFRG 988
Cdd:cd14905 437 ---FGKKPNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHK---NSITKYLFSRdgvfNINATVAELNQMFDAKNTA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 989 HKSALLSKK--MTASSIIGENKNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDiigklQKCTPHFIHCIRPN 1066
Cdd:cd14905 511 KKSPLSIVKvlLSCGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINN-----SNCDFHFIRCIKPN 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1622884518 1067 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1112
Cdd:cd14905 586 SKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRF 631
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
437-1113 |
1.62e-65 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 237.11 E-value: 1.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS----LPPHLFSCVERAFHQLFQEQRP 511
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAASaapfPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 512 QCFILSGERGSGKSEASKQIIRHLT-CRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQ-- 588
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHyIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTqk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 589 ------LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL--------NQTMQDDVSTG 654
Cdd:cd14884 162 nmfngcFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLlnpdeshqKRSVKGTLRLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 655 ERSLNREKLAVLK---------QALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAgMLQVS 725
Cdd:cd14884 242 SDSLDPSEEEKAKdeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKAAAECLQIEEEDLENVIKYK-NIRVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 726 TDelasalttdiqyfkgdmIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLD--------IG 796
Cdd:cd14884 321 HE-----------------VIRTErRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDiysineaiIS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 797 ILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVLFlHEQVECVQEGVTMETAYSPgNQNGVLDFffqkPSGFLTLLDE 875
Cdd:cd14884 384 ILDIYGFEELSGNDFDQLCINLANEKLNnYYINNEIE-KEKRIYARENIICCSDVAP-SYSDTLIF----IAKIFRRLDD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 876 ESQM-----------IWSMESNFPKKLQslLESSNTNAVYSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNK 944
Cdd:cd14884 458 ITKLknqgqkktddhFFRYLLNNERQQQ--LEGKVSYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 945 DSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrghksallskkmtasSIIGENKNYLelskllkkkgtst 1024
Cdd:cd14884 536 DKIETSIETLISCSSNRFLRE------------------------------------ANNGGNKGNF------------- 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1025 flqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 1104
Cdd:cd14884 567 ----------LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
....*....
gi 1622884518 1105 FSDFLSRYK 1113
Cdd:cd14884 637 KKETAAALK 645
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
437-1154 |
5.53e-63 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 229.50 E-value: 5.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 516
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMF---KGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 517 SGERGSGKSEASKQIIRHLTCRAASS---------RAMLDsrfkhvmcILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 587
Cdd:cd01386 79 LGRSGSGKTTNCRHILEYLVTAAGSVggvlsveklNAALT--------VLEAFGNVRTALNGNATRFSQLFSLDF-DQAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 588 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLC--AHRYLNQTM-QDDVSTGERSLNRekla 664
Cdd:cd01386 150 QLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAesNSFGIVPLQkPEDKQKAAAAFSK---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 665 vLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASAL----------- 733
Cdd:cd01386 226 -LQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqq 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 734 -TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeQRSMQTldIGILDIFGFE--EFQKNE 810
Cdd:cd01386 305 sTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSS--HHSTSS--ITIVDTPGFQnpAHSGSQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 811 ----FEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPS--------------GFLTL 872
Cdd:cd01386 381 rgatFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedrrGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 873 LDEESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGngnvalkDHGTAFTIMHYAGR--VMYDVVGaieknkdslsqn 950
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRS-------EGPLQFVLGHLLGTnpVEYDVSG------------ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 951 llFVMKTSENVvinhlfqSKLSQTGSLVSaypsfkfrghksallSKKMTAssiiGENKNYlelskllkkkgtstflqrle 1030
Cdd:cd01386 522 --WLKAAKENP-------SAQNATQLLQE---------------SQKETA----AVKRKS-------------------- 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1031 rgdpvtIASQLRKSLTDIIGKLQKCTPHFIHCIRPN------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG 1098
Cdd:cd01386 554 ------PCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkderstssPAAGDELLDVPLLRSQLRGSQLLDALRLYRQG 627
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884518 1099 YPVRLSFSDFLSRYKPLADTFLRE-------KKEHLAAERcrlVLQQCKLQ--GWQMGVRKVFLK 1154
Cdd:cd01386 628 FPDHMPLGEFRRRFQVLAPPLTKKlglnsevADERKAVEE---LLEELDLEksSYRIGLSQVFFR 689
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
438-1113 |
1.56e-59 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 220.23 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKL-------CSSLPPHLFSCVERAFHQLFQEQR 510
Cdd:cd14893 3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 511 PQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDS------------RFKHVMCILEAFGHAKTTLNDLSSCFIKYF 578
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSegasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 579 ELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEE--KHGLHLNNLCAHRYLNQTMQDDVstGER 656
Cdd:cd14893 163 SVEF-SKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNKCVNEFVMLKQADPLA--TNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 657 SLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG-------NSAFVSDLQ--------LLEQVAGM 721
Cdd:cd14893 240 ALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGgksvggaNSTTVSDAQscalkdpaQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 722 LQVSTDELASALTTDiQYFKGD-----MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL---LSQDEQRSM--Q 791
Cdd:cd14893 320 LEVEPVVLDNYFRTR-QFFSKDgnktvSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggiFDRYEKSNIviN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 792 TLDIGILDIFGFEEF--QKNEFEQLCVNMTNEKMHH-YINEVL-----FLHEQVECVQEGVTMETAYS-PGNQNGVLDFF 862
Cdd:cd14893 399 SQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHfYVQNTLainfsFLEDESQQVENRLTVNSNVDiTSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 863 FQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLE-----------SSNTNAVYSPLKDGNgnvalkdhgTAFTIMHYAGR 931
Cdd:cd14893 479 EDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEavgglsrpnmgADTTNEYLAPSKDWR---------LLFIVQHHCGK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 932 VMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAyPSFKFRGHKSALLSKKMTASSiigENKNyl 1011
Cdd:cd14893 550 VTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAA-KQTEERGSTSSKFRKSASSAR---ESKN-- 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1012 elskllkkKGTSTFLQRLERGDPVTIAsqlrksltdiigkLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEM 1091
Cdd:cd14893 624 --------ITDSAATDVYNQADALLHA-------------LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVEL 682
|
730 740
....*....|....*....|..
gi 1622884518 1092 VKIFRYGYPVRLSFSDFLSRYK 1113
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 ... |
445-1154 |
9.89e-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: 9.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 445 RFGNNQIYTFIGDILLLVNPYKELPIYSSmvsqlyfSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGK 524
Cdd:cd14937 10 RYKKNYIYTIAEPMLISINPYQVIDVDIN-------EYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGSGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 525 SEASKQIIRHLTCRAAS----SRAMLDSRFkhvmcILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGARIYTYLLE 600
Cdd:cd14937 83 TEASKLVIKYYLSGVKEdneiSNTLWDSNF-----ILEAFGNAKTLKNNNSSRYGKYIKIELDEY-QNIVSSSIEIFLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 601 KSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL-NQTMQ----DDVSTGER---SLNREKLAVLKqalnv 672
Cdd:cd14937 157 NIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIvNKNVVipeiDDAKDFGNlmiSFDKMNMHDMK----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 673 vgfsnlevENLFVILAAILHLGDIRFTALTEGNSAFVSDL-----QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 747
Cdd:cd14937 232 --------DDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELdknnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 748 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 827
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNY----IGILDIFGFEIFSKNSLEQLLINIANEEIHSIY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 828 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfffqkpsgfltLLDEESQMIWSMESNF--PKKLQSLLESSNTNAvYS 905
Cdd:cd14937 380 LYIVYEKETELYKAEDILIESVKYTTNES-IID-----------LLRGKTSIISILEDSClgPVKNDESIVSVYTNK-FS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 906 plKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkLSQTGSLvsaypsfk 985
Cdd:cd14937 447 --KHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-VEVSESL-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 986 frGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLTDIIGKLQKCTPHFIHCIRP 1065
Cdd:cd14937 516 --GRKNLITFKYL--------------------------------------------KNLNNIISYLKSTNIYFIKCIKP 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1066 NNSKLPDTFDNFYVSAQLQYIGVLEMVKI---FRYGYpvrlSFSDFLSRYKPL-----ADTFLREKkehlaaERCRLVLQ 1137
Cdd:cd14937 550 NENKEKNNFNQKKVFPQLFSLSIIETLNIsffFQYKY----TFDVFLSYFEYLdystsKDSSLTDK------EKVSMILQ 619
|
730
....*....|....*...
