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Conserved domains on  [gi|189083798|ref|NP_000251|]
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unconventional myosin-VIIa isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
79-729 0e+00

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: 1391.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 238
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEI 318
Cdd:cd01381   161 KSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  319 SKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAF 398
Cdd:cd01381   241 FKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  399 VKGIYGRLFVWIVDKINAAIYKPPSQDvkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYD 478
Cdd:cd01381   321 VKGIYGRLFIWIVNKINSAIYKPRGTD--SSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  479 LESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGINHFAGIV 558
Cdd:cd01381   399 KEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFAGVV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  559 YYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKP 638
Cdd:cd01381   479 FYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKP 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  639 NEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQrMAEAVLGTHDD 718
Cdd:cd01381   559 NEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRK-ICCAVLGGDAD 637
                         650
                  ....*....|.
gi 189083798  719 WQIGKTKIFLK 729
Cdd:cd01381   638 YQLGKTKIFLK 648
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
2111-2206 9.41e-67

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270020  Cd Length: 96  Bit Score: 220.21  E-value: 9.41e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2111 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2190
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80
                          90
                  ....*....|....*.
gi 189083798 2191 DDLLTSYISQMLTAMS 2206
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1257-1355 1.10e-65

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340612  Cd Length: 99  Bit Score: 217.12  E-value: 1.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1257 PIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQ 1336
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 189083798 1337 ERNAPWRLFFRKEVFTPWH 1355
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1901-1998 1.55e-62

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340613  Cd Length: 98  Bit Score: 208.25  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1901 QIFHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSVPENDFFFDFVRHLTDWIKKARPIK 1980
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80
                          90
                  ....*....|....*...
gi 189083798 1981 DGIVPSLTYQVFFMKKLW 1998
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1763-1896 1.19e-58

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


:

Pssm-ID: 214535  Cd Length: 152  Bit Score: 199.12  E-value: 1.19e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1763 SEELSQEACLAFIAVLKYMGDYPSKRTRSVNELTDQIFEGPLKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTG 1842
Cdd:smart00139   15 SDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEERGWQLLYLCTS 94
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798   1843 LFPPSNILLPHVQRFLQSRKHC----PLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQ 1896
Cdd:smart00139   95 LFPPSERLLPYLLQFLSRRADPgseqGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1017-1253 2.04e-55

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


:

Pssm-ID: 214535  Cd Length: 152  Bit Score: 189.88  E-value: 2.04e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1017 YTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPkyhtamsdgsekipvmtkiyetlgkktykrelqalqgegea 1096
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGDIPLP----------------------------------------- 39
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1097 qlpegqkkssvrhklvhltlkkksklteevtkrlhdgestvqgnsmledRPTSNLEKLHFIIGNGILRPALRDEIYCQIS 1176
Cdd:smart00139   40 -------------------------------------------------RPDSHLDLVQFILQKGLDHPELRDEIYCQLI 70
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1177 KQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPP-----GYAPYCEERLRRTFVNGTRTQPPSWLELQA 1251
Cdd:smart00139   71 KQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseqGLAKYCLYRLERTLKNGARKQPPSRLELEA 150

                    ..
gi 189083798   1252 TK 1253
Cdd:smart00139  151 IL 152
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
1468-1604 9.84e-52

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270019  Cd Length: 99  Bit Score: 177.41  E-value: 9.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1468 LLFSRFYEAYKFSGPSLPKNDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSrecrvwlslgcsdlgcaaphsgwag 1547
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSS------------------------- 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798 1548 ltpagpcspcwscRGAKTTAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKR 1604
Cdd:cd13198    56 -------------RGKRDGGQSFTLTTIQGEEFVFQSPNAEDIAELVNYFLEGLRKR 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1903-2115 6.01e-47

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 167.86  E-value: 6.01e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1903 FHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSvpendfffdfvrhltDWIKKARPIKDG 1982
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1983 IVPSLTYQVFFMKKLWTTTV--PGKDPMADsIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPK-- 2058
Cdd:smart00295   66 DVKSEPLTLYFRVKFYPPDPnqLKEDPTRL-NLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798   2059 LLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFF 2115
Cdd:smart00295  145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1259-1474 2.95e-38

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 142.82  E-value: 2.95e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1259 MLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVsslgsgsdhvmdaISQCEQYAKEQGAQER 1338
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1339 N-APWRLFFRKEVFTPWHS-PSEDNVATNLIYQQVVRGVKFGEYRCEKEdDLAELASQQYFVDYG---SEMILERLLNLV 1413
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEE-EALLLAALALQAEFGdydEELHDLRGELSL 146
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083798   1414 PTYIPDREITPlKTLEKWAQLAIAAHKKGIYaQRRTDAqKVKedVVSYARfKWPLLFSRFY 1474
Cdd:smart00295  147 KRFLPKQLLDS-RKLKEWRERIVELHKELIG-LSPEEA-KLK--YLELAR-KLPTYGVELF 201
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
1605-1669 1.02e-34

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


The actual alignment was detected with superfamily member cd11881:

Pssm-ID: 473055  Cd Length: 64  Bit Score: 127.63  E-value: 1.02e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189083798 1605 SKYVVALQDNPNPAGEeSGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDSVYV 1669
Cdd:cd11881     1 SKYVVALQDYPNPSDG-SSFLSFAKGDLIILDQDTGEQVMNSGWCNGRNDRTGQRGDFPADCVYV 64
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
857-933 7.69e-09

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


:

Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 56.59  E-value: 7.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   857 QRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQ---ERLAQL----------AREDAERELKEKE------ 917
Cdd:pfam05672   49 RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQreqEEQERLqkqkeeaeakAREEAERQRQEREkimqqe 128
                           90
                   ....*....|....*....
gi 189083798   918 -AAR--RKKELLEQMERAR 933
Cdd:pfam05672  129 eQERleRKKRIEEIMKRTR 147
tolA super family cl35847
cell envelope integrity inner membrane protein TolA; Provisional
796-966 4.69e-05

cell envelope integrity inner membrane protein TolA; Provisional


The actual alignment was detected with superfamily member PRK09510:

Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  796 RLQALHRSRKLHQQYRLARQRiiQFQARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRLA 875
Cdd:PRK09510  110 RLAAQEQKKQAEEAAKQAALK--QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  876 EEEKLRKEMSAKKAKEEAERKhqERLAQLAREDAERELKEK--EAARRKKELLEQMERA----RHEPVNHSDMVDKMFGF 949
Cdd:PRK09510  188 EAEAAAKAAAEAKKKAEAEAK--KKAAAEAKKKAAAEAKAAaaKAAAEAKAAAEKAAAAkaaeKAAAAKAAAEVDDLFGG 265
                         170       180
                  ....*....|....*....|...
gi 189083798  950 LGTSGGLPGQ------EGQAPSG 966
Cdd:PRK09510  266 LDSGKNAPKTgggakgNGAQGAG 288
CBD_MYO6-like super family cl41207
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
766-809 1.22e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


The actual alignment was detected with superfamily member cd21759:

Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 41.34  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 189083798  766 KLKN-------AATLIQRHWRGHNCRKNYGlmrlgfLRLQALHRSRKLHQQ 809
Cdd:cd21759    36 KLKNkilyrreALIKIQKTVRGYLARKKHR------PRIKGLRKIRALEKQ 80
 
Name Accession Description Interval E-value
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
79-729 0e+00

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: 1391.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 238
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEI 318
Cdd:cd01381   161 KSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  319 SKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAF 398
Cdd:cd01381   241 FKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  399 VKGIYGRLFVWIVDKINAAIYKPPSQDvkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYD 478
Cdd:cd01381   321 VKGIYGRLFIWIVNKINSAIYKPRGTD--SSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  479 LESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGINHFAGIV 558
Cdd:cd01381   399 KEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFAGVV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  559 YYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKP 638
Cdd:cd01381   479 FYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKP 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  639 NEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQrMAEAVLGTHDD 718
Cdd:cd01381   559 NEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRK-ICCAVLGGDAD 637
                         650
                  ....*....|.
gi 189083798  719 WQIGKTKIFLK 729
Cdd:cd01381   638 YQLGKTKIFLK 648
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
60-741 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: 1044.05  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798     60 HPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIAD 139
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    140 NCYFNMKRNSRDQCCIISGESGAGKTESTKLILQFLAAISGQ---HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKY 216
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSnteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    217 IDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQ 296
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    297 EYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLI 376
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDN-AASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    377 TRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSqdvknSRRSIGLLDIFGFENFAVNSFEQLCINF 456
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    457 ANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNA 536
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    537 NYIPPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDVAMGAETRKRSPTLSSQFKR 616
Cdd:smart00242  475 HFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP-SGVSNAGSKKRFQTVGSQFKE 553
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    617 SLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAy 696
Cdd:smart00242  554 QLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPP- 632
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*
gi 189083798    697 KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERD 741
Cdd:smart00242  633 WGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
67-729 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 850.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    67 VEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMK 146
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   147 RNSRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW-----IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF 221
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   222 NKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANI 301
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   302 RSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGET 381
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKE--RNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRET 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   382 VSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPpsqdvKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEH 460
Cdd:pfam00063  319 VSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVK-----TIEKASfIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   461 LQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIP 540
Cdd:pfam00063  394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   541 PKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ------------ADVAMGAETRKRSP 608
Cdd:pfam00063  474 PRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPdyetaesaaaneSGKSTPKRTKKKRF 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   609 -TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRV 687
Cdd:pfam00063  554 iTVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRI 633
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 189083798   688 LLPGVKPAYKqGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:pfam00063  634 LAPKTWPKWK-GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
59-946 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 798.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   59 MHPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIA 138
Cdd:COG5022    60 IKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  139 DNCYFNMKRNSRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRNDNSSRFG 214
Cdd:COG5022   140 EEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVeissIEKQILATNPILEAFGNAKTVRNDNSSRFG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  215 KYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVD 294
Cdd:COG5022   220 KYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDD 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  295 SQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQY-EARTfenlDACEVLFSPSLATAASLLEVNPPDLMSCLTSR 373
Cdd:COG5022   300 AKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFkEDRN----GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKR 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  374 TLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDvknsrRSIGLLDIFGFENFAVNSFEQLC 453
Cdd:COG5022   376 QIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-----NFIGVLDIYGFEIFEKNSFEQLC 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  454 INFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANK-PMNIISLIDEESKFPKGTDTTMLHKLNSQH 532
Cdd:COG5022   451 INYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRL 530
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  533 KLNAN--YIPPKNNhETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqaDVAMGAETRKRSPTL 610
Cdd:COG5022   531 NKNSNpkFKKSRFR-DNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF--DDEENIESKGRFPTL 607
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  611 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLP 690
Cdd:COG5022   608 GSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSP 687
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  691 GVKPAY---KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKAITDRVILLQKVIRGFKDRSNFLKL 767
Cdd:COG5022   688 SKSWTGeytWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQA 767
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  768 KNAATLIQRhwRGHN----CRKNYGLMRLGFLRLQALHRSRKLHQQYRLARQRIIQFQARCRAYLVRK-----AFRHRlw 838
Cdd:COG5022   768 LKRIKKIQV--IQHGfrlrRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLReteevEFSLK-- 843
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  839 AVLTVQAYARGMIARR-----LHQRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAK------------------EEAER 895
Cdd:COG5022   844 AEVLIQKFGRSLKAKKrfsllKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVnleleseiielkkslssdLIENL 923
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798  896 KHQ-ERLAQLAREDAEREL-----KEKEAARRKKELLEQMERARHEPVNHSDMVDKM 946
Cdd:COG5022   924 EFKtELIARLKKLLNNIDLeegpsIEYVKLPELNKLHEVESKLKETSEEYEDLLKKS 980
PTZ00014 PTZ00014
myosin-A; Provisional
73-781 4.75e-153

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 496.09  E-value: 4.75e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   73 LGDL---NEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQY-TNKKIGEMPPHIFAIADNCYFNMKRN 148
Cdd:PTZ00014  101 IGLLphtNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGV 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  149 SRDQCCIISGESGAGKTESTKLILQFLAAISGQH--SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGA 226
Cdd:PTZ00014  181 KKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNmdLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  227 IEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAmGNCITCEGRVDSQEYANIRSAMK 306
Cdd:PTZ00014  261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEEVMESFD 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  307 VLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLAT---AASLLEVNPPDLMSCLTSRTLITRGETVS 383
Cdd:PTZ00014  340 SMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLEVfneACELLFLDYESLKKELTVKVTYAGNQKIE 419
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  384 TPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIyKPPsqdvKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQ 463
Cdd:PTZ00014  420 GPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATI-EPP----GGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  464 FFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKN 543
Cdd:PTZ00014  495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSpTLSSQFKRSLELLMR 623
Cdd:PTZ00014  575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQ-LIGSQFLNQLDSLMS 653
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  624 TLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVL-LPGVKPayKQGDLR 702
Cdd:PTZ00014  654 LINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAVSND--SSLDPK 731
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  703 GTCQRMAEAVLGTHDDWQIGKTKIFLK-DHHDMLLEVERDK--AITDRVILLQKVIRGFKDRSNFLKLKNAATLIQRHWR 779
Cdd:PTZ00014  732 EKAEKLLERSGLPKDSYAIGKTMVFLKkDAAKELTQIQREKlaAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLR 811

                  ..
gi 189083798  780 GH 781
Cdd:PTZ00014  812 RH 813
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
2111-2206 9.41e-67

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270020  Cd Length: 96  Bit Score: 220.21  E-value: 9.41e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2111 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2190
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80
                          90
                  ....*....|....*.
gi 189083798 2191 DDLLTSYISQMLTAMS 2206
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1257-1355 1.10e-65

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 217.12  E-value: 1.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1257 PIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQ 1336
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 189083798 1337 ERNAPWRLFFRKEVFTPWH 1355
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1901-1998 1.55e-62

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 208.25  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1901 QIFHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSVPENDFFFDFVRHLTDWIKKARPIK 1980
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80
                          90
                  ....*....|....*...
gi 189083798 1981 DGIVPSLTYQVFFMKKLW 1998
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1763-1896 1.19e-58

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 199.12  E-value: 1.19e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1763 SEELSQEACLAFIAVLKYMGDYPSKRTRSVNELTDQIFEGPLKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTG 1842
Cdd:smart00139   15 SDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEERGWQLLYLCTS 94
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798   1843 LFPPSNILLPHVQRFLQSRKHC----PLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQ 1896
Cdd:smart00139   95 LFPPSERLLPYLLQFLSRRADPgseqGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1017-1253 2.04e-55

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 189.88  E-value: 2.04e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1017 YTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPkyhtamsdgsekipvmtkiyetlgkktykrelqalqgegea 1096
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGDIPLP----------------------------------------- 39
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1097 qlpegqkkssvrhklvhltlkkksklteevtkrlhdgestvqgnsmledRPTSNLEKLHFIIGNGILRPALRDEIYCQIS 1176
Cdd:smart00139   40 -------------------------------------------------RPDSHLDLVQFILQKGLDHPELRDEIYCQLI 70
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1177 KQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPP-----GYAPYCEERLRRTFVNGTRTQPPSWLELQA 1251
Cdd:smart00139   71 KQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseqGLAKYCLYRLERTLKNGARKQPPSRLELEA 150

                    ..
gi 189083798   1252 TK 1253
Cdd:smart00139  151 IL 152
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
1468-1604 9.84e-52

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270019  Cd Length: 99  Bit Score: 177.41  E-value: 9.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1468 LLFSRFYEAYKFSGPSLPKNDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSrecrvwlslgcsdlgcaaphsgwag 1547
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSS------------------------- 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798 1548 ltpagpcspcwscRGAKTTAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKR 1604
Cdd:cd13198    56 -------------RGKRDGGQSFTLTTIQGEEFVFQSPNAEDIAELVNYFLEGLRKR 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1903-2115 6.01e-47

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 167.86  E-value: 6.01e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1903 FHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSvpendfffdfvrhltDWIKKARPIKDG 1982
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1983 IVPSLTYQVFFMKKLWTTTV--PGKDPMADsIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPK-- 2058
Cdd:smart00295   66 DVKSEPLTLYFRVKFYPPDPnqLKEDPTRL-NLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798   2059 LLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFF 2115
Cdd:smart00295  145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1154-1251 6.26e-42

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 149.65  E-value: 6.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  1154 LHFIIGNGILRPALRDEIYCQISKQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIH-------GGPPGYAPY 1226
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpsREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 189083798  1227 CEERLRRTFVNGTRTQPPSWLELQA 1251
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1259-1474 2.95e-38

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 142.82  E-value: 2.95e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1259 MLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVsslgsgsdhvmdaISQCEQYAKEQGAQER 1338
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1339 N-APWRLFFRKEVFTPWHS-PSEDNVATNLIYQQVVRGVKFGEYRCEKEdDLAELASQQYFVDYG---SEMILERLLNLV 1413
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEE-EALLLAALALQAEFGdydEELHDLRGELSL 146
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083798   1414 PTYIPDREITPlKTLEKWAQLAIAAHKKGIYaQRRTDAqKVKedVVSYARfKWPLLFSRFY 1474
Cdd:smart00295  147 KRFLPKQLLDS-RKLKEWRERIVELHKELIG-LSPEEA-KLK--YLELAR-KLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1796-1894 2.71e-37

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 136.17  E-value: 2.71e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  1796 TDQIFEGPLKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTGLFPPSNILLPHVQRFLQ------SRKHCPLAID 1869
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpSREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 189083798  1870 CLQRLQKALRNGSRKYPPHLVEVEA 1894
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
1605-1669 1.02e-34

Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin that is involved in organelle transport. It is required for sensory function in both Drosophila and mammals. Mutations in the Myo7A gene cause both syndromic deaf-blindness [Usher syndrome I (USH1)] and nonsyndromic (DFNB2 and DFNA11) deafness in humans. It contains an N-terminal motor domain, light chain-binding IQ motifs, a coiled-coil region for heavy chain dimerization, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212814  Cd Length: 64  Bit Score: 127.63  E-value: 1.02e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189083798 1605 SKYVVALQDNPNPAGEeSGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDSVYV 1669
Cdd:cd11881     1 SKYVVALQDYPNPSDG-SSFLSFAKGDLIILDQDTGEQVMNSGWCNGRNDRTGQRGDFPADCVYV 64
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
2013-2115 3.43e-20

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 88.10  E-value: 3.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  2013 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF--EEDKSYFPSIPKLLReLVPQDLIRQVSPDDWKRSIVAYFNKHAG 2090
Cdd:pfam00373   14 LLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFgdYQPSSHTSEYLSLES-FLPKQLLRKMKSKELEKRVLEAHKNLRG 92
                           90       100
                   ....*....|....*....|....*
gi 189083798  2091 KSKEEAKLAFLKLIFKWPTFGSAFF 2115
Cdd:pfam00373   93 LSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
2013-2107 1.23e-18

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 83.06  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2013 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF-EEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGK 2091
Cdd:cd14473     4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYgDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83
                          90
                  ....*....|....*.
gi 189083798 2092 SKEEAKLAFLKLIFKW 2107
Cdd:cd14473    84 SPAEAKLKYLKIARKL 99
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
1363-1463 2.54e-10

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 59.18  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1363 ATNLIYQQVVRGVKFGEYRCeKEDDLAELASQQYFVDYG--SEMILERLLNLVPTYIPDREITPLKtLEKWAQLAIAAHK 1440
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPC-SEETAALLAALALQAEYGdyDPSEHKPKYLSLKRFLPKQLLKQRK-PEEWEKRIVELHK 78
                          90       100
                  ....*....|....*....|...
gi 189083798 1441 KgiyaQRRTDAQKVKEDVVSYAR 1463
Cdd:cd14473    79 K----LRGLSPAEAKLKYLKIAR 97
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
857-933 7.69e-09

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 56.59  E-value: 7.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   857 QRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQ---ERLAQL----------AREDAERELKEKE------ 917
Cdd:pfam05672   49 RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQreqEEQERLqkqkeeaeakAREEAERQRQEREkimqqe 128
                           90
                   ....*....|....*....
gi 189083798   918 -AAR--RKKELLEQMERAR 933
Cdd:pfam05672  129 eQERleRKKRIEEIMKRTR 147
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
853-924 9.24e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 53.31  E-value: 9.24e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189083798   853 RRLHQRLRAEYLWRlEAEKMRLAEEEKlRKEMSAKKAKEEAERKhqerlaqlAREDAERELKEKEAARRKKE 924
Cdd:TIGR02794   92 KELEQRAAAEKAAK-QAEQAAKQAEEK-QKQAEEAKAKQAAEAK--------AKAEAEAERKAKEEAAKQAE 153
PTZ00121 PTZ00121
MAEBL; Provisional
804-935 1.41e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  804 RKLHQQYRLARQRIIQFQarcRAYLVRKAFRHRLWAVLTVQAYARGMIArrlhQRLRAEYLWRLEAEKMRLAEEEKLRKE 883
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKA----EEAKKAEEAKIKAEELKKAEEEKKKVE 1636
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  884 MSAKKAKEE---AE--RKHQE----RLAQLAREDAE-----RELKEKEAARRKKEllEQMERARHE 935
Cdd:PTZ00121 1637 QLKKKEAEEkkkAEelKKAEEenkiKAAEEAKKAEEdkkkaEEAKKAEEDEKKAA--EALKKEAEE 1700
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
874-933 4.92e-06

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 46.11  E-value: 4.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  874 LAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERAR 933
Cdd:cd22249     1 LSKPGEIREEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRKREREEQLKQDE 60
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
857-935 5.66e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.58  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  857 QRLRAEylwrLEAEKMRLAEEEKLRKEMSAKKAKEEAERK---HQERLAQLAREDAERELK-EKEAARRKKELLEQMERA 932
Cdd:COG3064    25 KRAAAE----AEQKAKEEAEEERLAELEAKRQAEEEAREAkaeAEQRAAELAAEAAKKLAEaEKAAAEAEKKAAAEKAKA 100

                  ...
gi 189083798  933 RHE 935
Cdd:COG3064   101 AKE 103
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
796-966 4.69e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  796 RLQALHRSRKLHQQYRLARQRiiQFQARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRLA 875
Cdd:PRK09510  110 RLAAQEQKKQAEEAAKQAALK--QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  876 EEEKLRKEMSAKKAKEEAERKhqERLAQLAREDAERELKEK--EAARRKKELLEQMERA----RHEPVNHSDMVDKMFGF 949
Cdd:PRK09510  188 EAEAAAKAAAEAKKKAEAEAK--KKAAAEAKKKAAAEAKAAaaKAAAEAKAAAEKAAAAkaaeKAAAAKAAAEVDDLFGG 265
                         170       180
                  ....*....|....*....|...
gi 189083798  950 LGTSGGLPGQ------EGQAPSG 966
Cdd:PRK09510  266 LDSGKNAPKTgggakgNGAQGAG 288
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
795-1042 5.70e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  795 LRLQALHRSRKLHQQYRLARQRIIQFQARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRL 874
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  875 AEEEKLRKEMSAKKAKEEAERKHQERLAQLA-REDAERELKEKEAARRKKELLEQMERARHEPVnhSDMVDKMFGFLGTS 953
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLElLAELLEEAALLEAALAELLEELAEAAARLLLL--LEAEADYEGFLEGV 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  954 GGLPGQEGQAP-SGFEDLERGRREMVEEDLDAAL-----PLPDEDEEDLSEY-KFAKFA----ATYFQGTTTHSYTRRPL 1022
Cdd:COG1196   511 KAALLLAGLRGlAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAiEYLKAAkagrATFLPLDKIRARAALAA 590
                         250       260
                  ....*....|....*....|
gi 189083798 1023 KQPLLYHDDEGDQLAALAVW 1042
Cdd:COG1196   591 ALARGAIGAAVDLVASDLRE 610
growth_prot_Scy NF041483
polarized growth protein Scy;
857-941 6.21e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.67  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  857 QRLRAEylwrlEAEKMRLAEE--EKLRKEmsAKKAKEEAERKhQERLAQLAREDAERELKE--KEAARRKKELLEQMERA 932
Cdd:NF041483  971 ERLRAE-----AAETVGSAQQhaERIRTE--AERVKAEAAAE-AERLRTEAREEADRTLDEarKDANKRRSEAAEQADTL 1042

                  ....*....
gi 189083798  933 RHEPVNHSD 941
Cdd:NF041483 1043 ITEAAAEAD 1051
growth_prot_Scy NF041483
polarized growth protein Scy;
857-935 2.05e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 46.74  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  857 QRLRAEyLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLARE-------------DAERELKE--KEAARR 921
Cdd:NF041483  527 ERTRAE-AERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEEltrlhteaeerltAAEEALADarAEAERI 605
                          90
                  ....*....|....
gi 189083798  922 KKELLEQMERARHE 935
Cdd:NF041483  606 RREAAEETERLRTE 619
growth_prot_Scy NF041483
polarized growth protein Scy;
796-941 6.30e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.20  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  796 RLQAlhrsrKLHQQYRLARQRIIQFQARCRAYLVRKAFRHRLWAVltvQAYARG-MIARRLHQRLRAEY---LWRLEAEK 871
Cdd:NF041483  116 RLQA-----ELHTEAVQRRQQLDQELAERRQTVESHVNENVAWAE---QLRARTeSQARRLLDESRAEAeqaLAAARAEA 187
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  872 MRLAEEEKLRKEMSAKKAKEEAERkhqerLAQLAREDAERELkeKEAARRKKELLEQMERARHEPVNHSD 941
Cdd:NF041483  188 ERLAEEARQRLGSEAESARAEAEA-----ILRRARKDAERLL--NAASTQAQEATDHAEQLRSSTAAESD 250
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
844-1006 8.65e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 43.13  E-value: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   844 QAYARGM-IARRLHQRLRAEYL----WRLEAEKMRLAEEEKLRKEMSAKKAKEE--AERKHQER------LAQLAREDAE 910
Cdd:pfam04012   43 QALAQTIaRQKQLERRLEQQTEqakkLEEKAQAALTKGNEELAREALAEKKSLEkqAEALETQLaqqrsaVEQLRKQLAA 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   911 RELKEKEAARRKKELLEQMERARHEpvnhsDMVDKMFGFLGTSGglpgqegqAPSGFEDLERGRREMvEEDLDAALPLPD 990
Cdd:pfam04012  123 LETKIQQLKAKKNLLKARLKAAKAQ-----EAVQTSLGSLSTSS--------ATDSFERIEEKIEER-EARADAAAELAS 188
                          170
                   ....*....|....*.
gi 189083798   991 EDEEDlseykfAKFAA 1006
Cdd:pfam04012  189 AVDLD------AKLEQ 198
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1604-1667 1.00e-03

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 39.06  E-value: 1.00e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083798   1604 RSKYVVALQDNPnpaGEESGFLSFAKGDLIILDHDTgeqvmNSGWANGINERtKQRGDFPTDSV 1667
Cdd:smart00326    1 EGPQVRALYDYT---AQDPDELSFKKGDIITVLEKS-----DDGWWKGRLGR-GKEGLFPSNYV 55
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
1359-1441 1.11e-03

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 40.72  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  1359 EDNVATNLIYQQVVRGVKFGEYRCEkEDDLAELASQQYFVDYG---------SEMILERllnlvptYIPDREITPLKTlE 1429
Cdd:pfam00373    7 QDEVTRHLLYLQAKDDILEGRLPCS-EEEALLLAALQLQAEFGdyqpsshtsEYLSLES-------FLPKQLLRKMKS-K 77
                           90
                   ....*....|..
gi 189083798  1430 KWAQLAIAAHKK 1441
Cdd:pfam00373   78 ELEKRVLEAHKN 89
growth_prot_Scy NF041483
polarized growth protein Scy;
804-933 1.12e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.43  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  804 RKLhQQYRLARQRIIQ----FQARCRAYLVRKAF--RHRLWAVL-----TVQAYARGMIArrLHQRLRAeylwRLEAEKM 872
Cdd:NF041483   94 REL-RDARAQTQRILQehaeHQARLQAELHTEAVqrRQQLDQELaerrqTVESHVNENVA--WAEQLRA----RTESQAR 166
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083798  873 RLAEEEKLRKEMSAKKAKEEAERkhqerlaqLAREDAERELKEKEAARRKKELLeqMERAR 933
Cdd:NF041483  167 RLLDESRAEAEQALAAARAEAER--------LAEEARQRLGSEAESARAEAEAI--LRRAR 217
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
766-809 1.22e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 41.34  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 189083798  766 KLKN-------AATLIQRHWRGHNCRKNYGlmrlgfLRLQALHRSRKLHQQ 809
Cdd:cd21759    36 KLKNkilyrreALIKIQKTVRGYLARKKHR------PRIKGLRKIRALEKQ 80
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
766-787 1.26e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 38.08  E-value: 1.26e-03
                            10        20
                    ....*....|....*....|..
gi 189083798    766 KLKNAATLIQRHWRGHNCRKNY 787
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
768-787 3.55e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.53  E-value: 3.55e-03
                           10        20
                   ....*....|....*....|
gi 189083798   768 KNAATLIQRHWRGHNCRKNY 787
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRY 20
 
Name Accession Description Interval E-value
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
79-729 0e+00

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: 1391.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 238
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEI 318
Cdd:cd01381   161 KSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  319 SKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAF 398
Cdd:cd01381   241 FKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  399 VKGIYGRLFVWIVDKINAAIYKPPSQDvkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYD 478
Cdd:cd01381   321 VKGIYGRLFIWIVNKINSAIYKPRGTD--SSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  479 LESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGINHFAGIV 558
Cdd:cd01381   399 KEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFAGVV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  559 YYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKP 638
Cdd:cd01381   479 FYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKP 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  639 NEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQrMAEAVLGTHDD 718
Cdd:cd01381   559 NEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRK-ICCAVLGGDAD 637
                         650
                  ....*....|.
gi 189083798  719 WQIGKTKIFLK 729
Cdd:cd01381   638 YQLGKTKIFLK 648
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
60-741 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: 1044.05  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798     60 HPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIAD 139
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    140 NCYFNMKRNSRDQCCIISGESGAGKTESTKLILQFLAAISGQ---HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKY 216
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSnteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    217 IDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQ 296
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    297 EYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLI 376
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDN-AASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    377 TRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSqdvknSRRSIGLLDIFGFENFAVNSFEQLCINF 456
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    457 ANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNA 536
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    537 NYIPPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDVAMGAETRKRSPTLSSQFKR 616
Cdd:smart00242  475 HFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP-SGVSNAGSKKRFQTVGSQFKE 553
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    617 SLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAy 696
Cdd:smart00242  554 QLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPP- 632
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|....*
gi 189083798    697 KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERD 741
Cdd:smart00242  633 WGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
79-729 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: 917.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIG-EMPPHIFAIADNCYFNMKRNSRDQCCIIS 157
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLAAISGQH--------SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEG 229
Cdd:cd00124    81 GESGAGKTETTKLVLKYLAALSGSGsskssssaSSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  230 AKIEQYLLEKSRVCRQALDERNYHVFYCML----EGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAM 305
Cdd:cd00124   161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLaglsDGAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  306 KVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTP 385
Cdd:cd00124   241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  386 LSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKNSrrsIGLLDIFGFENFAVNSFEQLCINFANEHLQQFF 465
Cdd:cd00124   321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTSF---IGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  466 VRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNH 545
Cdd:cd00124   398 NQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  546 ETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSsrnkfikqifqadvamgaetrkrsptlSSQFKRSLELLMRTL 625
Cdd:cd00124   478 KLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS---------------------------GSQFRSQLDALMDTL 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  626 GACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRgTC 705
Cdd:cd00124   531 NSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKA-AV 609
                         650       660
                  ....*....|....*....|....
gi 189083798  706 QRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd00124   610 LALLLLLKLDSSGYQLGKTKVFLR 633
Myosin_head pfam00063
Myosin head (motor domain);
67-729 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 850.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798    67 VEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMK 146
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   147 RNSRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW-----IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF 221
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   222 NKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANI 301
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   302 RSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGET 381
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKE--RNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRET 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   382 VSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPpsqdvKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEH 460
Cdd:pfam00063  319 VSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVK-----TIEKASfIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   461 LQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIP 540
Cdd:pfam00063  394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   541 PKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ------------ADVAMGAETRKRSP 608
Cdd:pfam00063  474 PRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPdyetaesaaaneSGKSTPKRTKKKRF 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   609 -TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRV 687
Cdd:pfam00063  554 iTVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRI 633
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 189083798   688 LLPGVKPAYKqGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:pfam00063  634 LAPKTWPKWK-GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
80-729 0e+00

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: 831.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14883     2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEK 239
Cdd:cd14883    82 SGAGKTETTKLILQYLCAVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  240 SRVCRQALDERNYHVFYCMLEGMSEDQ--KKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWE 317
Cdd:cd14883   162 SRITFQAPGERNYHVFYQLLAGAKHSKelKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQEG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  318 ISKLLAAILHLGNLQyeartFENLDACEVLFSPS----LATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALD 393
Cdd:cd14883   242 IFSVLSAILHLGNLT-----FEDIDGETGALTVEdkeiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARD 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  394 VRDAFVKGIYGRLFVWIVDKINAAIYKPPsqdvkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLE 473
Cdd:cd14883   317 NRDAMAKALYSRTFAWLVNHINSCTNPGQ-----KNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  474 QEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYI-PPKNNHETQFGIN 552
Cdd:cd14883   392 QEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEkPDRRRWKTEFGVK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  553 HFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF--QADVA------------MGAETRKRSPTLSSQFKRSL 618
Cdd:cd14883   472 HYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLAltglsislggdtTSRGTSKGKPTVGDTFKHQL 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  619 ELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQ 698
Cdd:cd14883   552 QSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHK 631
                         650       660       670
                  ....*....|....*....|....*....|.
gi 189083798  699 GDlRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14883   632 ET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
COG5022 COG5022
Myosin heavy chain [General function prediction only];
59-946 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 798.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   59 MHPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIA 138
Cdd:COG5022    60 IKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  139 DNCYFNMKRNSRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRNDNSSRFG 214
Cdd:COG5022   140 EEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVeissIEKQILATNPILEAFGNAKTVRNDNSSRFG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  215 KYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVD 294
Cdd:COG5022   220 KYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDD 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  295 SQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQY-EARTfenlDACEVLFSPSLATAASLLEVNPPDLMSCLTSR 373
Cdd:COG5022   300 AKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFkEDRN----GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKR 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  374 TLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDvknsrRSIGLLDIFGFENFAVNSFEQLC 453
Cdd:COG5022   376 QIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-----NFIGVLDIYGFEIFEKNSFEQLC 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  454 INFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANK-PMNIISLIDEESKFPKGTDTTMLHKLNSQH 532
Cdd:COG5022   451 INYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRL 530
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  533 KLNAN--YIPPKNNhETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqaDVAMGAETRKRSPTL 610
Cdd:COG5022   531 NKNSNpkFKKSRFR-DNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF--DDEENIESKGRFPTL 607
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  611 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLP 690
Cdd:COG5022   608 GSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSP 687
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  691 GVKPAY---KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKAITDRVILLQKVIRGFKDRSNFLKL 767
Cdd:COG5022   688 SKSWTGeytWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQA 767
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  768 KNAATLIQRhwRGHN----CRKNYGLMRLGFLRLQALHRSRKLHQQYRLARQRIIQFQARCRAYLVRK-----AFRHRlw 838
Cdd:COG5022   768 LKRIKKIQV--IQHGfrlrRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLReteevEFSLK-- 843
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  839 AVLTVQAYARGMIARR-----LHQRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAK------------------EEAER 895
Cdd:COG5022   844 AEVLIQKFGRSLKAKKrfsllKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVnleleseiielkkslssdLIENL 923
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798  896 KHQ-ERLAQLAREDAEREL-----KEKEAARRKKELLEQMERARHEPVNHSDMVDKM 946
Cdd:COG5022   924 EFKtELIARLKKLLNNIDLeegpsIEYVKLPELNKLHEVESKLKETSEEYEDLLKKS 980
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
81-729 0e+00