gi 1622884518 1138 Q-CKLQGWQMGVRKVFLK 1154
Cdd:cd14937 620 NtVDPDLYKVGKTMVFLK 637
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
67-336 |
3.98e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 165.51 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 67 LKRLKHAKNPKVHFDLADMIQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDE 146
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 147 DFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmltd 226
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA-------------NGNLEI----------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 227 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLV 306
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
250 260 270
....*....|....*....|....*....|
gi 1622884518 307 NCNEEKPSDIAASEFIEEMLLKAEIAWEEK 336
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
66-355 |
3.41e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 157.04 E-value: 3.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 66 FLKRLKHAKNPKVHFDLADMIQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQD 145
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 146 EDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmlt 225
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY-------------NGNLEI---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 226 dVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHL 305
Cdd:COG0666 136 -VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622884518 306 VNCNEEKPSDIAASEF---IEEMLLKAEIAWEEKMKEPLSVSTLAQEEPYEEI 355
Cdd:COG0666 215 KDNDGKTALDLAAENGnleIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
437-1153 |
2.21e-39 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 158.46 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 437 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgkLCSSLPPHL----FSCVERAFHQLFQEQRPQ 512
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY------KCIDCIEDLslneYHVVHNALKNLNELKRNQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 513 CFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSR-----------------------FKHVMCILEAFGHAKTTLND 569
Cdd:cd14938 76 SIIISGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLndqeednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 570 LSSCFIKYFELQFceRKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNqtmqD 649
Cdd:cd14938 156 NSSRFSKFCTIHI--ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLN----N 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 650 DVSTGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF---------------VSDLQL 714
Cdd:cd14938 230 EKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLmgknqcgqninyetiLSELEN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 715 LEQVAGMLQVSTDELASAL-----TTDIQYFKGDMI------IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNsCLLS 783
Cdd:cd14938 310 SEDIGLDENVKNLLLACKLlsfdiETFVKYFTTNYIfndsilIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 784 QDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFF 863
Cdd:cd14938 389 QLQNININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 864 QKPSGFL-TLLDEESQMIWSMESNFpkkLQSLLESSNTNAVYSPLKDGNGNvalkdhGTAFTIMHYAGRVMYDVVGAIEK 942
Cdd:cd14938 469 GPTEGSLfSLLENVSTKTIFDKSNL---HSSIIRKFSRNSKYIKKDDITGN------KKTFVITHSCGDIIYNAENFVEK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 943 NKDSLSQNLLFVMKTSENVVINHLFQsklsqtgslvsaypSFKFRghksallskkmTASSIIGENKNYLELSKLlkkkgt 1022
Cdd:cd14938 540 NIDILTNRFIDMVKQSENEYMRQFCM--------------FYNYD-----------NSGNIVEEKRRYSIQSAL------ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1023 STFLQRLERGDPVTIaSQLRKSLTDIIGKLQKCTPHFIHCIRPNNSK-LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 1101
Cdd:cd14938 589 KLFKRRYDTKNQMAV-SLLRNNLTELEKLQETTFCHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPH 667
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 1102 RLSFSDFLSRYKpladtflreKKEHLAAERCRLVLQQCKL--QGWQMGVRKVFL 1153
Cdd:cd14938 668 KFTLNEFLSIFD---------IKNEDLKEKVEALIKSYQIsnYEWMIGNNMIFL 712
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
438-1122 |
1.46e-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: 109.06 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 438 LLYEIQKRFGNNQIYTFIGD-ILLLVNPYKEL------PIYSSMVSqLYFSSSGKLCSSLPPHLFSCVERAFHQLF---- 506
Cdd:cd14894 3 LVDALTSRFDDDRIYTYINHhTMAVMNPYRLLqtarftSIYDEQVV-LTYADTANAETVLAPHPFAIAKQSLVRLFfdne 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 507 ---------------QEQRPQCFILSGERGSGKSEASKQIIRHL--------------TCRAASSR-------------- 543
Cdd:cd14894 82 htmplpstissnrsmTEGRGQSLFLCGESGSGKTELAKDLLKYLvlvaqpalskgseeTCKVSGSTrqpkiklftsstks 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 544 ------------AMLDSR---------------------------------------------------------FKHVM 554
Cdd:cd14894 162 tiqmrteeartiALLEAKgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledeeqlrmyFKNPH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 555 C------------ILEAFGHAKTTLNDLSSCFIKYFELQFC----ERKQQLTGARIYTYLLEKSRLVSQPLGQS------ 612
Cdd:cd14894 242 AakklsivldsniVLEAFGHATTSMNLNSSRFGKMTTLQVAfglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnel 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 613 NFLIFSLLMDGLSAEE-----KHGLHLNNL-CA---------HRYLNQTMQDDvsTGERSLNREKLAVlkQALNVVGFSN 677
Cdd:cd14894 322 NFHILYAMVAGVNAFPfmrllAKELHLDGIdCSaltylgrsdHKLAGFVSKED--TWKKDVERWQQVI--DGLDELNVSP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 678 LEVENLFVILAAILHLGDIRFTALTEGNSAFVSD---LQLLEQVAGMLQV-STDELASALTTDIQYFKGDMIIRRHTIQI 753
Cdd:cd14894 398 DEQKTIFKVLSAVLWLGNIELDYREVSGKLVMSStgaLNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 754 AEF--FRDLLAKSLYSRLFSFLVNTMNSCL----LSQDEQRSMQTLD---------IGILDIFGFEEFQKNEFEQLCVNM 818
Cdd:cd14894 478 GQVnhVRDTLARLLYQLAFNYVVFVMNEATkmsaLSTDGNKHQMDSNasapeavslLKIVDVFGFEDLTHNSLDQLCINY 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 819 TNEKMhhYINEvlflhEQVecvqegvtMETAYSP-------GNQNGVLdFFFQKPSGF------LTLLDEESQMIWSMES 885
Cdd:cd14894 558 LSEKL--YARE-----EQV--------IAVAYSSrphltarDSEKDVL-FIYEHPLGVfasleeLTILHQSENMNAQQEE 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 886 NFPKKLQSLLESSNTNAVYSP---LKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvv 962
Cdd:cd14894 622 KRNKLFVRNIYDRNSSRLPEPprvLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNS-- 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 963 iNHLfqSKLSQTGSLVSAYPSfkfrghksallskkmTASSIIGENKNylelskllKKKGTSTFLqrlergdpvtiaSQLR 1042
Cdd:cd14894 700 -SHF--CRMLNESSQLGWSPN---------------TNRSMLGSAES--------RLSGTKSFV------------GQFR 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1043 KSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG----YPVRLSFSDFLSRYKPLadt 1118
Cdd:cd14894 742 SHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSsssySAIDISKSTLLTRYGSL--- 818
|
....