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: 775.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRY-RDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd01380     3 VLHNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAISGQHSW---IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYL 236
Cdd:cd01380    83 SGAGKTVSAKYAMRYFATVGGSSSGetqVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  237 LEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENW 316
Cdd:cd01380   163 LEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQM 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  317 EISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRD 396
Cdd:cd01380   243 EIFRILAAILHLGNVEIKAT--RNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  397 AFVKGIYGRLFVWIVDKINAAIYKPPSQDVKNsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEE 476
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASPVKEKQHS---FIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  477 YDLESIDWLHIEFTDNQDALDMIANKpMNIISLIDEESKFPKGTDTTMLHKLNSQH--KLNANYIPPKNNhETQFGINHF 554
Cdd:cd01380   398 YVKEEIEWSFIDFYDNQPCIDLIEGK-LGILDLLDEECRLPKGSDENWAQKLYNQHlkKPNKHFKKPRFS-NTAFIVKHF 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  555 AGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNkfikqifqadvamgaetrkRSPTLSSQFKRSLELLMRTLGACQPFFVR 634
Cdd:cd01380   476 ADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN-------------------RKKTVGSQFRDSLILLMETLNSTTPHYVR 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  635 CIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPayKQGDLRGTCQRMAEAVLG 714
Cdd:cd01380   537 CIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW--LRDDKKKTCENILENLIL 614
                         650
                  ....*....|....*
gi 189083798  715 THDDWQIGKTKIFLK 729
Cdd:cd01380   615 DPDKYQFGKTKIFFR 629
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
81-729 0e+00

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: 759.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGES 160
Cdd:cd01378     3 INENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYL 236
Cdd:cd01378    83 GAGKTEASKRIMQYIAAVSGGSESeverVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  237 LEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENW 316
Cdd:cd01378   163 LEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  317 EISKLLAAILHLGNLQYEartfENLDACEVLFSPS-LATAASLLEVNPPDLMSCLTSRTLITRGE---TVSTPLSREQAL 392
Cdd:cd01378   243 SIFRILAAILHLGNIQFA----EDEEGNAAISDTSvLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  393 DVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQdvknSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKL 472
Cdd:cd01378   319 YARDALAKAIYSRLFDWIVERINKSLAAKSGG----KKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKA 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  473 EQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFP-KGTDTTMLHKLNSQHKLNANYIPPKNNHE---TQ 548
Cdd:cd01378   395 EQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrrGE 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  549 FGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAmgAETRKRSPTLSSQFKRSLELLMRTLGAC 628
Cdd:cd01378   475 FRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD--LDSKKRPPTAGTKFKNSANALVETLMKK 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  629 QPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYkqgdlRGTCQRM 708
Cdd:cd01378   553 QPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAW-----DGTWQGG 627
                         650       660
                  ....*....|....*....|....*
gi 189083798  709 AEAVLGTH----DDWQIGKTKIFLK 729
Cdd:cd01378   628 VESILKDLnippEEYQMGKTKIFIR 652
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
79-729 0e+00

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: 736.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLS-IYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIIS 157
Cdd:cd14873     1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLAAISGQ---------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIE 228
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVISQQslelslkekTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  229 GAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVL 308
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  309 MFTDTENWEISKLLAAILHLGNLQyeartFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSR 388
Cdd:cd14873   241 QFSKEEVREVSRLLAGILHLGNIE-----FITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  389 EQALDVRDAFVKGIYGRLFVWIVDKINAAIYKppsqdvKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRH 468
Cdd:cd14873   316 QQAVDSRDSLAMALYARCFEWVIKKINSRIKG------KEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  469 VFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKpMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNhETQ 548
Cdd:cd14873   390 IFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKK-LGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVA-VNN 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  549 FGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVA------MGAETRKRSPTLSSQFKRSLELLM 622
Cdd:cd14873   468 FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSrnnqdtLKCGSKHRRPTVSSQFKDSLHSLM 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  623 RTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYkqgDLR 702
Cdd:cd14873   548 ATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE---DVR 624
                         650       660
                  ....*....|....*....|....*..
gi 189083798  703 GTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14873   625 GKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
79-729 0e+00

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: 729.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd01387     1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAIS-GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEGAKIEQYLL 237
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNqRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  238 EKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWE 317
Cdd:cd01387   160 EKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQDS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  318 ISKLLAAILHLGNLQYEARTFEN-LDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRD 396
Cdd:cd01387   240 IFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  397 AFVKGIYGRLFVWIVDKINAAIYKPpsqdvKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEE 476
Cdd:cd01387   320 AIAKALYALLFSWLVTRVNAIVYSG-----TQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEE 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  477 YDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNhETQFGINHFAG 556
Cdd:cd01387   395 YIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMP-LPEFTIKHYAG 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  557 IVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF-----QADVAM--GAE----TRK-RSPTLSSQFKRSLELLMRT 624
Cdd:cd01387   474 QVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFsshraQTDKAPprLGKgrfvTMKpRTPTVAARFQDSLLQLLEK 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  625 LGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGT 704
Cdd:cd01387   554 MERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVS 633
                         650       660
                  ....*....|....*....|....*.
gi 189083798  705 C-QRMAEAVlgTHDDWQIGKTKIFLK 729
Cdd:cd01387   634 LlSRLCTVT--PKDMYRLGATKVFLR 657
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
79-729 0e+00

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: 721.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd01377     1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSW----------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIE 228
Cdd:cd01377    81 ESGAGKTENTKKVIQYLASVAASSKKkkesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  229 GAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVL 308
Cdd:cd01377   161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  309 MFTDTENWEISKLLAAILHLGNLQYEARTfeNLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSR 388
Cdd:cd01377   241 GFSEEEKMSIFKIVAAILHLGNIKFKQRR--REEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  389 EQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVR 467
Cdd:cd01377   319 EQVVFSVGALAKALYERLFLWLVKRINKTL------DTKSKRQYfIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNH 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  468 HVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNANYIPPKNNH 545
Cdd:cd01377   393 HMFVLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHlGKSKNFKKPKPKK 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  546 -ETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAM---GAETRKRSP---TLSSQFKRSL 618
Cdd:cd01377   473 sEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESgggGGKKKKKGGsfrTVSQLHKEQL 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  619 ELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYkQ 698
Cdd:cd01377   553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-F 631
                         650       660       670
                  ....*....|....*....|....*....|.
gi 189083798  699 GDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd01377   632 DDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
81-729 0e+00

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: 718.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGES 160
Cdd:cd01385     3 LLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAIS--GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 238
Cdd:cd01385    83 GSGKTESTNFLLHHLTALSqkGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEI 318
Cdd:cd01385   163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  319 SKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAF 398
Cdd:cd01385   243 FSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAM 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  399 VKGIYGRLFVWIVDKINAAIYKPPSQDvKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYD 478
Cdd:cd01385   323 AKCLYSALFDWIVLRINHALLNKKDLE-EAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  479 LESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANY-IPPKNnhETQFGINHFAGI 557
Cdd:cd01385   402 KEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYeKPQVM--EPAFIIAHYAGK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  558 VYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQAD-VAM-------------------GAETR------------- 604
Cdd:cd01385   480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDpVAVfrwavlrafframaafreaGRRRAqrtaghsltlhdr 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  605 -----------KRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYP 673
Cdd:cd01385   560 ttksllhlhkkKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYS 639
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  674 IRYSFVEFVERYRVLLPGVKPAYKQgdlrgTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd01385   640 VRYTFQEFITQFQVLLPKGLISSKE-----DIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
79-729 0e+00

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: 711.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLS-IYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIIS 157
Cdd:cd01384     1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIE 233
Cdd:cd01384    81 GESGAGKTETTKMLMQYLAYMGGRAVTegrsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  234 QYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDT 313
Cdd:cd01384   161 TYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  314 ENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPS---LATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQ 390
Cdd:cd01384   241 EQDAIFRVVAAILHLGNIEFSKG--EEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  391 ALDVRDAFVKGIYGRLFVWIVDKINAAIykppSQDvKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVF 470
Cdd:cd01384   319 ATLSRDALAKTIYSRLFDWLVDKINRSI----GQD-PNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  471 KLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNhETQFG 550
Cdd:cd01384   394 KMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLS-RTDFT 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  551 INHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQP 630
Cdd:cd01384   473 IDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKFSSIGSRFKQQLQELMETLNTTEP 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  631 FFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAY--KQGDLRGTCQRM 708
Cdd:cd01384   553 HYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSddEKAACKKILEKA 632
                         650       660
                  ....*....|....*....|.
gi 189083798  709 AEavlgthDDWQIGKTKIFLK 729
Cdd:cd01384   633 GL------KGYQIGKTKVFLR 647
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
81-729 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 702.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGES 160
Cdd:cd01379     3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAIS-GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEK 239
Cdd:cd01379    83 GAGKTESANLLVQQLTVLGkANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  240 SRVCRQALDERNYHVFYCMLEGMSEDQK-KKLGLGQASDYNYLAMGNCITCEGRVDS---QEYANIRSAMKVLMFTDTEN 315
Cdd:cd01379   163 SRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFTKEEV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  316 WEISKLLAAILHLGNLQYE--ARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALD 393
Cdd:cd01379   243 DSVYSILAAILHIGDIEFTevESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEATD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  394 VRDAFVKGIYGRLFVWIVDKINAAIykPPSQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLE 473
Cdd:cd01379   323 ARDAMAKALYGRLFSWIVNRINSLL--KPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  474 QEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNnhETQFGINH 553
Cdd:cd01379   401 QQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYWRPKSN--ALSFGIHH 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  554 FAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQifqadvamgaetrkrspTLSSQFKRSLELLMRTLGACQPFFV 633
Cdd:cd01379   479 YAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-----------------TVATYFRYSLMDLLSKMVVGQPHFV 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  634 RCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLlpgvkpAYKQGDL----RGTCQRMA 709
Cdd:cd01379   542 RCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFL------AFKWNEEvvanRENCRLIL 615
                         650       660
                  ....*....|....*....|
gi 189083798  710 EAvLGThDDWQIGKTKIFLK 729
Cdd:cd01379   616 ER-LKL-DNWALGKTKVFLK 633
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
81-729 0e+00

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: 701.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGemPPHIFAIADNCYFNMKRNSRDQCCIISGES 160
Cdd:cd01383     3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLD--SPHVYAVADTAYREMMRDEINQSIIISGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKS 240
Cdd:cd01383    81 GAGKTETAKIAMQYLAALGGGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  241 RVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISK 320
Cdd:cd01383   161 RVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHIFQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  321 LLAAILHLGNLqyearTFENLDAC---EVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDA 397
Cdd:cd01383   241 MLAAVLWLGNI-----SFQVIDNEnhvEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  398 FVKGIYGRLFVWIVDKINAAIYKPPSQDvknsRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEY 477
Cdd:cd01383   316 LAKAIYASLFDWLVEQINKSLEVGKRRT----GRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEY 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  478 DLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYippKNNHETQFGINHFAGI 557
Cdd:cd01383   392 ELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF---KGERGGAFTIRHYAGE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  558 VYYETQGFLEKNRDTLHGDIIQLVHSSRNK----FIKQIFQADVAMGAETRKRSP-----TLSSQFKRSLELLMRTLGAC 628
Cdd:cd01383   469 VTYDTSGFLEKNRDLLHSDLIQLLSSCSCQlpqlFASKMLDASRKALPLTKASGSdsqkqSVATKFKGQLFKLMQRLENT 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  629 QPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPgvKPAYKQGDLRGTCQrm 708
Cdd:cd01383   549 TPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP--EDVSASQDPLSTSV-- 624
                         650       660
                  ....*....|....*....|....*
gi 189083798  709 aeAVLGTHDD----WQIGKTKIFLK 729
Cdd:cd01383   625 --AILQQFNIlpemYQVGYTKLFFR 647
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
79-726 0e+00

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: 644.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14872     1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 238
Cdd:cd14872    81 ESGAGKTEATKQCLSFFAEVAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLegMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEI 318
Cdd:cd14872   161 KSRVVYQIKGERNFHIFYQLL--ASPDPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADINNV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  319 SKLLAAILHLGNLQYEARTFENL-DACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRG-ETVSTPLSREQALDVRD 396
Cdd:cd14872   239 MSLIAAILKLGNIEFASGGGKSLvSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcDPTRIPLTPAQATDACD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  397 AFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEE 476
Cdd:cd14872   319 ALAKAAYSRLFDWLVKKINESMRPQKGAKTT----FIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  477 YDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIP-PKNNHETQFGINHFA 555
Cdd:cd14872   395 YQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYaEVRTSRTEFIVKHYA 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  556 GIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQadVAMGAETRKRsPTLSSQFKRSLELLMRTLGACQPFFVRC 635
Cdd:cd14872   475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP--PSEGDQKTSK-VTLGGQFRKQLSALMTALNATEPHYIRC 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  636 IKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQgDLRGTCQRMAEAVLGT 715
Cdd:cd14872   552 VKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVGP-DDRQRCDLLLKSLKQD 630
                         650
                  ....*....|.
gi 189083798  716 HDDWQIGKTKI 726
Cdd:cd14872   631 FSKVQVGKTRV 641
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
79-729 0e+00

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: 634.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQ-LLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKR----NSRDQC 153
Cdd:cd14890     1 ASLLHTLRLRYERDEIYTYVGPILISINPYKsIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  154 CIISGESGAGKTESTKLILQFLAAISGQHSWI-------------------EQQVLEATPILEAFGNAKTIRNDNSSRFG 214
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLARITSGFAQGasgegeaaseaieqtlgslEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  215 KYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLaMGNCITCEGRVD 294
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  295 SQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFsPSLATAASLLEVNPPDLMSCLTSRT 374
Cdd:cd14890   240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTL-QSLKLAAELLGVNEDALEKALLTRQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  375 LITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPpsQDVKNsrrSIGLLDIFGFENFAVNSFEQLCI 454
Cdd:cd14890   319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSP--DDKWG---FIGVLDIYGFEKFEWNTFEQLCI 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  455 NFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNI----ISLID------EES---------- 514
Cdd:cd14890   394 NYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNGKpgifITLDDcwrfkgEEAnkkfvsqlha 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  515 KFPKGTDTTMLHKLNSQHklnANYIPPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFikqifq 594
Cdd:cd14890   474 SFGRKSGSGGTRRGSSQH---PHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI------ 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  595 advamgaetrkRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPI 674
Cdd:cd14890   545 -----------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFAL 613
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798  675 RYSFVEFVERYRVLLPgvkpaykqgDLRGTCQRMAE--AVLG-THDDWQIGKTKIFLK 729
Cdd:cd14890   614 REEHDSFFYDFQVLLP---------TAENIEQLVAVlsKMLGlGKADWQIGSSKIFLK 662
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
81-729 0e+00

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: 632.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEM-PPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14897     3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAISG-QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 238
Cdd:cd14897    83 SGAGKTESTKYMIKHLMKLSPsDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNcITCEGRVDSQEYANIRSA-------MKVLMFT 311
Cdd:cd14897   163 KSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDN-RNRPVFNDSEELEYYRQMfhdltniMKLIGFS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  312 DTENWEISKLLAAILHLGNLQYEartfENLDACEVLFSPS--LATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSRE 389
Cdd:cd14897   242 EEDISVIFTILAAILHLTNIVFI----PDEDTDGVTVADEypLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  390 QALDVRDAFVKGIYGRLFVWIVDKINAAIYkpPSQDVKNSRR--SIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVR 467
Cdd:cd14897   318 QANDSRDALAKDLYSRLFGWIVGQINRNLW--PDKDFQIMTRgpSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  468 HVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHeT 547
Cdd:cd14897   396 YVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNR-V 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  548 QFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqadvamgaetrkrsptlSSQFKRSLELLMRTLGA 627
Cdd:cd14897   475 AFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF-----------------TSYFKRSLSDLMTKLNS 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  628 CQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAY--KQGDLRGTC 705
Cdd:cd14897   538 ADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRsdDLGKCQKIL 617
                         650       660
                  ....*....|....*....|....*
gi 189083798  706 Q-RMAEavlgthdDWQIGKTKIFLK 729
Cdd:cd14897   618 KtAGIK-------GYQFGKTKVFLK 635
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
79-729 0e+00