gi 1622884518 1119 fLRE 1122
Cdd:cd14894 819 -LRE 821
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
94-326 |
1.33e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.82 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 94 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACAC-----DNPDIVLLLV 168
Cdd:PHA03100 14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 169 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLR-------QMKLQRPMSMLTDVKHFLSSGGNVNEKN 241
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNsdgenllHLYLESNKIDLKILKLLIDKGVDINAKN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 242 degvtllhmacasgykeVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAASEF 321
Cdd:PHA03100 174 -----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
|
....*
gi 1622884518 322 IEEML 326
Cdd:PHA03100 237 NKEIF 241
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
89-302 |
1.45e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.82 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 89 AIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARY-----DNAFIAEILIDRGVNVNHQDEDFWTPMHIA-CACDN-P 161
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKSNsY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 162 DIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLrqmklqrpmsmlTDVKHFLSSGGNVNEKN 241
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAK------------NRVNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884518 242 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQAN 302
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
462-580 |
5.34e-20 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 88.94 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 462 VNPYKELPIYSSmvSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAAS 541
Cdd:cd01363 5 VNPFKELPIYRD--SKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFN 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 542 SRAMLDSRFK---------------HVMCILEAFGHAKTTLNDLSSCFIKYFEL 580
Cdd:cd01363 83 GINKGETEGWvylteitvtledqilQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
98-301 |
2.22e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 91.66 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 98 VLRLLKEGADPHTLVSSGGSLLHLCAR--YDNAFIaEILIDRGVNVNHQDEDFWTPMHIACACD-NPDIVLLLVLAGANV 174
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKngYDTENI-RTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 175 LLQDVNGNIPLDYAveGTESSSILLTYLDENGVDLTSLRQmKLQRPMSM-------LTDVKHFLSSGGNVNEKNDEGVTL 247
Cdd:PHA02876 369 NARDYCDKTPIHYA--AVRNNVVIINTLLDYGADIEALSQ-KIGTALHFalcgtnpYMSVKTLIDRGANVNSKNKDLSTP 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884518 248 LHMACASGYK-EVVSLILEHGGDLNIVDDQYWTPLHLAAKYgqANLVKLLLMHQA 301
Cdd:PHA02876 446 LHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGA 498
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
227-307 |
8.36e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 227 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHgGDLNIVDDQyWTPLHLAAKYGQANLVKLLLMHQANPHLV 306
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90
|
.
gi 1622884518 307 N 307
Cdd:pfam12796 91 D 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
126-313 |
1.00e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.85 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 126 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVllQDVNGNIPLDYAVEGTESSSILLTYLDEN 205
Cdd:PHA02874 13 DIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADI--NHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 206 GVDLTSLRQMKLQRPMsmltdVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAA 285
Cdd:PHA02874 91 GVDTSILPIPCIEKDM-----IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
|
170 180
....*....|....*....|....*...
gi 1622884518 286 KYGQANLVKLLLMHQANPHLVNCNEEKP 313
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
89-178 |
1.52e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.92 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 89 AIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRgVNVNHQDEDfWTPMHIACACDNPDIVLLLV 168
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLL 81
|
90
....*....|
gi 1622884518 169 LAGANVLLQD 178
Cdd:pfam12796 82 EKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
107-307 |
3.93e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.99 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 107 DPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMH--IACACDN-PDIVLLLVLAGANVLLQDVNG 181
Cdd:PHA03095 4 DESVDIIMEAALYDYLLNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 182 NIPLDYavegtesssilltYLdENGvdlTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKNDEGVTLLHmACASGY---KE 258
Cdd:PHA03095 84 FTPLHL-------------YL-YNA---TTLDVIKL------------LIKAGADVNAKDKVGRTPLH-VYLSGFninPK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622884518 259 VVSLILEHGGDLNIVDDQYWTPLHLAAKYGQAN--LVKLLLMHQANPHLVN 307
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVD 184
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
97-306 |
5.20e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.60 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 97 EVLRLL-KEGADPHTLVSSGGSLLHLCARYDN--AFIAEILIDRGVNVNHQDEDFWTPMHI-----ACacdNPDIVLLLV 168
Cdd:PHA03095 98 DVIKLLiKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVllksrNA---NVELLRLLI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 169 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKN 241
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgssckrsLVLPLLIAGISINARN 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884518 242 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLV 306
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
124-309 |
2.62e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.23 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 124 RYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLqdvngnIPLDyAVEGTESSSILLTYLD 203
Cdd:PHA02874 44 RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIP-CIEKDMIKTILDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 204 ENGVDLTSLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHL 283
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180
....*....|....*....|....*.
gi 1622884518 284 AAKYGQANLVKLLLMHQANPhLVNCN 309
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHI-MNKCK 221
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
96-313 |
5.87e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 96 KEVLRLLKEGADP-----------HTLVSSGGSL-------------------------LHLCARYDN-AFIAEILIDRG 138
Cdd:PHA03095 28 EEVRRLLAAGADVnfrgeygktplHLYLHYSSEKvkdivrllleagadvnapercgftpLHLYLYNATtLDVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 139 VNVNHQDEDFWTPMHIACA--CDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDL------- 209
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyavddrf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 210 -TSLRQMKL-----QRPMSMLTDvkhflsSGGNVNEKNDEGVTLLH-MACASGYKE-VVSLILEHGGDLNIVDDQYWTPL 281
Cdd:PHA03095 188 rSLLHHHLQsfkprARIVRELIR------AGCDPAATDMLGNTPLHsMATGSSCKRsLVLPLLIAGISINARNRYGQTPL 261
|
250 260 270
....*....|....*....|....*....|..
gi 1622884518 282 HLAAKYGQANLVKLLLMHQANPHLVNCNEEKP 313
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
95-325 |
7.40e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 95 DKEVLRLLKE-GADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGA 172
Cdd:PHA02878 146 EAEITKLLLSyGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 173 NVLLQDVNGNIPLDYAVEGTESSSILltyldengvdltslrqmklqrpmsmltdvKHFLSSGGNVNEKND-EGVTLLHMA 251
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDIL-----------------------------KLLLEHGVDVNAKSYiLGLTALHSS 276
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884518 252 CASgyKEVVSLILEHGGDLNIVDDQYWTPLHLAAK-YGQANLVKLLLMHqanphlVNCNEEKPSDIAASE-FIEEM 325
Cdd:PHA02878 277 IKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILISN------ICLLKRIKPDIKNSEgFIDNM 344
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
248-299 |
2.46e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 2.46e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1622884518 248 LHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMH 299
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
119-274 |
2.69e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 119 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLvlaganvllqdvngnipLDYAvegtesssil 198
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-----------------LEHA---------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884518 199 ltyldengvdltslrqmklqrpmsmltdvkhflssggNVNEKnDEGVTLLHMACASGYKEVVSLILEHGGDLNIVD 274
Cdd:pfam12796 54 -------------------------------------DVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
94-332 |
9.14e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.61 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 94 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGAN 173
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 174 VLLQDVNGNIPLDYAVEgtesssilltYLDengvdltslrqmklqrpmsmLTDVKHFLSSGGNVNEKNDEGVTLLHMACA 253
Cdd:PHA02874 183 ANVKDNNGESPLHNAAE----------YGD--------------------YACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 254 sgYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG-QANLVKLLLMHQANPHLVNCNEEKPSDIAASEFIEEMLLKAEIA 332
Cdd:PHA02874 233 --HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIA 310
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
244-297 |
1.80e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 1.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 244 GVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLL 297
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
94-302 |
3.74e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.17 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 94 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDedfwtpMHIACACDNPDI--VLLLVLAG 171
Cdd:PHA02876 190 NAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND------LSLLKAIRNEDLetSLLLYDAG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 172 ANVLLQDVNGNIPLDYAVEgTESSSILLTYLDENGVDLTSlRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKNDEG 244
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASQ-APSLSRLVPKLLERGADVNA-KNIKGETPLYLMAkngydteNIRTLIMLGADVNAADRLY 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884518 245 VTLLHMACA-SGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQAN 302
Cdd:PHA02876 342 ITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
126-318 |
1.78e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.86 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 126 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSI-------- 197
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaiidnrs 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 198 ---------------------LLTYldENGVDLTSLRQMK-------LQRPmSMLTDVKHFLSSGGNVNEKNDEGVTLLH 249
Cdd:PHA02876 236 ninkndlsllkairnedletsLLLY--DAGFSVNSIDDCKntplhhaSQAP-SLSRLVPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884518 250 MACASGY-KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQ-ANLVKLLLMHQANPHLVNCNEEKPSDIAA 318
Cdd:PHA02876 313 LMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAA 383
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1391-1668 |
1.04e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1391 RPGDARPPGAPGTAARVLTPGTPQCALPPatPPG--------DEDDGEPVYIEML--------------GHPARPDSPD- 1447
Cdd:PHA03247 2482 RPAEARFPFAAGAAPDPGGGGPPDPDAPP--APSrlapailpDEPVGEPVHPRMLtwirgleelasddaGDPPPPLPPAa 2559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1448 ----PGESVYEEMkcCLPDDGGPGAGSflRASPPllhGAPEDEAAGP-PGDMCDIP--PPFPNLLP---HRPPllvfPPT 1517
Cdd:PHA03247 2560 ppaaPDRSVPPPR--PAPRPSEPAVTS--RARRP---DAPPQSARPRaPVDDRGDPrgPAPPSPLPpdtHAPD----PPP 2628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1518 PvtcSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSP-------LSPQYSKSQKGDGDRPASPGLALFNGSGRASPPS 1590
Cdd:PHA03247 2629 P---SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP 2705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1591 tppppppgPPPAPFRPCAHLAFPPEPAPVSLGKAGPSTEAPKVHPKPNSA---PGAGSCSSFPKIPYSPVKAARVDARKA 1667
Cdd:PHA03247 2706 --------PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpatPGGPARPARPPTTAGPPAPAPPAAPAA 2777
|
.