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: 628.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPY-QLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIIS 157
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYfDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLAAISGQHSW-IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYL 236
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSGAGpIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  237 LEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDynylamgncitcegrvDSQEYANIRSAMKVLMFTDTENW 316
Cdd:cd01382   161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD----------------DVGDFIRMDKAMKKIGLSDEEKL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  317 EISKLLAAILHLGNLQYEARTFENLDACEVLFS--PSLATAASLLEVNPPDLMSCLTSR-TLITRGETVST----PLSRE 389
Cdd:cd01382   225 DIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKseQSLEYAAELLGLDQDELRVSLTTRvMQTTRGGAKGTvikvPLKVE 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  390 QALDVRDAFVKGIYGRLFVWIVDKINAAIykpPSQdvkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHV 469
Cdd:cd01382   305 EANNARDALAKAIYSKLFDHIVNRINQCI---PFE---TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERI 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  470 FKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNN----H 545
Cdd:cd01382   379 LKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSklkiH 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  546 ET-----QFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLS-----SQFK 615
Cdd:cd01382   459 RNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKAGKLSfisvgNKFK 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  616 RSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPgvkPA 695
Cdd:cd01382   539 TQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLP---PK 615
                         650       660       670
                  ....*....|....*....|....*....|....
gi 189083798  696 YKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd01382   616 LARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
81-729 0e+00

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: 608.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNM----KRNSRDQCCII 156
Cdd:cd14889     3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIVI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  157 SGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEGAKIEQYL 236
Cdd:cd14889    83 SGESGAGKTESTKLLLRQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINEYL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  237 LEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGncITCEGRVDS--QEYANIRSAMKVLMFTDTE 314
Cdd:cd14889   162 LEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNG--AGCKREVQYwkKKYDEVCNAMDMVGFTEQE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  315 NWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPsLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDV 394
Cdd:cd14889   240 EVDMFTILAGILSLGNITFEMDDDEALKVENDSNGW-LKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  395 RDAFVKGIYGRLFVWIVDKINAAIykPPSQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQ 474
Cdd:cd14889   319 RDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  475 EEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYiPPKNNHETQFGINHF 554
Cdd:cd14889   397 KEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY-GKSRSKSPKFTVNHY 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  555 AGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAM---------------GAETRKRSPTLSSQFKRSLE 619
Cdd:cd14889   476 AGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRtgtlmpraklpqagsDNFNSTRKQSVGAQFKHSLG 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  620 LLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLpgVKPaykqg 699
Cdd:cd14889   556 VLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILL--CEP----- 628
                         650       660       670
                  ....*....|....*....|....*....|..
gi 189083798  700 DLRGTCQRMAeAVLGTHD--DWQIGKTKIFLK 729
Cdd:cd14889   629 ALPGTKQSCL-RILKATKlvGWKCGKTRLFFK 659
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
79-729 0e+00

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: 606.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLL-SIYSPEHIRQYTnKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIIS 157
Cdd:cd14888     1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIpGLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLA-AISG---QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK---------R 224
Cdd:cd14888    80 GESGAGKTESTKYVMKFLAcAGSEdikKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsgdR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  225 GAIEGAKIEQYLLEKSRVCRQALDERNYHVFY--CMLEGMSEDQK-------KKLGLGQASD--------------YNYL 281
Cdd:cd14888   160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYqlCAAAREAKNTGlsyeendEKLAKGADAKpisidmssfephlkFRYL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  282 AMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQyeartFENLDAC------EVLFSPSLATA 355
Cdd:cd14888   240 TKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNIL-----FENNEACsegavvSASCTDDLEKV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  356 ASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIykPPSQDvkNSRRSIGL 435
Cdd:cd14888   315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESI--GYSKD--NSLLFCGV 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  436 LDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESK 515
Cdd:cd14888   391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECF 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  516 FPKGTDTTMLHKLNSQHKLNANYIPPKNNhETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQA 595
Cdd:cd14888   471 VPGGKDQGLCNKLCQKHKGHKRFDVVKTD-PNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  596 DVAMGAE---TRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGY 672
Cdd:cd14888   550 YLRRGTDgntKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGY 629
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798  673 PIRYSFVEFVERYRVLLPgvkpayKQGDLrgtcqrmaeavlgTHDDWQIGKTKIFLK 729
Cdd:cd14888   630 PVRLSHAEFYNDYRILLN------GEGKK-------------QLSIWAVGKTLCFFK 667
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
79-729 0e+00

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: 605.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLL-SIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIIS 157
Cdd:cd14903     1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLpELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLAAI-SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYL 236
Cdd:cd14903    81 GESGAGKTETTKILMNHLATIaGGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  237 LEKSRVCRQALDERNYHVFYCMLEgmSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENW 316
Cdd:cd14903   161 LEKTRVISHERPERNYHIFYQLLA--SPDVEERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  317 EISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRD 396
Cdd:cd14903   239 VLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  397 AFVKGIYGRLFVWIVDKINAAIykppsQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEE 476
Cdd:cd14903   319 ALAKAIYSNVFDWLVATINASL-----GNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  477 YDLESIDWLHIEFTDNQDALDMIANKpMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIP-PKNNhETQFGINHFA 555
Cdd:cd14903   394 YEEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEfPRTS-RTQFTIKHYA 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  556 GIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAET---------RKRSPTLS-----SQFKRSLELL 621
Cdd:cd14903   472 GPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAAstslargarRRRGGALTtttvgTQFKDSLNEL 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  622 MRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPG-----VKPAY 696
Cdd:cd14903   552 MTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEgrntdVPVAE 631
                         650       660       670
                  ....*....|....*....|....*....|...
gi 189083798  697 KQGDLrgtcqrMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14903   632 RCEAL------MKKLKLESPEQYQMGLTRIYFQ 658
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
79-729 0e+00

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: 600.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQllSI---YS-PEHIRQYTNKKIGEM-PPHIFAIADNCYFNMKR----NS 149
Cdd:cd14892     1 APLLDVLRRRYERDAIYTFTADILISINPYK--SIpllYDvPGFDSQRKEEATASSpPPHVFSIAERAYRAMKGvgkgQG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  150 RDQCCIISGESGAGKTESTKLILQFLAAIS-------------GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKY 216
Cdd:cd14892    79 TPQSIVVSGESGAGKTEASKYIMKYLATASklakgastskgaaNAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  217 IDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQ 296
Cdd:cd14892   159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDAT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  297 EYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLI 376
Cdd:cd14892   239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  377 T-RGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAA-----IYKPPSQDVKNSRRSIGLLDIFGFENFAVNSFE 450
Cdd:cd14892   319 TaRGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqqtSGVTGGAASPTFSPFIGILDIFGFEIMPTNSFE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  451 QLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFP-KGTDTTMLHKLN 529
Cdd:cd14892   399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKrKTTDKQLLTIYH 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  530 SQH-KLNANYIPPKNNHEtQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRnkfikqifqadvamgaetrkrsp 608
Cdd:cd14892   479 QTHlDKHPHYAKPRFECD-EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS----------------------- 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  609 tlssQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVL 688
Cdd:cd14892   535 ----KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPL 610
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 189083798  689 L-PGVKPAYKQGDLRGTCQR-MAEAVLGTH---DDWQIGKTKIFLK 729
Cdd:cd14892   611 ArNKAGVAASPDACDATTARkKCEEIVARAlerENFQLGRTKVFLR 656
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
79-728 0e+00

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: 582.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQY----TNKKIGE--MPPHIFAIADNCYFNMKRNSR-- 150
Cdd:cd14901     1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgERRAAGErkLPPHVYAVADKAFRAMLFASRgq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  151 --DQCCIISGESGAGKTESTKLILQFLAAIS---------GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 219
Cdd:cd14901    81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqnaTERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  220 HFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNC-ITCEGRVDSQEY 298
Cdd:cd14901   161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCyDRRDGVDDSVQY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  299 ANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITR 378
Cdd:cd14901   241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  379 GETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAI-YKPPSqdvkNSRRSIGLLDIFGFENFAVNSFEQLCINFA 457
Cdd:cd14901   320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaYSEST----GASRFIGIVDIFGFEIFATNSLEQLCINFA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  458 NEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNAN 537
Cdd:cd14901   396 NEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHAS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  538 YIPPK-NNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIkqifqadvamgaetrkrSPTLSSQFKR 616
Cdd:cd14901   476 FSVSKlQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL-----------------SSTVVAKFKV 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  617 SLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVkpAY 696
Cdd:cd14901   539 QLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDG--AS 616
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 189083798  697 KQGDLRGTCQRMA------EAVLGTHDDWQIGKTKIFL 728
Cdd:cd14901   617 DTWKVNELAERLMsqlqhsELNIEHLPPFQVGKTKVFL 654
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
79-729 0e+00

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: 568.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLS-IYSPEHIRQYTNK--------KIGEMPPHIFAIADNCYFNMKRNS 149
Cdd:cd14907     1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  150 RDQCCIISGESGAGKTESTKLILQFLAAISGQHSW--------------------IEQQVLEATPILEAFGNAKTIRNDN 209
Cdd:cd14907    81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNseevltltssiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  210 SSRFGKYIDIHFNKR-GAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGL---GQASDYNYLAMGN 285
Cdd:cd14907   161 SSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  286 CITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPD 365
Cdd:cd14907   241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLLGIDEEE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  366 LMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQD---VKNSRRSIGLLDIFGFE 442
Cdd:cd14907   321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDqqlFQNKYLSIGLLDIFGFE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  443 NFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESI-DWL-HIEFTDNQDALDMIANKPMNIISLIDEESKFPKGT 520
Cdd:cd14907   401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLeDYLnQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLATGT 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  521 DTTMLHKLNSQHKLNANYIPPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQAD---- 596
Cdd:cd14907   481 DEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEdgsq 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  597 ---VAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYP 673
Cdd:cd14907   561 qqnQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYP 640
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  674 IRYSFVEFVERYRVLLpgvkpaykqgdlrgtcqrmaEAVLgthddwqIGKTKIFLK 729
Cdd:cd14907   641 YRKSYEDFYKQYSLLK--------------------KNVL-------FGKTKIFMK 669
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
81-729 1.32e-169

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: 535.51  E-value: 1.32e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGES 160
Cdd:cd14896     3 VLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGHS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAI-SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEGAKIEQYLLEK 239
Cdd:cd14896    83 GSGKTEAAKKIVQFLSSLyQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHYLLET 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  240 SRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEIS 319
Cdd:cd14896   162 SRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIW 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  320 KLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFV 399
Cdd:cd14896   242 AVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDARDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  400 KGIYGRLFVWIVDKINAAIYKPPSQDvknSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDL 479
Cdd:cd14896   322 KTLYSRLFTWLLKRINAWLAPPGEAE---SDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  480 ESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETqFGINHFAGIVY 559
Cdd:cd14896   399 ELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPV-FTVRHYAGTVT 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  560 YETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-ADVAMGAETRKrsPTLSSQFKRSLELLMRTLGACQPFFVRCIKP 638
Cdd:cd14896   478 YQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQeAEPQYGLGQGK--PTLASRFQQSLGDLTARLGRSHVYFIHCLNP 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  639 NEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYkqgDLRGTCQRMAEAVLGTHDD 718
Cdd:cd14896   556 NPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEAL---SDRERCGAILSQVLGAESP 632
                         650
                  ....*....|..
gi 189083798  719 -WQIGKTKIFLK 729
Cdd:cd14896   633 lYHLGATKVLLK 644
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
79-729 3.17e-165

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: 523.74  E-value: 3.17e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLL-SIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIIS 157
Cdd:cd14904     1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIdNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLAAISG--QHSWIEQqVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQY 235
Cdd:cd14904    81 GESGAGKTETTKIVMNHLASVAGgrKDKTIAK-VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  236 LLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMG-NCITCEGRVDSQEYANIRSAMKVLMFTDTE 314
Cdd:cd14904   160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  315 NWEISKLLAAILHLGNLQY-----EARTFENLDACEVLfSPSLATAASLLEvnppdlmSCLTSRTLITRGETVSTPLSRE 389
Cdd:cd14904   240 QRTLFKILSGVLHLGEVMFdksdeNGSRISNGSQLSQV-AKMLGLPTTRIE-------EALCNRSVVTRNESVTVPLAPV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  390 QALDVRDAFVKGIYGRLFVWIVDKINAAIykppSQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHV 469
Cdd:cd14904   312 EAEENRDALAKAIYSKLFDWMVVKINAAI----STDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  470 FKLEQEEYDLESIDWLHIEFTDNQDALDMIANKpMNIISLIDEESKFPKGTDTTMLHKL--NSQHKLNANYIP-PKNNhE 546
Cdd:cd14904   388 FKTVEEEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIrtNHQTKKDNESIDfPKVK-R 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  547 TQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-----ADVAMGAETRKRS--PTLSSQFKRSLE 619
Cdd:cd14904   466 TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGsseapSETKEGKSGKGTKapKSLGSQFKTSLS 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  620 LLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPgvkPAYKQG 699
Cdd:cd14904   546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP---PSMHSK 622
                         650       660       670
                  ....*....|....*....|....*....|..
gi 189083798  700 DLRGTCQRMAEAVlGTHD--DWQIGKTKIFLK 729
Cdd:cd14904   623 DVRRTCSVFMTAI-GRKSplEYQIGKSLIYFK 653
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
79-729 6.58e-159

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: 507.14  E-value: 6.58e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTN------------KKIGempPHIFAIADNCYFNMK 146
Cdd:cd14908     1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqgiespQALG---PHVFAIADRSYRQMM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  147 RNSR-DQCCIISGESGAGKTESTKLILQFLAAI------------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRF 213
Cdd:cd14908    78 SEIRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapnegeELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  214 GKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKK--------LGLGQASDYNYLAMGN 285
Cdd:cd14908   158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKyefhdgitGGLQLPNEFHYTGQGG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  286 CITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENL-DACEVLFSPSLATAASLLEVNPP 364
Cdd:cd14908   238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAaEIAEEGNEKCLARVAKLLGVDVD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  365 DLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVknsRRSIGLLDIFGFENF 444
Cdd:cd14908   318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDI---RSSVGVLDIFGFECF 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  445 AVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFP-KGTDTt 523
Cdd:cd14908   395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGiRGSDA- 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  524 mlhklNSQHKLNANYIPPKNNHETQ---------------FGINHFAGIVYYETQ-GFLEKNRDTLhgdiiqlvhssrNK 587
Cdd:cd14908   474 -----NYASRLYETYLPEKNQTHSEntrfeatsiqktkliFAVRHFAGQVQYTVEtTFCEKNKDEI------------PL 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  588 FIKQIFQAdvamgaetrkrsptlSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRI 667
Cdd:cd14908   537 TADSLFES---------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  668 RRAGYPIRYSFVEFVERYRVLLPG----VKPAYKQG-DLRGTCQRMAEAVLGTH--------------DDWQIGKTKIFL 728
Cdd:cd14908   602 ARSGYPVRLPHKDFFKRYRMLLPLipevVLSWSMERlDPQKLCVKKMCKDLVKGvlspamvsmknipeDTMQLGKSKVFM 681

                  .
gi 189083798  729 K 729
Cdd:cd14908   682 R 682
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
79-729 8.72e-159

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: 506.47  E-value: 8.72e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14920     1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSW---------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEG 229
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  230 AKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNcITCEGRVDSQEYANIRSAMKVLM 309
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  310 FTDTENWEISKLLAAILHLGNLQYeaRTFENLDACEVLFSPSLATAASLLEVNPPDLM-SCLTSRTLITRgETVSTPLSR 388
Cdd:cd14920   240 FSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQKLCHLLGMNVMEFTrAILTPRIKVGR-DYVQKAQTK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  389 EQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRH 468
Cdd:cd14920   317 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS----FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  469 VFKLEQEEYDLESIDWLHIEF-TDNQDALDMI---ANKPmNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKN- 543
Cdd:cd14920   393 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIerpANPP-GVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQl 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADV----------------AMGAETRK-R 606
Cdd:cd14920   472 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtgmtetafGSAYKTKKgM 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  607 SPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYR 686
Cdd:cd14920   552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 189083798  687 VLLPGVKP-AYKQGdlRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14920   632 ILTPNAIPkGFMDG--KQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
79-729 9.67e-159

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: 506.05  E-value: 9.67e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14929     1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISG------QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 232
Cdd:cd14929    81 ESGAGKTVNTKHIIQYFATIAAmieskkKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  233 EQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGnCITCEGRVDSQEYANIRSAMKVLMFTD 312
Cdd:cd14929   161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCG-AVAVESLDDAEELLATEQAMDILGFLP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  313 TENWEISKLLAAILHLGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQAL 392
Cdd:cd14929   240 DEKYGCYKLTGAIMHFGNMKFKQKPRE--EQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  393 DVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRR-SIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFK 471
Cdd:cd14929   318 YAVGALSKSIYERMFKWLVARINRVL------DAKLSRQfFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  472 LEQEEYDLESIDWLHIEF-TDNQDALDMIaNKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYI----PPKNNHE 546
Cdd:cd14929   392 LEQEEYRKEGIDWVSIDFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFqkpkPDKKKFE 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  547 TQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVA------MGAETRKRSP---TLSSQFKRS 617
Cdd:cd14929   471 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIStdsaiqFGEKKRKKGAsfqTVASLHKEN 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  618 LELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYK 697
Cdd:cd14929   551 LNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSK 630
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 189083798  698 QGDLRgtcqRMAEAVLGT----HDDWQIGKTKIFLK 729
Cdd:cd14929   631 FVSSR----KAAEELLGSleidHTQYRFGITKVFFK 662
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
79-729 4.56e-158