gi 1622884518 1668 G 1668
Cdd:PHA03247 2778 G 2778
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
119-317 |
2.31e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.82 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 119 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIAC-----------------------------ACDNPD------- 162
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdAFNNRNveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 163 ----------------------------IVLLLVLAGANVLLQDVN-GNIPLDYAVEG--TESSSILLTYLDE-NGVDLT 210
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYATENkdQRLTELLLSYGANvNIPDKT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 211 SLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMacASGY---KEVVSLILEHGGDLNIVDD-QYWTPLHLAAK 286
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI--SVGYckdYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
|
250 260 270
....*....|....*....|....*....|.
gi 1622884518 287 YGQAnlVKLLLMHQANPHLVNCNEEKPSDIA 317
Cdd:PHA02878 279 SERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
36-283 |
6.16e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.04 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 36 GQRQRLVKRMRCEQI----KAYYEREKAFQKQEGFLKRL--------KHAKNPKVHfDLADMIQDAIIHH---NDKEVLR 100
Cdd:PLN03192 433 GEKERVVGTLGCGDIfgevGALCCRPQSFTFRTKTLSQLlrlktstlIEAMQTRQE-DNVVILKNFLQHHkelHDLNVGD 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 101 LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILiDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVN 180
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 181 GNIPLDYAVEGTESSSILLTYL------DENGVDLTSLRQMKlqrpmSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACAS 254
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRILYHfasisdPHAAGDLLCTAAKR-----NDLTAMKELLKQGLNVDSEDHQGATALQVAMAE 665
|
250 260 270
....*....|....*....|....*....|
gi 1622884518 255 GYKEVVSLILEHGGDLNIVD-DQYWTPLHL 283
Cdd:PLN03192 666 DHVDMVRLLIMNGADVDKANtDDDFSPTEL 695
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
134-188 |
1.39e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 52.73 E-value: 1.39e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884518 134 LIDRG-VNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYA 188
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
227-304 |
1.76e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 1.76e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884518 227 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPH 304
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
88-309 |
2.46e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.46 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 88 DAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIacACDNPDIVLLL 167
Cdd:PHA02875 8 DAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHD--AVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 168 VLAGANVLLQDV---NGNIPLDYAVEgtesssilltyldengvdLTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKNDEG 244
Cdd:PHA02875 86 ELLDLGKFADDVfykDGMTPLHLATI------------------LKKLDIMKL------------LIARGADPDIPNTDK 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884518 245 VTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCN 309
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1354-1645 |
3.33e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1354 PRPHSDDYStmkkIPPRKPKRSPNTKLSGSYEEISGSRPGDARP--PGAPGTAARVLTPGTPqcaLPPATPPGDEDDGEP 1431
Cdd:PHA03247 2559 APPAAPDRS----VPPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSP 2631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1432 vyiemlghPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLR-----ASPPLLHGAPED-------EAAGPPGDMCDIPP 1499
Cdd:PHA03247 2632 --------SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRrarrlGRAAQASSPPQRprrraarPTVGSLTSLADPPP 2703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1500 PFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDRPASPGLAL 1579
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL 2783
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884518 1580 FNGSGRA---------SPPSTPPPPPPGPPPAPFRPCAHLAFPPEPAPVSLGKAGPSTEAPkvhPKPNSAPGAGS 1645
Cdd:PHA03247 2784 TRPAVASlsesreslpSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG---PPPPSLPLGGS 2855
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
87-273 |
7.59e-08 |
|
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal family of eukaryotic proteins that are substrates of tyrosine kinase in the brain. When first identified, the family members were referred to as unconventional myosin XVI, or Myr 8. However, proteins have now been identified as being integrally involved in neuronal function and morphogenesis. The family is involved in both the activation of phosphoinositide 3-kinase (PI3K) and the recruitment of the downstream effector WAVE complex to the close vicinity of PI3K; it also appears to regulate the brain size and neurite outgrowth in mice.
Pssm-ID: 464717 [Multi-domain] Cd Length: 379 Bit Score: 56.71 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 87 QDAIIHHNDKEvLRLLKEGADPHTLVSSGGSLLHL-----CARYDN---AFIAEILI--DRGVNVNHQDED--FWTPMHI 154
Cdd:pfam15439 7 LEKRRRQEEGI-KRSGEEVAGKVRDISSEGRHFRMgfmtmPASQDRlphPCAAGMSIrsQSLHSVGSGDEDgsLPSSRKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 155 ACACDNPDIVLLLVLAGANVLLQDVNGNIpldyaVEGTESSSILLTYLDENgVDLTSLRQMKLQR-PMSMLT-------- 225
Cdd:pfam15439 86 PPPKPKRDPSTKLSMSSEAVSAGLSAGAK-----ETPSETEALSKPRPHSD-EYSRKIPPPKPKRsPNTQLSgsfdeipa 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884518 226 ------DVKHFLSSGG---NVNEKNDE---------GVTLLHMACA----------SGYKEVVSLILEHGGDLNIV 273
Cdd:pfam15439 160 pyirphGLLQRASSSDgpsPAPLPDEEeepvyiemvGNVLRDFSPTtpdddpdqseAVYEEMKYPLPEDSGAANGP 235
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
114-282 |
1.64e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 56.46 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 114 SGGSLLH--LCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDN--PDIVLLLVLAGANVLLQDVNGNIP-LDYA 188
Cdd:PHA02716 176 TGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPiMTYI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 189 VE----GTESSSILLTYLDENGVD-----LTSLRQMKLQRPMSMltdVKHFLSSGGNVNEKNDEGVTLLHMACASGY--K 257
Cdd:PHA02716 256 INidniNPEITNIYIESLDGNKVKnipmiLHSYITLARNIDISV---VYSFLQPGVKLHYKDSAGRTCLHQYILRHNisT 332
|
170 180
....*....|....*....|....*
gi 1622884518 258 EVVSLILEHGGDLNIVDDQYWTPLH 282
Cdd:PHA02716 333 DIIKLLHEYGNDLNEPDNIGNTVLH 357
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
115-168 |
2.71e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 2.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 115 GGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLV 168
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
236-284 |
3.40e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 3.40e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622884518 236 NVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLA 284
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
152-319 |
3.83e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 152 MHIACACD-----NPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILL-----TYLDENGVDLTSLRQMKLQRpm 221
Cdd:PHA02875 1 MDQVALCDailfgELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLlmkhgAIPDVKYPDIESELHDAVEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 222 SMLTDVKHFLSSGGNVNEK-NDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQ 300
Cdd:PHA02875 79 GDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
170
....*....|....*....