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: 504.51  E-value: 4.56e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14911     1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHS------------------WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIH 220
Cdd:cd14911    81 ESGAGKTENTKKVIQFLAYVAASKPkgsgavphpavnpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  221 FNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNcITCEGRVDSQEYAN 300
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGS-LPVPGVDDYAEFQA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  301 IRSAMKVLMFTDTENWEISKLLAAILHLGNLQYeaRTFENLDACEVLFSPSLATAASLLEVNPPDLMSC-LTSRTLITRg 379
Cdd:cd14911   240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF--RQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIKVGR- 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  380 ETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANE 459
Cdd:cd14911   317 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAS----FIGILDMAGFEIFELNSFEQLCINYTNE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  460 HLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIaNKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANY 538
Cdd:cd14911   393 KLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKF 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  539 IPPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ------------ADVAMGAETRK- 605
Cdd:cd14911   472 MKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKdaeivgmaqqalTDTQFGARTRKg 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  606 RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERY 685
Cdd:cd14911   552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 189083798  686 RVLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14911   632 ELLTPNVIP---KGfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
79-729 1.60e-157

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: 502.83  E-value: 1.60e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14909     1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAI---------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEG 229
Cdd:cd14909    81 ESGAGKTENTKKVIAYFATVgaskktdeaAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  230 AKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQ-ASDYNYLAMGNcITCEGRVDSQEYANIRSAMKVL 308
Cdd:cd14909   161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDnIYDYYIVSQGK-VTVPNVDDGEEFSLTDQAFDIL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  309 MFTDTENWEISKLLAAILHLGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSR 388
Cdd:cd14909   240 GFTKQEKEDVYRITAAVMHMGGMKFKQRGRE--EQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  389 EQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVR 467
Cdd:cd14909   318 QQVTNSIGALCKGVFDRLFKWLVKKCNETL------DTQQKRQHfIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNH 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  468 HVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIaNKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNANYIPPK--- 542
Cdd:cd14909   392 HMFVLEQEEYKREGIDWAFIDFgMDLLACIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKppk 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  543 -NNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF-----QADVAMGAETRKRS-----PTLS 611
Cdd:cd14909   471 pGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFadhagQSGGGEQAKGGRGKkgggfATVS 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  612 SQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPg 691
Cdd:cd14909   551 SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP- 629
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 189083798  692 vKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14909   630 -AGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
79-729 4.27e-157

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: 501.79  E-value: 4.27e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14927     1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISG---------------QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 223
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaqflatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  224 RGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMS-EDQKKKLGLGQASDYNYLAMGnCITCEGRVDSQEYANIR 302
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLVSMNPYDYHFCSQG-VTTVDNMDDGEELMATD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  303 SAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCL------TSRTLI 376
Cdd:cd14927   240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQRE--EQAEADGTESADKAAYLMGVSSADLLKGLlhprvkVGNEYV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  377 TRGETVstplsrEQALDVRDAFVKGIYGRLFVWIVDKINAAIY-KPPSQDVknsrrsIGLLDIFGFENFAVNSFEQLCIN 455
Cdd:cd14927   318 TKGQSV------EQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQFF------IGVLDIAGFEIFEFNSFEQLCIN 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  456 FANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIaNKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-K 533
Cdd:cd14927   386 FTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDASFKAKLYDNHlG 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  534 LNANYIPP----KNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------ADVAMGA 601
Cdd:cd14927   465 KSPNFQKPrpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEnyvgsdstEDPKSGV 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  602 ETRKRSP----TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYS 677
Cdd:cd14927   545 KEKRKKAasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 624
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 189083798  678 FVEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14927   625 YADFKQRYRILNPSAIPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
79-729 5.90e-156

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: 497.64  E-value: 5.90e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYR--DHLIYTYTGSILVAVNPyqLLSIYSPeHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNS---RDQC 153
Cdd:cd14891     1 AGILHNLEERSKldNQRPYTFMANVLIAVNP--LRRLPEP-DKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  154 CIISGESGAGKTESTKLILQFL-------AAISGQHSW------------IEQQVLEATPILEAFGNAKTIRNDNSSRFG 214
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFLttravggKKASGQDIEqsskkrklsvtsLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  215 KYIDIHFNKRG-AIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRV 293
Cdd:cd14891   158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  294 DSQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFS--PSLATAASLLEVNPPDLMSCLT 371
Cdd:cd14891   238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESdkEALATAAELLGVDEEALEKVIT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  372 SRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPsqdvkNSRRSIGLLDIFGFENFA-VNSFE 450
Cdd:cd14891   318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDP-----DPLPYIGVLDIFGFESFEtKNDFE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  451 QLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNS 530
Cdd:cd14891   393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHK 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  531 QHKLNANYIPP--KNNHETqFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSrNKFIKQifqadvamgaetrkrsp 608
Cdd:cd14891   473 THKRHPCFPRPhpKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKFSDQ----------------- 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  609 tlssqfkrsLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVL 688
Cdd:cd14891   534 ---------MQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPV 604
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 189083798  689 LP-GVKPAYKQGDlrgtcQRMAEAVLGTH----DDWQIGKTKIFLK 729
Cdd:cd14891   605 LPpSVTRLFAEND-----RTLTQAILWAFrvpsDAYRLGRTRVFFR 645
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
80-729 6.79e-156

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: 498.42  E-value: 6.79e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14913     2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAI-----------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIE 228
Cdd:cd14913    82 SGAGKTVNTKRVIQYFATIaatgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  229 GAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLG-QASDYNYLAMGNcITCEGRVDSQEYANIRSAMKV 307
Cdd:cd14913   162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGE-ILVASIDDAEELLATDSAIDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  308 LMFTDTENWEISKLLAAILHLGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCL------TSRTLITR 378
Cdd:cd14913   241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKTAYLMGLNSSDLLKALcfprvkVGNEYVTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  379 GETVstplsrEQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFA 457
Cdd:cd14913   316 GQTV------DQVHHAVNALSKSVYEKLFLWMVTRINQQL------DTKLPRQHfIGVLDIAGFEIFEYNSLEQLCINFT 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  458 NEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNA 536
Cdd:cd14913   384 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSN 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  537 NYIPPKN---NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF------QADVAMGAETRKRS 607
Cdd:cd14913   464 NFQKPKVvkgRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfataDADSGKKKVAKKKG 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  608 P---TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVER 684
Cdd:cd14913   544 SsfqTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQR 623
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 189083798  685 YRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14913   624 YRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
81-700 2.38e-155

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: 495.21  E-value: 2.38e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLL-SIYSPEHIRQY-----------TNKKIGEMPPHIFAIADNCYFNMKR- 147
Cdd:cd14900     3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLpGLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMMLg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  148 -NSR--DQCCIISGESGAGKTESTKLILQFLA-----------AISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRF 213
Cdd:cd14900    83 lNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  214 GKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKklglgqasdynylamgncitcegrv 293
Cdd:cd14900   163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  294 dSQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVL-FSPS----LATAASLLEVNPPDLMS 368
Cdd:cd14900   218 -RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSdLAPSsiwsRDAAATLLSVDATKLEK 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  369 CLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKNSRRSIGLLDIFGFENFAVNS 448
Cdd:cd14900   297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHFIGILDIFGFEVFPKNS 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  449 FEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKL 528
Cdd:cd14900   377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLASKL 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  529 ----NSQHKLNANYIppkNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLvhssrnkfikqiFQAdvamgaetr 604
Cdd:cd14900   457 yracGSHPRFSASRI---QRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDL------------FVY--------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  605 krsptlSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVER 684
Cdd:cd14900   513 ------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVAR 586
                         650
                  ....*....|....*...
gi 189083798  685 YRVLLPGVKP--AYKQGD 700
Cdd:cd14900   587 YFSLARAKNRllAKKQGT 604
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
79-713 6.32e-154

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: 494.80  E-value: 6.32e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQ-LLSIYSPEHIRQY--------TNKKIGEMPPHIFAIADNCYFNMKRNS 149
Cdd:cd14902     1 AALLQALSERFEHDQIYTSIGDILVALNPLKpLPDLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  150 R-DQCCIISGESGAGKTESTKLILQFLAAISGQHSWIEQ----------QVLEATPILEAFGNAKTIRNDNSSRFGKYID 218
Cdd:cd14902    81 RrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQegsdaveigkRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  219 IHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEY 298
Cdd:cd14902   161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKRAVADKY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  299 ANiRSAMKVLMFTDT-----ENWEISKLLAAILHLGNLQYEArTFENLDACEVLFSPS--LATAASLLEVNPPDLMSCLT 371
Cdd:cd14902   241 AQ-LYVETVRAFEDTgvgelERLDIFKILAALLHLGNVNFTA-ENGQEDATAVTAASRfhLAKCAELMGVDVDKLETLLS 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  372 SRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIV----DKINAAIYKPPSQDVKNSRRSIGLLDIFGFENFAVN 447
Cdd:cd14902   319 SREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVrrlsDEINYFDSAVSISDEDEELATIGILDIFGFESLNRN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  448 SFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHK 527
Cdd:cd14902   399 GFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTK 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  528 LNSQHklnanyippknNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQAD--VAMGAETRK 605
Cdd:cd14902   479 FYRYH-----------GGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADEnrDSPGADNGA 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  606 ---------RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRY 676
Cdd:cd14902   548 agrrrysmlRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRL 627
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 189083798  677 SFVEFVERYRVLLP-------GVKPAYKQGDLRGTCQRMAEAVL 713
Cdd:cd14902   628 AHASFIELFSGFKCflstrdrAAKMNNHDLAQALVTVLMDRVLL 671
PTZ00014 PTZ00014
myosin-A; Provisional
73-781 4.75e-153

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 496.09  E-value: 4.75e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   73 LGDL---NEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQY-TNKKIGEMPPHIFAIADNCYFNMKRN 148
Cdd:PTZ00014  101 IGLLphtNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGV 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  149 SRDQCCIISGESGAGKTESTKLILQFLAAISGQH--SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGA 226
Cdd:PTZ00014  181 KKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNmdLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  227 IEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAmGNCITCEGRVDSQEYANIRSAMK 306
Cdd:PTZ00014  261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEEVMESFD 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  307 VLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLAT---AASLLEVNPPDLMSCLTSRTLITRGETVS 383
Cdd:PTZ00014  340 SMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLEVfneACELLFLDYESLKKELTVKVTYAGNQKIE 419
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  384 TPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIyKPPsqdvKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQ 463
Cdd:PTZ00014  420 GPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATI-EPP----GGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  464 FFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKN 543
Cdd:PTZ00014  495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSpTLSSQFKRSLELLMR 623
Cdd:PTZ00014  575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQ-LIGSQFLNQLDSLMS 653
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  624 TLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVL-LPGVKPayKQGDLR 702
Cdd:PTZ00014  654 LINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAVSND--SSLDPK 731
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  703 GTCQRMAEAVLGTHDDWQIGKTKIFLK-DHHDMLLEVERDK--AITDRVILLQKVIRGFKDRSNFLKLKNAATLIQRHWR 779
Cdd:PTZ00014  732 EKAEKLLERSGLPKDSYAIGKTMVFLKkDAAKELTQIQREKlaAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLR 811

                  ..
gi 189083798  780 GH 781
Cdd:PTZ00014  812 RH 813
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
79-729 1.24e-148

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: 477.60  E-value: 1.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14934     1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAIS--------GQHSwIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGA 230
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGgtgkqssdGKGS-LEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  231 KIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGL-GQASDYNYLAMGnCITCEGRVDSQEYANIRSAMKVLM 309
Cdd:cd14934   160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  310 FTDTENWEISKLLAAILHLGNLQYEARTFE---NLDACEVLfspslATAASLLEVNPPDLMSCLTSRTLITRGETVSTPL 386
Cdd:cd14934   239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREeqaEVDTTEVA-----DKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  387 SREQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHLQQFF 465
Cdd:cd14934   314 NMEQCNNSIGALGKAVYDKMFKWLVVRINKTL------DTKMQRQFfIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  466 VRHVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIaNKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNANYIPPKN 543
Cdd:cd14934   388 NHHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLL-EKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKG 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 NH----ETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAM-GAETRKRSP---TLSSQFK 615
Cdd:cd14934   467 GKgkgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPaGSKKQKRGSsfmTVSNFYR 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  616 RSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPa 695
Cdd:cd14934   547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIP- 625
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 189083798  696 ykQGDLRGtcQRMAEAVLGTHD----DWQIGKTKIFLK 729
Cdd:cd14934   626 --QGFVDN--KKASELLLGSIDldvnEYKIGHTKVFFR 659
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
79-729 1.09e-147

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: 475.67  E-value: 1.09e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14932     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQ-------------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRG 225
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVASSfktkkdqssialsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  226 AIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNcITCEGRVDSQEYANIRSAM 305
Cdd:cd14932   161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-VTIPGQQDKELFAETMEAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  306 KVLMFTDTENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTP 385
Cdd:cd14932   240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKE--RNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  386 LSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFF 465
Cdd:cd14932   318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGAS----FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  466 VRHVFKLEQEEYDLESIDWLHIEF-TDNQDALDMI--ANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPK 542
Cdd:cd14932   394 NHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIekPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPK 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  543 N-NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGA-ETRK- 605
Cdd:cd14932   474 KlKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKdvdrivgldkvagmGESLHGAfKTRKg 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  606 RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERY 685
Cdd:cd14932   554 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 189083798  686 RVLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14932   634 EILTPNAIP---KGfmDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
79-728 1.35e-146

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: 474.08  E-value: 1.35e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQ-LLSIYSPEHIRQYTN-KKIGEMPPHIFAIADNCYFNMKRNSRDQCCII 156
Cdd:cd14906     1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKdISSIYSNLILNEYKDiNQNKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  157 SGESGAGKTESTKLILQFLAAISGQHSW-----------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKR- 224
Cdd:cd14906    81 SGESGSGKTEASKTILQYLINTSSSNQQqnnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  225 GAIEGAKIEQYLLEKSRVC-RQALDERNYHVFYCMLEGMSEDQKKKLGL-GQASDYNYL-------------AMGNCITC 289
Cdd:cd14906   161 GKIDGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLdarddvissfksqSSNKNSNH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  290 EGRVDSQE-YANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEA-RTFENLDACEVLFSPSLATAASLLEVNPPDLM 367
Cdd:cd14906   241 NNKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdSDFSKYAYQKDKVTASLESVSKLLGYIESVFK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  368 SCLTSRTLIT--RGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAA-IYKPPSQDV-----KNSRRSIGLLDIF 439
Cdd:cd14906   321 QALLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDLaggsnKKNNLFIGVLDIF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  440 GFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKG 519
Cdd:cd14906   401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  520 TDTTMLHKLNSQ-HKLNANYIppKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVA 598
Cdd:cd14906   481 SEQSLLEKYNKQyHNTNQYYQ--RTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQIT 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  599 MGAETRKR---SPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIR 675
Cdd:cd14906   559 STTNTTKKqtqSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYR 638
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  676 YSFVEFVERYRVLLPGVKPAYKQGDLRGT--CQRMAEAVLGTHDD---------------------WQIGKTKIFL 728
Cdd:cd14906   639 RDFNQFFSRYKCIVDMYNRKNNNNPKLASqlILQNIQSKLKTMGIsnnkkknnsnsnsnttndkplFQIGKTKIFI 714
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
88-729 1.04e-144

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: 466.00  E-value: 1.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   88 RYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTN-KKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGESGAGKTE 166
Cdd:cd14876    10 RYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGKTE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  167 STKLILQFLAAISGQH--SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCR 244
Cdd:cd14876    90 ATKQIMRYFASAKSGNmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  245 QALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAmGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAA 324
Cdd:cd14876   170 QDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLTEEQIDTVFSIVSG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  325 ILHLGNLQYEARTFENLDACEVLFSPSLA---TAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKG 401
Cdd:cd14876   249 VLLLGNVKITGKTEQGVDDAAAISNESLEvfkEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKA 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  402 IYGRLFVWIVDKINAAIyKPPSqdvkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLES 481
Cdd:cd14876   329 MYDKLFLWIIRNLNSTI-EPPG----GFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEG 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  482 IDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGINHFAGIVYYE 561
Cdd:cd14876   404 IPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTIGDIQYN 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  562 TQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEF 641
Cdd:cd14876   484 AEGFLFKNKDVLRAELVEVVQASTNPVVKALF-EGVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNET 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  642 KKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAyKQGDLRGTCQRMAEAVLGTHDDWQI 721
Cdd:cd14876   563 KKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIAND-KSLDPKVAALKLLESSGLSEDEYAI 641

                  ....*...
gi 189083798  722 GKTKIFLK 729
Cdd:cd14876   642 GKTMVFLK 649
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
88-729 1.68e-144