gi 1622884518 301 ANPHLVNCNEEKPSDIAAS 319
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMA 177
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1346-1681 |
5.55e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.79 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1346 AANEALARPRPHSDDYSTMKKIPPRKPKRSPNTklsgsyeeiSGSRPGDARPPGAPGTAARvlTPGTPQCALPPATPPGD 1425
Cdd:PHA03307 133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVASD---------AASSRQAALPLSSPEETAR--APSSPPAEPPPSTPPAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1426 EDDGEPVYIEMLGHPARPDSPDPGESvyeemkcclpDDGGPGAGSFLRASPPllhgaPEDEAAGPPgDMCDIPPPFPNLL 1505
Cdd:PHA03307 202 ASPRPPRRSSPISASASSPAPAPGRS----------AADDAGASSSDSSSSE-----SSGCGWGPE-NECPLPRPAPITL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1506 PHRPPLLVFP-PTPVTCSPASDESPLTPLEVKKLPvletnlkypvQSEGSSPLSPQYSKSQKGDGDRPASPGLALFNGSG 1584
Cdd:PHA03307 266 PTRIWEASGWnGPSSRPGPASSSSSPRERSPSPSP----------SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSES 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1585 RASppstppppppgpppapfrpcahLAFPPEPAPVSLGKAGPSTEAPKVHPK---PNSAPGAGSCSSFPKIPYSPVKAAR 1661
Cdd:PHA03307 336 SRG----------------------AAVSPGPSPSRSPSPSRPPPPADPSSPrkrPRPSRAPSSPAASAGRPTRRRARAA 393
|
330 340
....*....|....*....|
gi 1622884518 1662 VDARKAGSSASPPAPYSPPS 1681
Cdd:PHA03307 394 VAGRARRRDATGRFPAGRPR 413
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
1318-1659 |
5.78e-07 |
|
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.
Pssm-ID: 434857 [Multi-domain] Cd Length: 668 Bit Score: 54.77 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1318 PPKPKRDPNTRLSASYE-AVSACLSAAREAANEALARPRPHSDDYS-----TMKKIPPRKPKRSpntklSGSYEEISGSR 1391
Cdd:pfam15685 198 SATSPTDSQAKHIAEGKtAGGACGGAPPQAGEGEMARFAASESGLSllckvTFKSAAPLCPAAA-----SGPLAAKASLG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1392 PGDARPPGAPGTA---ARVLTPG--TPQCALPPATPP-------GDEDDGEPVYiemlGHPARPDS-----PDPGESVYE 1454
Cdd:pfam15685 273 GGGGGGLFAASGAiscAEVLKQGplAPGAARPLGEVPraaleteGGEGDGEGCS----GGPAAPASharalPPPAYTTFP 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1455 EMKCCL----PDDG--------GPGAGSflrasppllhGAPEDEAAGPPGDMCDIPPP----FPNLLPHRP-PLLVFPPT 1517
Cdd:pfam15685 349 GSKPKFdwvsPPDGperhfrfnGAGGGI----------GAPRRRAAALSGPWGSPPPPpgkaHPIPGPRRPaPALLAPPM 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1518 PVTCSPASDESPLT-PLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQKGD--GDRPASPGlalfNGSGRASPpstppp 1594
Cdd:pfam15685 419 FIFPAPTNGEPVRPgPPAPQALLPRPPPPTPPATPPPVPPPIPQLPALQPMPlaAARPPTPR----PCPGHGES------ 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884518 1595 pppgpppapfrpcahlAFPPEP-APVSLGKAGPSTEAPKVH--PKPNSAPGAGSCSSFPKIPySPVKA 1659
Cdd:pfam15685 489 ----------------ALAPAPtAPLPPALAADQAPAPALAaaPAPSPAPAPATADPLPPAP-APIKA 539
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1329-1668 |
6.51e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.79 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1329 LSASYEAVSACLSAAREAANealaRPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAArvl 1408
Cdd:PHA03307 44 VSDSAELAAVTVVAGAAACD----RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1409 TPGTPQCALPPATPPgdeddgePVYIEML------GHPARPDSPDPGESvyeemKCCLPDDGGPGAGSFLRASPPllhga 1482
Cdd:PHA03307 117 PPPTPPPASPPPSPA-------PDLSEMLrpvgspGPPPAASPPAAGAS-----PAAVASDAASSRQAALPLSSP----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1483 PEDEAAGPPGDMCDIPPPFPNLLPHRPPllvfPPTPVTCSPASDESPLTP--LEVKKLPVLETNLKYPVQSEGSSPL--- 1557
Cdd:PHA03307 180 EETARAPSSPPAEPPPSTPPAAASPRPP----RRSSPISASASSPAPAPGrsAADDAGASSSDSSSSESSGCGWGPEnec 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1558 -----SPQYSKSQKGDGDRPASPGLALFNGSGRASPPSTPPPPPPGPPPAPFRPCAH-------------LAFPPEPAPV 1619
Cdd:PHA03307 256 plprpAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPrasssssssressSSSTSSSSES 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622884518 1620 SLGKAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPySPVKAARVDARKAG 1668
Cdd:PHA03307 336 SRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP-RPSRAPSSPAASAG 383
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1330-1545 |
8.26e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 54.11 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1330 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDA-RPPGAPGTAARVl 1408
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASArGPGGAPAPAPAP- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1409 tPGTPQCALPPAT----PPGDEDDGEPVYIEMLGHPAR-PDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLHGAP 1483
Cdd:PRK12323 455 -AAAPAAAARPAAagprPVAAAAAAAPARAAPAAAPAPaDDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATAD 533
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622884518 1484 EDEAAGPPGDMcdiPPPFPNLLPHRPPLLVFPPTPvtcsPASDESPLTPLEVKKLPVLETNL 1545
Cdd:PRK12323 534 PDDAFETLAPA---PAAAPAPRAAAATEPVVAPRP----PRASASGLPDMFDGDWPALAARL 588
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
159-312 |
1.09e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 159 DNP--DIVLLLVLAGANVLLQDVNGNIPLdyavegtesSSILLTYLDENgvdltslrqmklqrpmSMLTDVKHFLSSGGN 236
Cdd:PHA02798 47 DSPstDIVKLFINLGANVNGLDNEYSTPL---------CTILSNIKDYK----------------HMLDIVKILIENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 237 VNEKNDEGVTLLHMACASGY---KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG---QANLVKLLLMHQANPHLVNcNE 310
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHN-NK 180
|
..
gi 1622884518 311 EK 312
Cdd:PHA02798 181 EK 182
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
263-317 |
2.91e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 2.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884518 263 ILEHGG-DLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIA 317
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1328-1659 |
3.93e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1328 RLSASYEAVSACLSAAREAANEALARPRPHSddysTMKKIP-PRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAAR 1406
Cdd:PHA03247 2684 RRRAARPTVGSLTSLADPPPPPPTPEPAPHA----LVSATPlPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1407 VLTPGTPQCALPPATPPGDEDDGEPVYIEMLGHPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLHGAPede 1486
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQP--- 2836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1487 AAGPPGdmcdiPPPFPNLLPhrPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQK 1566
Cdd:PHA03247 2837 TAPPPP-----PGPPPPSLP--LGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1567 gdgdRPASPGLALFNGSGRASPPSTPPPPPPGPPPAPFRPCAHLAFPPEPAPVS----LGKAGPS-TEAPKVHPKPNSAP 1641
Cdd:PHA03247 2910 ----QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVpqpwLGALVPGrVAVPRFRVPQPAPS 2985
|
330
....*....|....*...