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: 467.51  E-value: 1.68e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   88 RYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKR-------NSRDQCCIISGES 160
Cdd:cd14895    10 RYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGWTALPPHVFSIAEGAYRSLRRrlhepgaSKKNQTILVSGES 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAIS----------GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF-----NKRG 225
Cdd:cd14895    90 GAGKTETTKFIMNYLAESSkhttatssskRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRMFFeghelDTSL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  226 AIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLG--QASDYNYLAMGNCITCEGRV-DSQEYANIR 302
Cdd:cd14895   170 RMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQCYQRNDGVrDDKQFQLVL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  303 SAMKVLMFTDTENWEISKLLAAILHLGNLQYEART-----FENLDACEVLF----SPS-------LATAASLLEVNPPDL 366
Cdd:cd14895   250 QSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSedegeEDNGAASAPCRlasaSPSsltvqqhLDIVSKLFAVDQDEL 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  367 MSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAI------YKPPSQDVKNSRRSIGLLDIFG 440
Cdd:cd14895   330 VSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfaLNPNKAANKDTTPCIAVLDIFG 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  441 FENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGT 520
Cdd:cd14895   410 FEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFSLLDEECVVPKGS 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  521 DTTMLHKLNSQHKLNANYIPPKNNH-ETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-ADVA 598
Cdd:cd14895   490 DAGFARKLYQRLQEHSNFSASRTDQaDVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEfFKAS 569
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  599 MGAE-------TRKRSPTLS-----SQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIR 666
Cdd:cd14895   570 ESAElslgqpkLRRRSSVLSsvgigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVE 649
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083798  667 IRRAGYPIRYSFVEFVERYRVLLpgvkPAYKQGDLRGTCQRMAEAVLGThddwQIGKTKIFLK 729
Cdd:cd14895   650 IMRQSYPVRMKHADFVKQYRLLV----AAKNASDATASALIETLKVDHA----ELGKTRVFLR 704
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
79-729 2.59e-143

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: 462.95  E-value: 2.59e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14921     1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSW---------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEG 229
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAVVASSHKGkkdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  230 AKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNcITCEGRVDSQEYANIRSAMKVLM 309
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGF-VPIPAAQDDEMFQETLEAMSIMG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  310 FTDTENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSC-LTSRTLITRgETVSTPLSR 388
Cdd:cd14921   240 FSEEEQLSILKVVSSVLQLGNIVFKKE--RNTDQASMPDNTAAQKVCHLMGINVTDFTRSiLTPRIKVGR-DVVQKAQTK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  389 EQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRH 468
Cdd:cd14921   317 EQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGAS----FLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  469 VFKLEQEEYDLESIDWLHIEF-TDNQDALDMI--ANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKN-N 544
Cdd:cd14921   393 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIerPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQlK 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  545 HETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDV-------AMGAETRKRSPTLSSQ---- 613
Cdd:cd14921   473 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK-DVdrivgldQMAKMTESSLPSASKTkkgm 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  614 -------FKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYR 686
Cdd:cd14921   552 frtvgqlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 189083798  687 VLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14921   632 ILAANAIP---KGfmDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
80-729 1.20e-142

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: 461.11  E-value: 1.20e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14917     2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAIS--GQHS---------WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIE 228
Cdd:cd14917    82 SGAGKTVNTKRVIQYFAVIAaiGDRSkkdqtpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  229 GAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGL-GQASDYNYLAMGNcITCEGRVDSQEYANIRSAMKV 307
Cdd:cd14917   162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGE-TTVASIDDAEELMATDNAFDV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  308 LMFTDTENWEISKLLAAILHLGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLS 387
Cdd:cd14917   241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQRE--EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  388 REQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHLQQFFV 466
Cdd:cd14917   319 VQQVIYATGALAKAVYEKMFNWMVTRINATL------ETKQPRQYfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  467 RHVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIaNKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNANYIPPKN- 543
Cdd:cd14917   393 HHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNi 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 --NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF------QADVAMGAETRKRSP---TLSS 612
Cdd:cd14917   472 kgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFanyagaDAPIEKGKGKAKKGSsfqTVSA 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  613 QFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGV 692
Cdd:cd14917   552 LHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 631
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 189083798  693 KPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14917   632 IPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
76-728 1.28e-142

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: 460.09  E-value: 1.28e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   76 LNEAGILRNLLIRYRDHLIYTYTGS-ILVAVNPYQLLSIYSPEHIRQY-------TNKKIGEMPPHIFAIADNCYFNMKR 147
Cdd:cd14879     1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  148 NSRDQCCIISGESGAGKTESTKLILQ---FLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKR 224
Cdd:cd14879    81 RSEDQAVVFLGETGSGKSESRRLLLRqllRLSSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  225 GAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRV---DSQEYANI 301
Cdd:cd14879   161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGCHPLPLGPgsdDAEGFQEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  302 RSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGET 381
Cdd:cd14879   241 KTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVRKEL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  382 VSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIyKPPSQDVKNsrrSIGLLDIFGFENFA---VNSFEQLCINFAN 458
Cdd:cd14879   321 CTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKL-CAPEDDFAT---FISLLDFPGFQNRSstgGNSLDQFCVNFAN 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  459 EHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESK-FPKGTDTTMLHKLNSQHKLNAN 537
Cdd:cd14879   397 ERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTRrMPKKTDEQMLEALRKRFGNHSS 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  538 YI----PPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVhssrnkfikqifqadvamgaetrkRSPTlssQ 613
Cdd:cd14879   477 FIavgnFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL------------------------RGAT---Q 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  614 FKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGvk 693
Cdd:cd14879   530 LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRG-- 607
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 189083798  694 paykqGDLRGTCQRMAEAVLGTHDDWQIGKTKIFL 728
Cdd:cd14879   608 -----SAAERIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
80-729 2.76e-141

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: 457.27  E-value: 2.76e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14918     2 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLA--AISGQ---------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIE 228
Cdd:cd14918    82 SGAGKTVNTKRVIQYFAtiAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  229 GAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLG-QASDYNYLAMGNcITCEGRVDSQEYANIRSAMKV 307
Cdd:cd14918   162 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  308 LMFTDTENWEISKLLAAILHLGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLITRGETVST 384
Cdd:cd14918   241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  385 PLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHLQQ 463
Cdd:cd14918   316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL------DTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  464 FFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNANYIPP- 541
Cdd:cd14918   390 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPk 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  542 --KNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF------QADVAMGAETRKRSP---TL 610
Cdd:cd14918   470 vvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFstyasaEADSGAKKGAKKKGSsfqTV 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  611 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLP 690
Cdd:cd14918   550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 189083798  691 GVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14918   630 SAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
92-729 3.21e-141

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: 456.96  E-value: 3.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   92 HLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEM-PPHIFAIADNCYFNMK-RNSRDQCCIISGESGAGKTESTK 169
Cdd:cd14875    15 HQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIFvQGLGNQSVVISGESGSGKTENAK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  170 LILQFLAAISGQHS------WIEQQVLE----ATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK-RGAIEGAKIEQYLLE 238
Cdd:cd14875    95 MLIAYLGQLSYMHSsntsqrSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPtSGVMVGGQTVTYLLE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLG-LGQASDYNYLAMGNCIT---CEGRV--DSQEYANIRSAMKVLMFTD 312
Cdd:cd14875   175 KSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGgLKTAQDYKCLNGGNTFVrrgVDGKTldDAHEFQNVRHALSMIGVEL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  313 TENWEISKLLAAILHLGNLQYEArtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTlitRGETVSTPLSREQAL 392
Cdd:cd14875   255 ETQNSIFRVLASILHLMEVEFES---DQNDKAQIADETPFLTACRLLQLDPAKLRECFLVKS---KTSLVTILANKTEAE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  393 DVRDAFVKGIYGRLFVWIVDKINAAIYkpPSQDVkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKL 472
Cdd:cd14875   329 GFRNAFCKAIYVGLFDRLVEFVNASIT--PQGDC-SGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFIN 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  473 EQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANY-IPPKNNHETQFGI 551
Cdd:cd14875   406 DEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYfVLPKSTIPNQFGV 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  552 NHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGaetrKRSPTLSSQFKRSLELLMRTLGACQPF 631
Cdd:cd14875   486 NHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA----RRKQTVAIRFQRQLTDLRTELESTETQ 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  632 FVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLP-GVKPAYKQGDLRGTCQRMAE 710
Cdd:cd14875   562 FIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPrSTASLFKQEKYSEAAKDFLA 641
                         650       660
                  ....*....|....*....|....
gi 189083798  711 AVLGTHdDWQ-----IGKTKIFLK 729
Cdd:cd14875   642 YYQRLY-GWAkpnyaVGKTKVFLR 664
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
80-729 4.31e-141

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: 456.89  E-value: 4.31e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14912     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLA--AISGQ-----------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGA 226
Cdd:cd14912    82 SGAGKTVNTKRVIQYFAtiAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  227 IEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLG-QASDYNYLAMGNcITCEGRVDSQEYANIRSAM 305
Cdd:cd14912   162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGE-ISVASIDDQEELMATDSAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  306 KVLMFTDTENWEISKLLAAILHLGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLITRGETV 382
Cdd:cd14912   241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQaepDGTEVA-----DKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  383 STPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHL 461
Cdd:cd14912   316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL------DTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  462 QQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNANYIP 540
Cdd:cd14912   390 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQK 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  541 P---KNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-ADVAMG---------AETRKRS 607
Cdd:cd14912   470 PkvvKGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgAQTAEGasagggakkGGKKKGS 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  608 P--TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERY 685
Cdd:cd14912   550 SfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 189083798  686 RVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14912   630 KVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
80-729 1.08e-140

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: 455.73  E-value: 1.08e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14910     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAI------------SGQ-HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGA 226
Cdd:cd14910    82 SGAGKTVNTKRVIQYFATIavtgekkkeeatSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  227 IEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLG-QASDYNYLAMGNcITCEGRVDSQEYANIRSAM 305
Cdd:cd14910   162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGE-ITVPSIDDQEELMATDSAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  306 KVLMFTDTENWEISKLLAAILHLGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCL------TSRTLI 376
Cdd:cd14910   241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAAYLQNLNSADLLKALcyprvkVGNEYV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  377 TRGETVstplsrEQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCIN 455
Cdd:cd14910   316 TKGQTV------QQVYNAVGALAKAVYDKMFLWMVTRINQQL------DTKQPRQYfIGVLDIAGFEIFDFNSLEQLCIN 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  456 FANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLN 535
Cdd:cd14910   384 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  536 ANYI----PPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAET-------R 604
Cdd:cd14910   464 SNNFqkpkPAKGKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgggkkggK 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  605 KRSP---TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEF 681
Cdd:cd14910   544 KKGSsfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 189083798  682 VERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14910   624 KQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
79-729 1.45e-139

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: 452.24  E-value: 1.45e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14919     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSW------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 232
Cdd:cd14919    81 ESGAGKTENTKKVIQYLAHVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  233 EQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNcITCEGRVDSQEYANIRSAMKVLMFTD 312
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  313 TENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLM-SCLTSRTLITRgETVSTPLSREQA 391
Cdd:cd14919   240 EEQMGLLRVISGVLQLGNIVFKKE--RNTDQASMPDNTAAQKVSHLLGINVTDFTrGILTPRIKVGR-DYVQKAQTKEQA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  392 LDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFK 471
Cdd:cd14919   317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS----FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  472 LEQEEYDLESIDWLHIEF-TDNQDALDMIANK--PMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKN-NHET 547
Cdd:cd14919   393 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlKDKA 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  548 QFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGAETRKRS---PTL 610
Cdd:cd14919   473 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmSETALPGAFKTRKgmfRTV 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  611 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLP 690
Cdd:cd14919   553 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 632
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 189083798  691 GVKPaykQGDLRG--TCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14919   633 NSIP---KGFMDGkqACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
80-729 1.60e-138

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: 449.56  E-value: 1.60e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14915     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAI------------SGQ-HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGA 226
Cdd:cd14915    82 SGAGKTVNTKRVIQYFATIavtgekkkeeaaSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  227 IEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLG-QASDYNYLAMGNcITCEGRVDSQEYANIRSAM 305
Cdd:cd14915   162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQGE-ITVPSIDDQEELMATDSAV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  306 KVLMFTDTENWEISKLLAAILHLGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLITRGETV 382
Cdd:cd14915   241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAAYLTSLNSADLLKALCYPRVKVGNEYV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  383 STPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHL 461
Cdd:cd14915   316 TKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQL------DTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  462 QQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYI-- 539
Cdd:cd14915   390 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFqk 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  540 --PPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAE--------TRKRSP- 608
Cdd:cd14915   470 pkPAKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEggggkkggKKKGSSf 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  609 -TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRV 687
Cdd:cd14915   550 qTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 189083798  688 LLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14915   630 LNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
80-729 4.37e-138

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: 448.35  E-value: 4.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14916     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAISG------------QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAI 227
Cdd:cd14916    82 SGAGKTVNTKRVIQYFASIAAigdrskkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  228 EGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGL-GQASDYNYLAMGNcITCEGRVDSQEYANIRSAMK 306
Cdd:cd14916   162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGE-VSVASIDDSEELLATDSAFD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  307 VLMFTDTENWEISKLLAAILHLGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPL 386
Cdd:cd14916   241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQRE--EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  387 SREQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHLQQFF 465
Cdd:cd14916   319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATL------ETKQPRQYfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  466 VRHVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIaNKPMNIISLIDEESKFPKGTDTTMLHKLNSQH-KLNANYIPPKN 543
Cdd:cd14916   393 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRN 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 ---NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-------ADVAMGAETRKRSP---TL 610
Cdd:cd14916   472 vkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyasadtGDSGKGKGGKKKGSsfqTV 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  611 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLP 690
Cdd:cd14916   552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 631
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 189083798  691 GVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14916   632 AAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
80-729 6.04e-138

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: 447.98  E-value: 6.04e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   80 GILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14923     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLAAI------------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAI 227
Cdd:cd14923    82 SGAGKTVNTKRVIQYFATIavtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  228 EGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLG-QASDYNYLAMGNcITCEGRVDSQEYANIRSAMK 306
Cdd:cd14923   162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGE-VTVASIDDSEELLATDNAID 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  307 VLMFTDTENWEISKLLAAILHLGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLITRGETVS 383
Cdd:cd14923   241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  384 TPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqDVKNSRRS-IGLLDIFGFENFAVNSFEQLCINFANEHLQ 462
Cdd:cd14923   316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL------DTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  463 QFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYI--- 539
Cdd:cd14923   390 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFqkp 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  540 -PPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ----ADVAMGAETRKRSP------ 608
Cdd:cd14923   470 kPAKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagAEAGDSGGSKKGGKkkgssf 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  609 -TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRV 687
Cdd:cd14923   550 qTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 189083798  688 LLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14923   630 LNASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
79-728 9.03e-138

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: 446.99  E-value: 9.03e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLS-IYSPEHIRQY-TNKKIGEMPPHIFAIADNCYFNMK--RNSRDQCC 154
Cdd:cd14880     1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRNVKslIEPVNQSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  155 IISGESGAGKTESTKLILQFLAAISGQH-SW--------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRG 225
Cdd:cd14880    81 VVSGESGAGKTWTSRCLMKFYAVVAASPtSWeshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  226 AIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAmgnciTCEGRVDSQEYANIRSAM 305
Cdd:cd14880   161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLP-----NPERNLEEDCFEVTREAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  306 KVL-MFTDTENwEISKLLAAILHLGNLQY-----EARTFENLDACEVlfspSLATAASLLEVNPPDLMSCLTSRTlITRG 379
Cdd:cd14880   236 LHLgIDTPTQN-NIFKVLAGLLHLGNIQFadsedEAQPCQPMDDTKE----SVRTSALLLKLPEDHLLETLQIRT-IRAG 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  380 ---ETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQdvknSRRSIGLLDIFGFENFAVNSFEQLCINF 456
Cdd:cd14880   310 kqqQVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDS----WTTFIGLLDVYGFESFPENSLEQLCINY 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  457 ANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHK-----LNSQ 531
Cdd:cd14880   386 ANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSAAQLQTriesaLAGN 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  532 HKLNANYIPPKNNhetqFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAE----TRKRS 607
Cdd:cd14880   466 PCLGHNKLSREPS----FIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQeepsGQSRA 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  608 P--TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERY 685
Cdd:cd14880   542 PvlTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERY 621
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 189083798  686 RVLLPgVKPAYKqgdlrgTCQRMAEAVLGTHDDWQIGKTKIFL 728
Cdd:cd14880   622 KLLRR-LRPHTS------SGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
79-729 1.19e-136

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: 444.12  E-value: 1.19e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd15896     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSW-------------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRG 225
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASSHKTkkdqnslalshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  226 AIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNcITCEGRVDSQEYANIRSAM 305
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGN-VTIPGQQDKDLFTETMEAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  306 KVLMFTDTENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTP 385
Cdd:cd15896   240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKE--RHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  386 LSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFF 465
Cdd:cd15896   318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGAS----FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  466 VRHVFKLEQEEYDLESIDWLHIEF-TDNQDALDMIAN--KPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPK 542
Cdd:cd15896   394 NHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPK 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  543 N-NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGAETRK-R 606
Cdd:cd15896   474 KlKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvdrivgldkvsgmSEMPGAFKTRKgM 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  607 SPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYR 686
Cdd:cd15896   554 FRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 633
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 189083798  687 VLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd15896   634 ILTPNAIP---KGfmDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
81-729 4.31e-132