gi 1622884518 1642 GAGSCSSFPKIPYSPVKA 1659
Cdd:PHA03247 2986 REAPASSTPPLTGHSLSR 3003
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
59-190 |
5.29e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 59 AFQKQEGFLKRLKHAKNPK-VHFDLADMIQDAIIHHNDK-EVLRLLKEGAD--PHTLVSSGG-----------SLLHLCA 123
Cdd:PTZ00322 12 AFAAQLFFGTEGSRKRRAKpISFERMAAIQEEIARIDTHlEALEATENKDAtpDHNLTTEEVidpvvahmltvELCQLAA 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884518 124 RYDnAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVE 190
Cdd:PTZ00322 92 SGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1354-1664 |
1.66e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 50.07 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1354 PRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYE----EISGSRPGDARPPGAPGTAARvltpgTPQCALPPATPPGdeddg 1429
Cdd:PHA03378 659 ITPYKPTWTQIGHIPYQPSPTGANTMLPIQWApgtmQPPPRAPTPMRPPAAPPGRAQ-----RPAAATGRARPPA----- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1430 epvyiemlGHPARPDSPDPGesvyeemkcclPDDGGPGAGSFLRASPPLLHGAPEDEAAGPPGDMCDIPPP--------F 1501
Cdd:PHA03378 729 --------AAPGRARPPAAA-----------PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPqappapqqR 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1502 PNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEvkklPVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDRPaSPglalfn 1581
Cdd:PHA03378 790 PRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTK----QILRQLLTGGVKRGRPSLKKPAALERQAAAGPTP-SP------ 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1582 GSGRASPPSTppppppgpppapfrpcAHLAFPPEPAPVSL-GKAGPSTE--APKVHPKPNSAPG---AGSCSSFPKIPys 1655
Cdd:PHA03378 859 GSGTSDKIVQ----------------APVFYPPVLQPIQVmRQLGSVRAaaASTVTQAPTEYTGerrGVGPMHPTDIP-- 920
|
....*....
gi 1622884518 1656 PVKAARVDA 1664
Cdd:PHA03378 921 PSKRAKTDA 929
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
70-287 |
2.01e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.22 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 70 LKHAKNPKVHF-DLADMIQDAIIHHNDKEVLRLLKEGADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDED 147
Cdd:PHA02875 55 MKHGAIPDVKYpDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 148 FWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSilltyldengvdltslrqmklqrpmsmltdV 227
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI------------------------------C 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884518 228 KHFLSSGGNVNEKNDEG-VTLLHMACASGYKEVVSLILEHGGDLNI---VDDQYWTPLHLAAKY 287
Cdd:PHA02875 185 KMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNImfmIEGEECTILDMICNM 248
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1369-1575 |
2.16e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1369 PRKPK--RSPNTKLSGSYEEisgSRPGDARPPGA--PGTAARVLTPGTPQCALPPATPPGDEDDGEPVYIEMLGHPARPD 1444
Cdd:PTZ00449 588 PKDPEepKKPKRPRSAQRPT---RPKSPKLPELLdiPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPK 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1445 SP-DPG--ESVYE----------EMKCCLPDDggPGAGSFLRASPPLLHGAPEDEaagppgdmcdiPPPFPNLLPHRPPL 1511
Cdd:PTZ00449 665 PPfDPKfkEKFYDdyldaaakskETKTTVVLD--ESFESILKETLPETPGTPFTT-----------PRPLPPKLPRDEEF 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1512 LVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYP-------------VQSEGSSPLSPQ------YSKSQKGDGDRP 1572
Cdd:PTZ00449 732 PFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPlpdilaeefkeedIHAETGEPDEAMkrpdspSEHEDKPPGDHP 811
|
...
gi 1622884518 1573 ASP 1575
Cdd:PTZ00449 812 SLP 814
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
130-297 |
2.20e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 49.06 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 130 IAEILIDRGVNVNHQDEDFWTPM-----HIACACDNPDIVLLLVLAGANVLLQDVNGNIPLdYAV--EGTESSSILLTYL 202
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLlsNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 203 DENGVDLTSLRQMKlqrpmsmLTDVKHFLSSGGNVNekndegvtllhmacasgyKEVVSLILEHGGDLNIVDDQY-WTPL 281
Cdd:PHA02798 132 IENGADTTLLDKDG-------FTMLQVYLQSNHHID------------------IEIIKLLLEKGVDINTHNNKEkYDTL 186
|
170 180
....*....|....*....|
gi 1622884518 282 HLAAKYG----QANLVKLLL 297
Cdd:PHA02798 187 HCYFKYNidriDADILKLFV 206
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
91-227 |
2.60e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 48.81 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 91 IHHNDKEVLRLLKE-GADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVL 169
Cdd:PHA02874 165 IKHNFFDIIKLLLEkGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINN 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884518 170 AGANVllQDVNGNIPLDYAVEGTESSSILLTYL---------DENGVDLTSLrQMKLQRPMSMLTDV 227
Cdd:PHA02874 245 ASIND--QDIDGSTPLHHAINPPCDIDIIDILLyhkadisikDNKGENPIDT-AFKYINKDPVIKDI 308
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
1342-1532 |
3.44e-05 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 48.80 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1342 AAREAANEAlarPRPHSDDYSTMKKIPPRKPKRSPntklsgsyeeisgsRPGDARPPGAPGTAARVLTPGTPQcaLPPAT 1421
Cdd:PHA03321 486 AAPPPEPAA---APSPATYYTRMGGGPPRLPPRNR--------------ATETLRPDWGPPAAAPPEQMEDPY--LEPDD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1422 PPGDEDDGEPVYIEmlGHPARPDSPDpGESVYEEMKcclpDDGGPGAGSF--LRASPPLLhGAPEDEAAGPPgdmcDIPP 1499
Cdd:PHA03321 547 DRFDRRDGAAAAAT--SHPREAPAPD-DDPIYEGVS----DSEEPVYEEIptPRVYQNPL-PRPMEGAGEPP----DLDA 614
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622884518 1500 PFPNLLPH--------RPPLLVFPPTPVTCSPASDESPLTP 1532
Cdd:PHA03321 615 PTSPWVEEenpiygwgDSPLFSPPPAARFPPPDPALSPEPP 655
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
278-307 |
4.37e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.28 E-value: 4.37e-05
10 20 30
....*....|....*....|....*....|.
gi 1622884518 278 WTPLHLAA-KYGQANLVKLLLMHQANPHLVN 307
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
83-189 |
4.71e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.10 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 83 ADMIQDAIIHH------NDKEVLR-LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMH 153
Cdd:PHA03095 183 VDDRFRSLLHHhlqsfkPRARIVReLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLH 262
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622884518 154 IACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAV 189
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1329-1656 |
9.09e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 47.45 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1329 LSASYEAVSACLSAAREAANEALARPRPHSddystmkkiPPRKPKRSPNTKLSgsyeeisgsrPGDARPPGAPGT----- 1403
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSA---------PSVPPQGSPATSQP----------PNQTQSTAAPHTliqqt 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1404 ----AARVLTPGTPQCALPPATPPgDEDDGEPVYIEMLgHPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLL 1479
Cdd:pfam03154 235 ptlhPQRLPSPHPPLQPMTQPPPP-SQVSPQPLPQPSL-HGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1480 hgaPEDEAAGPPGDMCDIPPPFPNLLPHRPPL-LVFPPTPVTCsPASDESPLTPleVKKLPVLETNlKYPVQSEGSSPLS 1558
Cdd:pfam03154 313 ---PSPAAPGQSQQRIHTPPSQSQLQSQQPPReQPLPPAPLSM-PHIKPPPTTP--IPQLPNPQSH-KHPPHLSGPSPFQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1559 PqysksqkgDGDRPASPGLALFngsgraSPPSTPPPPPPGPPPAPFRPCAHlAFPPEPAPVSLGKAGPSTEAPKV-HPKP 1637
Cdd:pfam03154 386 M--------NSNLPPPPALKPL------SSLSTHHPPSAHPPPLQLMPQSQ-QLPPPPAQPPVLTQSQSLPPPAAsHPPT 450
|
330
....*....|....*....