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: 430.46  E-value: 4.31e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNlliRYRDHLIYTYTGSILVAVNPYQLLS-IYSPEHIRQY--TNKKIG---EMPPHIFAIADNCYFNMKRNSRDQCC 154
Cdd:cd14886     6 ILRD---RFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYrqADTSRGfpsDLPPHSYAVAQSALNGLISDGISQSC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  155 IISGESGAGKTESTKLILQFLAAISGQHS-WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIE 233
Cdd:cd14886    83 IVSGESGAGKTETAKQLMNFFAYGHSTSStDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKIT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  234 QYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVlMFTDT 313
Cdd:cd14886   163 SYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEK-LFSKN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  314 ENWEISKLLAAILHLGNLQYEARTFENLD-ACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQAL 392
Cdd:cd14886   242 EIDSFYKCISGILLAGNIEFSEEGDMGVInAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAE 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  393 DVRDAFVKGIYGRLFVWIVDKINAAIykppsQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKL 472
Cdd:cd14886   322 VNIRAVAKDLYGALFELCVDTLNEII-----QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKS 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  473 EQEEYDLESIDWLHIEFTDNQDALdMIANKP-MNIISLIDEESKFPKGTDTTMLHKLNSQHKlNANYIPPKNNhETQFGI 551
Cdd:cd14886   397 EIQEYEIEGIDHSMITFTDNSNVL-AVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSCKSKIK-NNSFIPGKGS-QCNFTI 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  552 NHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRspTLSSQFKRSLELLMRTLGACQPF 631
Cdd:cd14886   474 VHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKGK--FLGSTFQLSIDQLMKTLSATKSH 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  632 FVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQG-DLRGTCQRMAE 710
Cdd:cd14886   552 FIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGeDLVEAVKSILE 631
                         650
                  ....*....|....*....
gi 189083798  711 AVLGTHDDWQIGKTKIFLK 729
Cdd:cd14886   632 NLGIPCSDYRIGKTKVFLR 650
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
79-729 1.91e-128

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: 420.66  E-value: 1.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14930     1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAIS---------GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEG 229
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVAsspkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  230 AKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCiTCEGRvDSQEYANIRSAMKVLM 309
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQETLESLRVLG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  310 FTDTENWEISKLLAAILHLGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDL-MSCLTSRTLITRgETVSTPLSR 388
Cdd:cd14930   239 FSHEEITSMLRMVSAVLQFGNIVLKRE--RNTDQATMPDNTAAQKLCRLLGLGVTDFsRALLTPRIKVGR-DYVQKAQTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  389 EQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKnsrrSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRH 468
Cdd:cd14930   316 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  469 VFKLEQEEYDLESIDWLHIEF-TDNQDALDMI---ANKPmNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKN- 543
Cdd:cd14930   392 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIerpANPP-GLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHl 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGAETRK-RSP 608
Cdd:cd14930   471 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslGDGPPGGRPRRgMFR 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  609 TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVL 688
Cdd:cd14930   551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 189083798  689 LPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14930   631 TPNAIP---KGfmDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
88-729 1.22e-121

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: 400.35  E-value: 1.22e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   88 RYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQY---TNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGESGAGK 164
Cdd:cd14878    10 RFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFILSGERGSGK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  165 TESTKLILQFLAAISG-QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF-NKRGAIEGAKIEQYLLEKSRV 242
Cdd:cd14878    90 TEASKQIMKHLTCRASsSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYMLEKSRL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  243 CRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYL---AMGNCITCEGRVDSQEYANIRSAMKVLMFTdteNWEIS 319
Cdd:cd14878   170 VSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLnqtMREDVSTAERSLNREKLAVLKQALNVVGFS---SLEVE 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  320 KL---LAAILHLGNLQYEARTfenlDACEVLFS--PSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDV 394
Cdd:cd14878   247 NLfviLSAILHLGDIRFTALT----EADSAFVSdlQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  395 RDAFVKGIYGRLFVWIVDKINAAIYkppSQDVKNSRRS--IGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKL 472
Cdd:cd14878   323 RDLLAKSLYSRLFSFLVNTVNCCLQ---SQDEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  473 EQEEYDLESIDWLHIEFTDNQDA-LDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQ---HKLNANYIPPKN----- 543
Cdd:cd14878   400 EQTECVQEGVTMETAYSPGNQTGvLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLlesSNTNAVYSPMKDgngnv 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  544 ---NHETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAmgaetrkrspTLSSQFKRSLEL 620
Cdd:cd14878   480 alkDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV----------TIASQLRKSLAD 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  621 LMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYR----VLLPGVKPAY 696
Cdd:cd14878   550 IIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladTLLGEKKKQS 629
                         650       660       670
                  ....*....|....*....|....*....|...
gi 189083798  697 KQGDLRGTCQRMaeavlgTHDDWQIGKTKIFLK 729
Cdd:cd14878   630 AEERCRLVLQQC------KLQGWQMGVRKVFLK 656
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
79-700 5.37e-119

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: 394.85  E-value: 5.37e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQ---------LLSIYSPEHIRQYTNKKIGEMP--PHIFAIADNCYFNMKR 147
Cdd:cd14899     1 ASILNALRLRYERHAIYTHIGDILISINPFQdlpqlygdeILRGYAYDHNSQFGDRVTSTDPrePHLFAVARAAYIDIVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  148 NSRDQCCIISGESGAGKTESTKLILQFLAAISG------------------QHSWIEQQVLEATPILEAFGNAKTIRNDN 209
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  210 SSRFGKYIDIHF-NKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEG----MSEDQKKKLGL-GQASDYNYLAM 283
Cdd:cd14899   161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALsGGPQSFRLLNQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  284 GNCITC-EGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQYEARTFEN-----LDACEVLFSPS-----L 352
Cdd:cd14899   241 SLCSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfADEARVMSSTTgafdhF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  353 ATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPS--------- 423
Cdd:cd14899   321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  424 -QDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIANK 502
Cdd:cd14899   401 vDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  503 PMNIISLIDEESKFPKGTDTTMLHK--LNSQHKLNANYI--PPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDII 578
Cdd:cd14899   481 PIGIFSLTDQECVFPQGTDRALVAKyyLEFEKKNSHPHFrsAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  579 QLVHSSRNKFIKQIFQADV-----------AMGAETRKRSPT------LSSQFKRSLELLMRTLGACQPFFVRCIKPNEF 641
Cdd:cd14899   561 QLLAGSSNPLIQALAAGSNdedangdseldGFGGRTRRRAKSaiaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 189083798  642 KKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVkpaYKQGD 700
Cdd:cd14899   641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRVLLSL---YKWGD 696
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
79-729 9.33e-112

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: 370.74  E-value: 9.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYtnkkigemppHIFAIADNCYFNMKRN-SRDQCCIIS 157
Cdd:cd14874     1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMsSNAESIVFG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  158 GESGAGKTESTKLILQFLAAiSGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEGAKIEQYL- 236
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTS-QPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKYTVp 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  237 LEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEgRVDSQEYANIRSAMKVLMFTDTENW 316
Cdd:cd14874   149 LEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENI-QSDVNHFKHLEDALHVLGFSDDHCI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  317 EISKLLAAILHLGNLQYEARTFENL--DACEVLFSPSLATAASLLEVNPPDLMSCLTSRTlitrgeTVSTPLSREQALDV 394
Cdd:cd14874   228 SIYKIISTILHIGNIYFRTKRNPNVeqDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKS------EDGTTIDLNAALDN 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  395 RDAFVKGIYGRLFVWIVDKINAAiYKPPsqdvkNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQ 474
Cdd:cd14874   302 RDSFAMLIYEELFKWVLNRIGLH-LKCP-----LHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQL 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  475 EEYDLE--SIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGIN 552
Cdd:cd14874   376 VDYAKDgiSVDYKVPNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERLEFGVR 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  553 HFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQadvAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFF 632
Cdd:cd14874   456 HCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE---SYSSNTSDMIVSQAQFILRGAQEIADKINGSHAHF 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  633 VRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPgvkpaykqGDLrGTCQRMAEAV 712
Cdd:cd14874   533 VRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLP--------GDI-AMCQNEKEII 603
                         650       660
                  ....*....|....*....|....*
gi 189083798  713 --------LGTHDDWQIGKTKIFLK 729
Cdd:cd14874   604 qdilqgqgVKYENDFKIGTEYVFLR 628
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
81-690 7.15e-107

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: 354.97  E-value: 7.15e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQllSIYSPEHIRQYTnKKIGEMPPHIFAIADNCYFNMKRNSrDQCCIISGES 160
Cdd:cd14898     3 TLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNkrGAIEGAKIEQYLLEKS 240
Cdd:cd14898    79 GSGKTENAKLVIKYLVERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLLEKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  241 RVCRQALDERNYHVFY--CMLEGMSEDQkkklglgQASDYNYLAmGNcitCEGRVD-SQEYANIRSAMKVLMFTDTEnwE 317
Cdd:cd14898   157 RVTHHEKGERNFHIFYqfCASKRLNIKN-------DFIDTSSTA-GN---KESIVQlSEKYKMTCSAMKSLGIANFK--S 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  318 ISKLLAAILHLGNLQYeartfeNLDACEVLFS-PSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRD 396
Cdd:cd14898   224 IEDCLLGILYLGSIQF------VNDGILKLQRnESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRN 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  397 AFVKGIYGRLFVWIVDKINAAIYkppsqdvKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEE 476
Cdd:cd14898   298 SMARLLYSNVFNYITASINNCLE-------GSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGM 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  477 YDLESIDWLHIEFTDNqDALDMIANKPMNIISLIDEESKFPKGTDTTMLHKLnsqHKLNANYIppKNNHETQFGINHFAG 556
Cdd:cd14898   371 YKEEGIEWPDVEFFDN-NQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKI---KKYLNGFI--NTKARDKIKVSHYAG 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  557 IVYYETQGFLEKNRDTLHGDIIQlvhssrnkfikqifqaDVAMGAETRKRSptLSSQFKRSLELLMRTLGACQPFFVRCI 636
Cdd:cd14898   445 DVEYDLRDFLDKNREKGQLLIFK----------------NLLINDEGSKED--LVKYFKDSMNKLLNSINETQAKYIKCI 506
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 189083798  637 KPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLP 690
Cdd:cd14898   507 RPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
79-729 6.85e-103

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: 345.46  E-value: 6.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIyspeHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd14937     1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDV----DINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 238
Cdd:cd14937    77 ESGSGKTEASKLVIKYYLSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRvDSQEYANIRSAMKVLMFTDTENwEI 318
Cdd:cd14937   157 NIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEID-DAKDFGNLMISFDKMNMHDMKD-DL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  319 SKLLAAILHLGNLQYEARTFENLDACEVLFSPSLAT---AASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVR 395
Cdd:cd14937   235 FLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNNLELvneISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSIC 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  396 DAFVKGIYGRLFVWIVDKINAAIykppsQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQE 475
Cdd:cd14937   315 KSISKDLYNKIFSYITKRINNFL-----NNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  476 EYDLESIDWLHIEFTDNQDALDMIANKpMNIISLIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGINHFA 555
Cdd:cd14937   390 LYKAEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTV 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  556 GIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDVAMgAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRC 635
Cdd:cd14937   469 SDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYE-DVEV-SESLGRKNLITFKYLKNLNNIISYLKSTNIYFIKC 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  636 IKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAgYPIRYSFVEFVERYRVLLPGVKPAYKQGDlRGTCQRMAEAVLGT 715
Cdd:cd14937   547 IKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSKDSSLTD-KEKVSMILQNTVDP 624
                         650
                  ....*....|....
gi 189083798  716 hDDWQIGKTKIFLK 729
Cdd:cd14937   625 -DLYKVGKTMVFLK 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
79-729 8.55e-103

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: 348.18  E-value: 8.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRY--------RDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSR 150
Cdd:cd14887     1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  151 DQCCIISGESGAGKTESTKLILQFLAAISG-QH----SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRG 225
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSDrRHgadsQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  226 AIEGAKIEQYLLEKSRVCRQALDERNYHVFY--CMLEGMSEDQKKKLGLGqasdYNYLAMGNCITcegrvdsqeyanirS 303
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYalCNAAVAAATQKSSAGEG----DPESTDLRRIT--------------A 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  304 AMKVLMFTDTENWEISKLLAAILHLGNLQY--------------EARTFENLDACEVLFSPS------------------ 351
Cdd:cd14887   223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFttdqepetskkrklTSVSVGCEETAADRSHSSevkclssglkvteasrkh 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  352 LATAASLLEVNPPD-----LMSCLTSRTLitrGETVSTpLSREQALDVRDAFVKGIYGRLFVWIVDKINAA-------IY 419
Cdd:cd14887   303 LKTVARLLGLPPGVegeemLRLALVSRSV---RETRSF-FDLDGAAAARDAACKNLYSRAFDAVVARINAGlqrsakpSE 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  420 KPPSQDVKNSR--RSIGLLDIFGFENF---AVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQD 494
Cdd:cd14887   379 SDSDEDTPSTTgtQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFS 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  495 --ALDMIANKPMNIISLI-------------------------DEESKFP---KGTDTTML--HKLNSQHKLNANY---I 539
Cdd:cd14887   459 fpLASTLTSSPSSTSPFSptpsfrsssafatspslpsslsslsSSLSSSPpvwEGRDNSDLfyEKLNKNIINSAKYkniT 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  540 PPKNNHETQFGINHFAGIVYYETQGFLEKNRDTLHGDI----------IQLVHSSRNKFIKQIfqadvamgaetRKRSPT 609
Cdd:cd14887   539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDELerlflacstyTRLVGSKKNSGVRAI-----------SSRRST 607
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  610 LSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLL 689
Cdd:cd14887   608 LSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKL 687
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 189083798  690 P-GVKPAYKQGDLrgtCQRMAEAVLGTHDDWQIGKTKIFLK 729
Cdd:cd14887   688 PmALREALTPKMF---CKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
81-728 4.80e-102

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: 342.86  E-value: 4.80e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSiySPEHIRQYTNKKIGempPHIFAIADNCYFNMKRNSRDQCCIISGES 160
Cdd:cd14881     3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGTS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAISGQHSWIE--QQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKrGAIEGAKIEQYLLE 238
Cdd:cd14881    78 GSGKTYASMLLLRQLFDVAGGGPETDafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIHCYFLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  239 KSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYN--YLAMGNcITCEGRVDSQEYANIRSAMKVL--MFTDte 314
Cdd:cd14881   157 QTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANlrYLSHGD-TRQNEAEDAARFQAWKACLGILgiPFLD-- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  315 nweISKLLAAILHLGNLQYEARTFENLDaceVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDV 394
Cdd:cd14881   234 ---VVRVLAAVLLLGNVQFIDGGGLEVD---VKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNMT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  395 RDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQ 474
Cdd:cd14881   308 RDALAKALYCRTVATIVRRANSLKRLGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  475 EEYDLESIDW-LHIEFTDNQDALDMIANKPMNIISLIDEESKfPKGTDTTMLHKLNSQHKLNANYIPPKNNHETQFGINH 553
Cdd:cd14881   388 ESCRDEGIQCeVEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIRH 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  554 FAGIVYYETQGFLEKNRDTLHGDIIQLvhssrnkFIKQIFQADVAmgaetrkrspTLSSQFKRSLELLMRTLGACQPFFV 633
Cdd:cd14881   467 FAGRVVYDASDFLDTNRDVVPDDLVAV-------FYKQNCNFGFA----------THTQDFHTRLDNLLRTLVHARPHFV 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  634 RCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPgVKPAYKQGDLRGTCQRMAEAVL 713
Cdd:cd14881   530 RCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAP-FRLLRRVEEKALEDCALILQFL 608
                         650       660
                  ....*....|....*....|....
gi 189083798  714 GTHDD---------WQIGKTKIFL 728
Cdd:cd14881   609 EAQPPsklssvstsWALGKRHIFL 632
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
79-686 1.06e-97

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: 331.87  E-value: 1.06e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPY-QLLSIYSPEHIRQYTNKKIGE-------MPPHIFAIADNCYFNMKRNSR 150
Cdd:cd14884     1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYkPLKELYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  151 DQCCIISGESGAGKTESTKLILQFLAAISGQHSWIE--QQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKR---- 224
Cdd:cd14884    81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTEriDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVentq 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  225 -----GAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQ-----------ASDYNYLAMGNCIT 288
Cdd:cd14884   161 knmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRncgvygllnpdESHQKRSVKGTLRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  289 CEGRVD------SQEYANIRSAMKVLMFTDTENWEISK---LLAAILHLGNLQYEArtfenldacevlfspslatAASLL 359
Cdd:cd14884   241 GSDSLDpseeekAKDEKNFVALLHGLHYIKYDERQINEffdIIAGILHLGNRAYKA-------------------AAECL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  360 EVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSQDVKNSRRS------- 432
Cdd:cd14884   302 QIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDIysineai 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  433 IGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQDALDMIAnkpmNIISLIDE 512
Cdd:cd14884   382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIA----KIFRRLDD 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  513 ESKFP----KGTDT------------TMLHKLNSQHKLN---ANYIPPKNN-HETQFGINHFAGIVYYETQGFLEKNRDT 572
Cdd:cd14884   458 ITKLKnqgqKKTDDhffryllnnerqQQLEGKVSYGFVLnhdADGTAKKQNiKKNIFFIRHYAGLVTYRINNWIDKNSDK 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  573 LHGDIIQLVHSSRNKFIKQifqadvAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLC 652
Cdd:cd14884   538 IETSIETLISCSSNRFLRE------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLV 611
                         650       660       670
                  ....*....|....*....|....*....|....
gi 189083798  653 VRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYR 686
Cdd:cd14884   612 YRQLKQCGSNEMIKILNRGLSHKIPKKETAAALK 645
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
79-729 1.21e-94