gi 1622884518 1638 NSAPGAGSCSSFPKIPYSP 1656
Cdd:pfam03154 451 SGLHQVPSQSPFPQHPFVP 469
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
243-272 |
1.10e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|
gi 1622884518 243 EGVTLLHMACASGYKEVVSLILEHGGDLNI 272
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
276-305 |
1.27e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.65 E-value: 1.27e-04
10 20 30
....*....|....*....|....*....|
gi 1622884518 276 QYWTPLHLAAKYGQANLVKLLLMHQANPHL 305
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1330-1616 |
1.64e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1330 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISG---SRPGDARPPGA-PGT-- 1403
Cdd:PHA03247 2800 SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAkPAApa 2879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1404 ---AARVLTPGTPQCALPPATPPgdeDDGEPvyiemlghPARPDSPDPGESVYEEMKCCLPDDGGPGAGsflRASPPLlh 1480
Cdd:PHA03247 2880 rppVRRLARPAVSRSTESFALPP---DQPER--------PPQPQAPPPPQPQPQPPPPPQPQPPPPPPP---RPQPPL-- 2943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1481 gAPEDEAAGPPGDMCDIPPP-FPNLLPHR---PPLLVFPPTPVTCSPASDESPLTPLEVKKL----------------PV 1540
Cdd:PHA03247 2944 -APTTDPAGAGEPSGAVPQPwLGALVPGRvavPRFRVPQPAPSREAPASSTPPLTGHSLSRVsswasslalheetdppPV 3022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1541 -LETNLKYPVQSEGSSPLSPQYSKSQKGDGDR----PASPGLALFNGSGRASppstppppppgpPPAPFRPCAHLAFPPE 1615
Cdd:PHA03247 3023 sLKQTLWPPDDTEDSDADSLFDSDSERSDLEAldplPPEPHDPFAHEPDPAT------------PEAGARESPSSQFGPP 3090
|
.
gi 1622884518 1616 P 1616
Cdd:PHA03247 3091 P 3091
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
95-217 |
2.02e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 95 DKEVLRLL-KEGAD-PHTLVSSGGSLLHLCARYD---NAFIAEILIDRGVNVNHQDEDFWTPMHI-ACACD-NPDIVLLL 167
Cdd:PHA02859 65 NVEILKFLiENGADvNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLL 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622884518 168 VLAGANVLLQDVNGNIPLdYAVEGTESSSILLTYLDENGVDLTSLRQMKL 217
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNIL-YSYILFHSDKKIFDFLTSLGIDINETNKSGY 193
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1344-1661 |
2.24e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.21 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1344 REAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYeeisgsrPGDARPPGAPGTAARVLTPGTP---------- 1413
Cdd:PHA03378 433 KKAARTEQPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQA-------PLEPWQPLPHPQVTPVILHQPPaqgvqahgsm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1414 ----------------QCALPPATP-PGDEDDGEPVYIEMLGhpARPDSPDPGESVYEEMkccLPDDG-GP--------G 1467
Cdd:PHA03378 506 ldllekddedmeqrvmATLLPPSPPqPRAGRRAPCVYTEDLD--IESDEPASTEPVHDQL---LPAPGlGPlqiqpltsP 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1468 AGSFLRASPPLLHGAP-----EDEAAGPPGDMCDIPP---PFPNLLPHRP-PLLVFPPTPVTCSPASDESPLTPLEVKKL 1538
Cdd:PHA03378 581 TTSQLASSAPSYAQTPwpvphPSQTPEPPTTQSHIPEtsaPRQWPMPLRPiPMRPLRMQPITFNVLVFPTPHQPPQVEIT 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1539 PVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDR----PASPGL----ALFNGSGRASPPSTPPPPPPGPPPAPFRPCAHL 1610
Cdd:PHA03378 661 PYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTmqppPRAPTPmrppAAPPGRAQRPAAATGRARPPAAAPGRARPPAAA 740
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622884518 1611 AFPPEPAPVSLGKAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPYSPVKAAR 1661
Cdd:PHA03378 741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPR 791
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
243-275 |
2.25e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 2.25e-04
10 20 30
....*....|....*....|....*....|....
gi 1622884518 243 EGVTLLHMACAS-GYKEVVSLILEHGGDLNIVDD 275
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
243-272 |
2.71e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.93 E-value: 2.71e-04
10 20 30
....*....|....*....|....*....|
gi 1622884518 243 EGVTLLHMACASGYKEVVSLILEHGGDLNI 272
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1367-1668 |
3.60e-04 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 45.44 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1367 IPPRKPKRSPNT---KLSGSYEEISGSRPGDARPPGAPGTAARvltPGTPQCALPPAT-PPGDEDDGEPVYIEMLGHPAR 1442
Cdd:COG5180 84 LDPAPPKSSPDTpeeQLGAPAGDLLVLPAAKTPELAAGALPAP---AAAAALPKAKVTrEATSASAGVALAAALLQRSDP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1443 PDSPDPGEsvyeemkccLPDDGGPGAGSFLR--ASPPLLHGAPEDEAAgppgdmcDIPPPfpnllPHRPPLLVFPPTPVT 1520
Cdd:COG5180 161 ILAKDPDG---------DSASTLPPPAEKLDkvLTEPRDALKDSPEKL-------DRPKV-----EVKDEAQEEPPDLTG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1521 CS-----PASDESPLTPLEvkklPVLETNLKYPVQSEG-SSPLSPQYSKSQKGDGDRPAS--PGL-ALFNGSGRASPPST 1591
Cdd:COG5180 220 GAdhprpEAASSPKVDPPS----TSEARSRPATVDAQPeMRPPADAKERRRAAIGDTPAAepPGLpVLEAGSEPQSDAPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1592 PPPPPPGPPPAPFRPcahlafPPEPAPVSLG---------KAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPYSPVKAARV 1662
Cdd:COG5180 296 AETARPIDVKGVASA------PPATRPVRPPggardpgtpRPGQPTERPAGVPEAASDAGQPPSAYPPAEEAVPGKPLEQ 369
|
....*.
gi 1622884518 1663 DARKAG 1668
Cdd:COG5180 370 GAPRPG 375
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
245-317 |
5.63e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 5.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884518 245 VTLLHMAcASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIA 317
Cdd:PTZ00322 84 VELCQLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
277-304 |
9.51e-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: 9.51e-04
10 20
....*....|....*....|....*...
gi 1622884518 277 YWTPLHLAAKYGQANLVKLLLMHQANPH 304
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1337-1529 |
1.33e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1337 SACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAArvltpgtpqca 1416
Cdd:PHA03307 227 SAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS----------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1417 lpPATPPGDEDDGEpvyiemlgHPARPDSPDPGESVYEEmkcclpDDGGPGAGSFLRASPPLLHGAPEDEAAGPPGDMCD 1496
Cdd:PHA03307 296 --PSPSPSSPGSGP--------APSSPRASSSSSSSRES------SSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPP 359
|
170 180 190
....*....|....*....|....*....|...
gi 1622884518 1497 IPPPFPnllPHRPPLLVFPPTPVTcSPASDESP 1529
Cdd:PHA03307 360 ADPSSP---RKRPRPSRAPSSPAA-SAGRPTRR 388
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
1365-1575 |
2.08e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 42.99 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1365 KKIPPRKPKRS--PNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQCALPPATPP------------------- 1423
Cdd:PLN03209 326 QRVPPKESDAAdgPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPiptppssspassksvdava 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1424 -GDEDDGEPVYIEMLGHP-----------ARPDSPdpgESVYEEMK-CCLPDDGGPGAGSFLRASPPLLHGAPEDEAAGP 1490
Cdd:PLN03209 406 kPAEPDVVPSPGSASNVPevepaqveakkTRPLSP---YARYEDLKpPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1491 PGDMCDIPPPFPNllPHRPPL----LVFPPTPVTCSPASDESPLTPLEVKKL--------PVLETNLKYPVQsegsSPLS 1558
Cdd:PLN03209 483 ATDAAAPPPANMR--PLSPYAvyddLKPPTSPSPAAPVGKVAPSSTNEVVKVgnsapptaLADEQHHAQPKP----RPLS 556
|
250
....*....|....*..
gi 1622884518 1559 PqYSKSQkgDGDRPASP 1575
Cdd:PLN03209 557 P-YTMYE--DLKPPTSP 570
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
1358-1547 |
2.10e-03 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 43.12 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1358 SDDYSTMKKipPRKPKRSPNT--KLSGSYEE------ISGSRPG--DARPPGA--PGTAARVLTPGT--PQCALPPATPP 1423
Cdd:PHA03377 520 TEEEESVTQ--PAKPHRKVQDgfQRSGRRQKratppkVSPSDRGppKASPPVMapPSTGPRVMATPStgPRDMAPPSTGP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1424 GDE---DDGEPVYIEMLGHP--ARPDSPDPgeSVYEEM--KCCLPDDGGPGAGSF--LRAS--------PPLLHGAPEDE 1486
Cdd:PHA03377 598 RQQakcKDGPPASGPHEKQPpsSAPRDMAP--SVVRMFlrERLLEQSTGPKPKSFweMRAGrdgsgiqqEPSSRRQPATQ 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884518 1487 AAgppgdmcdipPPFPNLLphrPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKY 1547
Cdd:PHA03377 676 ST----------PPRPSWL---PSVFVLPSVDAGRAQPSEESHLSSMSPTQPISHEEQPRY 723
|
|
| PHA03325 |
PHA03325 |
nuclear-egress-membrane-like protein; Provisional |
1392-1534 |
2.11e-03 |
|
nuclear-egress-membrane-like protein; Provisional
Pssm-ID: 223044 Cd Length: 418 Bit Score: 42.56 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1392 PGDARPPGAPGTAARVLTPGTPQCALPPATPPGDEDDGEPVyiemlgHPARPDSPDPGESVYEEMkcclpDDGGPGAGSF 1471
Cdd:PHA03325 282 AMRAAAGETADLADDDGSEHSDPEPLPASLPPPPVRRPRVK------HPEAGKEEPDGARNAEAK-----EPAQPATSTS 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1472 LRASPpllHGAPEDEAAGPPGDMC-------DIPPPFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLE 1534
Cdd:PHA03325 351 SKGSS---SAQNKDSGSTGPGSSLaaassflEDDDFGSPPLDLTTSLRHMPSPSVTSAPEPPSIPLTYLS 417
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
149-178 |
3.02e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 3.02e-03
10 20 30
....*....|....*....|....*....|.
gi 1622884518 149 WTPMHIACA-CDNPDIVLLLVLAGANVLLQD 178
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1375-1561 |
3.06e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 42.51 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1375 SPNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQC-ALPPATP--PGDEDDGEP-----------VYIEMLGHP 1440
Cdd:PRK14086 96 APPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQdQLPTARPayPAYQQRPEPgawpraaddygWQQQRLGFP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1441 ARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPpllHGaPEDEAAGPPGDMCDIPPPFPNllPHRPPLLVFPPTPVT 1520
Cdd:PRK14086 176 PRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDY---DH-PRPDWDRPRRDRTDRPEPPPG--AGHVHRGGPGPPERD 249
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622884518 1521 CSPASDESPLTPLEVKKLPvlETNlkyPVQSEGSSPLSPQY 1561
Cdd:PRK14086 250 DAPVVPIRPSAPGPLAAQP--APA---PGPGEPTARLNPKY 285
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1356-1490 |
3.09e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1356 PHS-DDYSTMKKIPPRKP-----------KRSPNTKLSGSYEEISGSRPGDARPP--GAPGTAARVltPGTPQCALPPAT 1421
Cdd:PHA03247 362 PSSlEDLSAGRHHPKRASlptrkrrsarhAATPFARGPGGDDQTRPAAPVPASVPtpAPTPVPASA--PPPPATPLPSAE 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884518 1422 PPGDEDDGEPVYiemlGHPARPDSPDPGESvyeemkcclPDDGGPGAGSFLRASPPllhgaPEDEAAGP 1490
Cdd:PHA03247 440 PGSDDGPAPPPE----RQPPAPATEPAPDD---------PDDATRKALDALRERRP-----PEPPGADL 490
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
101-155 |
3.96e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 3.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884518 101 LLKEG-ADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIA 155
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
236-310 |
3.99e-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: 41.99 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 236 NVNEKNDEGVTLLHMAcASGYKEVVSLILEH-------GGDLNIVDDQYW-------TPLHLAAKYGQANLVKLLLMHQA 301
Cdd:TIGR00870 74 NLSCRGAVGDTLLHAI-SLEYVDAVEAILLHllaafrkSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGA 152
|
90
....*....|
gi 1622884518 302 NPHL-VNCNE 310
Cdd:TIGR00870 153 SVPArACGDF 162
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
281-331 |
4.85e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.17 E-value: 4.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884518 281 LHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAAS----EFIEEMLLKAEI 331
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKnghlEIVKLLLEHADV 55
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
147-174 |
5.10e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 5.10e-03
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
149-174 |
5.75e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 5.75e-03
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
91-283 |
5.76e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 41.54 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 91 IHHNDKEVL-RLLK-EGADPHTLVSSGGSLLHLCARYDNAFIAEILID---RGVNVNHQDEDFW--TPMHIACACDNPDI 163
Cdd:cd22192 25 AKENDVQAIkKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDLYQgeTALHIAVVNQNLNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 164 VLLLVLAGANVLLQDVNGnipldyavegtesssillTYLdengvdltslrqmkLQRPMSMLTDVKHFLSsggnvneknde 243
Cdd:cd22192 105 VRELIARGADVVSPRATG------------------TFF--------------RPGPKNLIYYGEHPLS----------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622884518 244 gvtllHMACAsGYKEVVSLILEHGGDLNIVDDQYWTPLHL 283
Cdd:cd22192 142 -----FAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1395-1667 |
6.05e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1395 ARPPGAPGTAARVLTPGTPQCALPPatpPGDEDDGEPVYIEMLGHPARPDSPDPGESVYEEmkcclpDDGGPGAGSFLRA 1474
Cdd:PHA03307 22 PRPPATPGDAADDLLSGSQGQLVSD---SAELAAVTVVAGAAACDRFEPPTGPPPGPGTEA------PANESRSTPTWSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1475 SPPLLHGAPEDEAAGPPGdmcdipppfpnllphRPPLLVFPPTPVTCSPASDESPLTPlevkklPVLETNLKYPVQSEGS 1554
Cdd:PHA03307 93 STLAPASPAREGSPTPPG---------------PSSPDPPPPTPPPASPPPSPAPDLS------EMLRPVGSPGPPPAAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884518 1555 SPLSPqySKSQKGDGDRPASPGLALFNGSGRASPPSTPPPPPpgpppapfrpcahlAFPPEPAPVSLGKAGPSTEAPKVH 1634
Cdd:PHA03307 152 PPAAG--ASPAAVASDAASSRQAALPLSSPEETARAPSSPPA--------------EPPPSTPPAAASPRPPRRSSPISA 215
|
250 260 270
....*....|....*....|....*....|...
gi 1622884518 1635 PKPNSAPGAGSCSSFPKIPYSPVKAARVDARKA 1667
Cdd:PHA03307 216 SASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248
|
|
| |