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: 323.11  E-value: 1.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   79 AGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISG 158
Cdd:cd01386     1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  159 ESGAGKTESTKLILQFLAAISGQHSW-IEQQVLEAT-PILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYL 236
Cdd:cd01386    81 RSGSGKTTNCRHILEYLVTAAGSVGGvLSVEKLNAAlTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  237 LEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVD-SQEYANIRSAMKVLMFTDTEN 315
Cdd:cd01386   161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKaAAAFSKLQAAMKTLGISEEEQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  316 WEISKLLAAILHLGNlqyeARTFENLDACEVLFS-PSLAT-AASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQ--- 390
Cdd:cd01386   241 RAIWSILAAIYHLGA----AGATKAASAGRKQFArPEWAQrAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESpar 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  391 ---------ALDVRDAFVKGIYGRLFVWIVDKINAAIykppsqdvKNSRR---SIGLLDIFGFENFAVN------SFEQL 452
Cdd:cd01386   317 sssggpkltGVEALEGFAAGLYSELFAAVVSLINRSL--------SSSHHstsSITIVDTPGFQNPAHSgsqrgaTFEDL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  453 CINFANEHLQQFFVRHVFKLEQEEYDLESIDwLHIEFTDN--QDALDMIANKPMNIIS--------------LIDEESKF 516
Cdd:cd01386   389 CHNYAQERLQLLFHERTFVAPLERYKQENVE-VDFDLPELspGALVALIDQAPQQALVrsdlrdedrrgllwLLDEEALY 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  517 PKGTDTTMLHKLNSQH----KLNANYIPPKNNHETQFGINHFAGI--VYYETQGFLEKNRDTL-HGDIIQLVHSSRNKFi 589
Cdd:cd01386   468 PGSSDDTFLERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKENPsAQNATQLLQESQKET- 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  590 kqifqadvamgAETRKRSPTLssQFKRSLELLMRTLGACQPFFVRCIKPN------------EFKKPMLFDRHLCVRQLR 657
Cdd:cd01386   547 -----------AAVKRKSPCL--QIKFQVDALIDTLRRTGLHFVHCLLPQhnagkderstssPAAGDELLDVPLLRSQLR 613
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  658 YSGMMETIRIRRAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHD----DWQIGKTKIFLK 729
Cdd:cd01386   614 GSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKAVEELLEELDleksSYRIGLSQVFFR 689
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
88-729 2.55e-90

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: 310.10  E-value: 2.55e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   88 RYRDHLIYTYTGSILVAVNPYQLLS-IYSPEHIRQYTNKKigEMPPHIFAIADNCYFNMKRNSRDQCCIISGESGAGKTE 166
Cdd:cd14905    10 RYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  167 STKLILQFLAAISGQHS-WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQ 245
Cdd:cd14905    88 NTKIIIQYLLTTDLSRSkYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  246 ALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAI 325
Cdd:cd14905   168 NKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  326 LHLGNLQYeartFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTlitrgetvSTPLSreQALDVRDAFVKGIYGR 405
Cdd:cd14905   248 IILGNVTF----FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDR--------SMPVN--EAVENRDSLARSLYSA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  406 LFVWIVDKINAAIykPPSQdvknSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWL 485
Cdd:cd14905   314 LFHWIIDFLNSKL--KPTQ----YSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWM 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  486 H-IEFTDNQDALDMIAnkpmNIISLIDEESKFPKGTDTTMLHKLnsQHKLNANYIPPKNnhETQFGINHFAGIVYYETQG 564
Cdd:cd14905   388 TpISFKDNEESVEMME----KIINLLDQESKNINSSDQIFLEKL--QNFLSRHHLFGKK--PNKFGIEHYFGQFYYDVRG 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  565 FLEKNRDtlhgDIIQLVHS-SRNKFIKQIFQAD-----VAMGAETRKRSPTLSSQFKRSLELLMRTLGA----------- 627
Cdd:cd14905   460 FIIKNRD----EILQRTNVlHKNSITKYLFSRDgvfniNATVAELNQMFDAKNTAKKSPLSIVKVLLSCgsnnpnnvnnp 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  628 --------------------------------------CQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRR 669
Cdd:cd14905   536 nnnsgggggggnsgggsgsggstyttysstnkainnsnCDFHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQR 615
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083798  670 AGYPIRYSFVEFVERYRVLLPgvkpayKQGDLRGTCQRMAEAVLGTHD----DWQIGKTKIFLK 729
Cdd:cd14905   616 FGYTIHYNNKIFFDRFSFFFQ------NQRNFQNLFEKLKENDINIDSilppPIQVGNTKIFLR 673
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
81-729 2.41e-86

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: 297.42  E-value: 2.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGES 160
Cdd:cd14882     3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  161 GAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKS 240
Cdd:cd14882    83 YSGKTTNARLLIKHLCYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  241 RVCRQALDERNYHVFYCMLEGM-SEDQKKKLGLGQASDYNYLAMGNCITCEG----RVDSQE----YANIRSAMKVLMFT 311
Cdd:cd14882   163 RVSTTDGNQSNFHIFYYFYDFIeAQNRLKEYNLKAGRNYRYLRIPPEVPPSKlkyrRDDPEGnverYKEFEEILKDLDFN 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  312 DTENWEISKLLAAILHLGNLQY-EARTFENLDACEVlfspsLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQ 390
Cdd:cd14882   243 EEQLETVRKVLAAILNLGEIRFrQNGGYAELENTEI-----ASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  391 ALDVRDAFVKGIYGRLFVWIVDKINAAIYKPPSqdVKNSRRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVF 470
Cdd:cd14882   318 ARDARDVLASTLYSRLVDWIINRINMKMSFPRA--VFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  471 KLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEESKFPKGTDTTMlhklNSQHKLNANYIPPKNNHEtqFG 550
Cdd:cd14882   396 ISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQNYIM----DRIKEKHSQFVKKHSAHE--FS 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  551 INHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQadvamGAETRKRSpTLSSQFK-RSLELLmRTL---- 625
Cdd:cd14882   470 VAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFT-----NSQVRNMR-TLAATFRaTSLELL-KMLsiga 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  626 GACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLlpgvkpAYKqgdlrgtc 705
Cdd:cd14882   543 NSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL------AFD-------- 608
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 189083798  706 qrMAEAVLGTHDD------------WQIGKTKIFLK 729
Cdd:cd14882   609 --FDETVEMTKDNcrlllirlkmegWAIGKTKVFLK 642
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
82-728 1.27e-83

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: 292.26  E-value: 1.27e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   82 LRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKK----------IGEMPPHIFAIADNCYFNMKRNSRD 151
Cdd:cd14893     4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGED 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  152 QCCIISGESGAGKTESTKLILQFLAAI-------------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYID 218
Cdd:cd14893    84 QAVILLGGMGAGKSEAAKLIVQYLCEIgdeteprpdsegaSGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  219 IHFNKRGAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQ--KKKLGLGQ-ASDYNYLAMGNCITCEGRVDS 295
Cdd:cd14893   164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNKcVNEFVMLKQADPLATNFALDA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  296 QEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQY-------------EARTFENLDACEVLFSPSLATAASLLEVN 362
Cdd:cd14893   244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQSCALKDPAQILLAAKLLEVE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  363 PPDLMSCLTSRTLITR--GETVST--PLSREQALDVRDAFVKGIYGRLFVWIVDKINAAI------YKpPSQDVKNSrRS 432
Cdd:cd14893   324 PVVLDNYFRTRQFFSKdgNKTVSSlkVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdrYE-KSNIVINS-QG 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  433 IGLLDIFGFENF--AVNSFEQLCINFANEHLQQFFVRHVFK-----LEQEEYDLES--IDWLHIEFTDNQD-ALDMIANK 502
Cdd:cd14893   402 VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEkCLQLFEDK 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  503 PMNIISLIDEESKFPKGTDTTMLHKLNSQHK---------LNAN----YIPPKNNHETQFGINHFAGIVYYETQGFLEKN 569
Cdd:cd14893   482 PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEavgglsrpnMGADttneYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKN 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  570 RDTLHGDIIQLVHSSRNKFI-----KQIFQADVAMGAETRKRSPTLSSQFKRSL---------------------ELLMR 623
Cdd:cd14893   562 MLSISSTCAAIMQSSKNAVLhavgaAQMAAASSEKAAKQTEERGSTSSKFRKSAssaresknitdsaatdvynqaDALLH 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  624 TLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVLLpgvkpaykqgDLRG 703
Cdd:cd14893   642 ALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVC----------GHRG 711
                         730       740
                  ....*....|....*....|....*....
gi 189083798  704 TCQRMAEAV--LGTHDD--WQIGKTKIFL 728
Cdd:cd14893   712 TLESLLRSLsaIGVLEEekFVVGKTKVYL 740
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
2111-2206 9.41e-67

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270020  Cd Length: 96  Bit Score: 220.21  E-value: 9.41e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2111 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2190
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80
                          90
                  ....*....|....*.
gi 189083798 2191 DDLLTSYISQMLTAMS 2206
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1257-1355 1.10e-65

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 217.12  E-value: 1.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1257 PIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQ 1336
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 189083798 1337 ERNAPWRLFFRKEVFTPWH 1355
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1901-1998 1.55e-62

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 208.25  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1901 QIFHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSVPENDFFFDFVRHLTDWIKKARPIK 1980
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80
                          90
                  ....*....|....*...
gi 189083798 1981 DGIVPSLTYQVFFMKKLW 1998
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1763-1896 1.19e-58

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 199.12  E-value: 1.19e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1763 SEELSQEACLAFIAVLKYMGDYPSKRTRSVNELTDQIFEGPLKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTG 1842
Cdd:smart00139   15 SDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPSRQSEERGWQLLYLCTS 94
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798   1843 LFPPSNILLPHVQRFLQSRKHC----PLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQ 1896
Cdd:smart00139   95 LFPPSERLLPYLLQFLSRRADPgseqGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1017-1253 2.04e-55

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 189.88  E-value: 2.04e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1017 YTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPkyhtamsdgsekipvmtkiyetlgkktykrelqalqgegea 1096
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGDIPLP----------------------------------------- 39
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1097 qlpegqkkssvrhklvhltlkkksklteevtkrlhdgestvqgnsmledRPTSNLEKLHFIIGNGILRPALRDEIYCQIS 1176
Cdd:smart00139   40 -------------------------------------------------RPDSHLDLVQFILQKGLDHPELRDEIYCQLI 70
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1177 KQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPP-----GYAPYCEERLRRTFVNGTRTQPPSWLELQA 1251
Cdd:smart00139   71 KQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseqGLAKYCLYRLERTLKNGARKQPPSRLELEA 150

                    ..
gi 189083798   1252 TK 1253
Cdd:smart00139  151 IL 152
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
81-728 2.06e-53

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: 201.60  E-value: 2.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   81 ILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYT-NKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGE 159
Cdd:cd14938     3 VLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  160 SGAGKTESTKLILQFLA----------AISGQHSWIEQQVLEATP--------------ILEAFGNAKTIRNDNSSRFGK 215
Cdd:cd14938    83 SGSGKSEIAKNIINFIAyqvkgsrrlpTNLNDQEEDNIHNEENTDyqfnmsemlkhvnvVMEAFGNAKTVKNNNSSRFSK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  216 YIDIHFNKRgAIEGAKIEQYLLEKSRVCRQALDERNYHVFYCMLEGMSEDQKKKLGLGQASDYNYLAMGNCITCEGRvDS 295
Cdd:cd14938   163 FCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD-YS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  296 QEYANIRSAMKVLMFTDTENWEISKLLAAILHLGNLQ-----YEARTFENLDACEVLFS--------------------P 350
Cdd:cd14938   241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafRKKSLLMGKNQCGQNINyetilselensedigldenvK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  351 SLATAASLLEVNPPDLMSCLTSRTLITrgETVSTPLSREQALDVR-DAFVKGIYGRLFVWIVDKINAAIYKppSQDVKNS 429
Cdd:cd14938   321 NLLLACKLLSFDIETFVKYFTTNYIFN--DSILIKVHNETKIQKKlENFIKTCYEELFNWIIYKINEKCTQ--LQNININ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  430 RRSIGLLDIFGFENFAVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDW-LHIEFTDNQDALDMIANKPMNIIS 508
Cdd:cd14938   397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCeYNSENIDNEPLYNLLVGPTEGSLF 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  509 LIDEESKFPKGTDTTMLHKLNSQHKLNANYIPPKNN---HETQFGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSR 585
Cdd:cd14938   477 SLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDitgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  586 NKFIKQI---FQADVAMGAETRKRSPTLSSQFK------------------RSLELLMRTLGACQPFFVRCIKPNEFKKP 644
Cdd:cd14938   557 NEYMRQFcmfYNYDNSGNIVEEKRRYSIQSALKlfkrrydtknqmavsllrNNLTELEKLQETTFCHFIVCMKPNESKRE 636
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  645 M-LFDRHLCVRQLRYSGMMETIRIRRAGYPIRYSFVEFVERYRVllpgvkpayKQGDLRGTCQRMAEAVLGTHDDWQIGK 723
Cdd:cd14938   637 LcSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI---------KNEDLKEKVEALIKSYQISNYEWMIGN 707

                  ....*
gi 189083798  724 TKIFL 728
Cdd:cd14938   708 NMIFL 712
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
1468-1604 9.84e-52

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270019  Cd Length: 99  Bit Score: 177.41  E-value: 9.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1468 LLFSRFYEAYKFSGPSLPKNDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSrecrvwlslgcsdlgcaaphsgwag 1547
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSS------------------------- 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798 1548 ltpagpcspcwscRGAKTTAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKR 1604
Cdd:cd13198    56 -------------RGKRDGGQSFTLTTIQGEEFVFQSPNAEDIAELVNYFLEGLRKR 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1903-2115 6.01e-47

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 167.86  E-value: 6.01e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1903 FHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSvpendfffdfvrhltDWIKKARPIKDG 1982
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1983 IVPSLTYQVFFMKKLWTTTV--PGKDPMADsIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPK-- 2058
Cdd:smart00295   66 DVKSEPLTLYFRVKFYPPDPnqLKEDPTRL-NLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798   2059 LLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFF 2115
Cdd:smart00295  145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1154-1251 6.26e-42

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 149.65  E-value: 6.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  1154 LHFIIGNGILRPALRDEIYCQISKQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIH-------GGPPGYAPY 1226
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpsREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 189083798  1227 CEERLRRTFVNGTRTQPPSWLELQA 1251
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
101-219 1.49e-39

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: 145.18  E-value: 1.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  101 ILVAVNPYQLLSIYSPEH-IRQYTNKKIGEMPPHIFAIADNCYFNMKRNSRDQCCIISGESGAGKTESTKLILQFLAAIS 179
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKiIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  180 GQH-------SW---------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 219
Cdd:cd01363    81 FNGinkgeteGWvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1259-1474 2.95e-38

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 142.82  E-value: 2.95e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1259 MLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVsslgsgsdhvmdaISQCEQYAKEQGAQER 1338
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   1339 N-APWRLFFRKEVFTPWHS-PSEDNVATNLIYQQVVRGVKFGEYRCEKEdDLAELASQQYFVDYG---SEMILERLLNLV 1413
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEE-EALLLAALALQAEFGdydEELHDLRGELSL 146
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083798   1414 PTYIPDREITPlKTLEKWAQLAIAAHKKGIYaQRRTDAqKVKedVVSYARfKWPLLFSRFY 1474
Cdd:smart00295  147 KRFLPKQLLDS-RKLKEWRERIVELHKELIG-LSPEEA-KLK--YLELAR-KLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1796-1894 2.71e-37

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 136.17  E-value: 2.71e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  1796 TDQIFEGPLKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTGLFPPSNILLPHVQRFLQ------SRKHCPLAID 1869
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpSREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 189083798  1870 CLQRLQKALRNGSRKYPPHLVEVEA 1894
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
1605-1669 1.02e-34

Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin that is involved in organelle transport. It is required for sensory function in both Drosophila and mammals. Mutations in the Myo7A gene cause both syndromic deaf-blindness [Usher syndrome I (USH1)] and nonsyndromic (DFNB2 and DFNA11) deafness in humans. It contains an N-terminal motor domain, light chain-binding IQ motifs, a coiled-coil region for heavy chain dimerization, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212814  Cd Length: 64  Bit Score: 127.63  E-value: 1.02e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189083798 1605 SKYVVALQDNPNPAGEeSGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDSVYV 1669
Cdd:cd11881     1 SKYVVALQDYPNPSDG-SSFLSFAKGDLIILDQDTGEQVMNSGWCNGRNDRTGQRGDFPADCVYV 64
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
189-669 5.77e-28

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: 123.31  E-value: 5.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  189 VLEATPILEAFGNAKTIRNDNSSRFGKY--IDIHFNKRG---AIEGAKIEQYLLEKSRVC----RQALD--ERNYHVFYC 257
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTsergRESGDqnELNFHILYA 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  258 MLEGMSEDQ-----KKKLGLG--QASDYNYLA-----MGNCITCEG--RVDSQEYANIRSAMKVLMFTDTENWEISKLLA 323
Cdd:cd14894   329 MVAGVNAFPfmrllAKELHLDgiDCSALTYLGrsdhkLAGFVSKEDtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  324 AILHLGNLQYEARTFEN---LDACEVLFSPSlaTAASLLE---VNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDA 397
Cdd:cd14894   409 AVLWLGNIELDYREVSGklvMSSTGALNAPQ--KVVELLElgsVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRDT 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  398 FVKGIYGRLFVWIVDKIN-----AAIYKPPSQDVKNSRRS-------IGLLDIFGFENFAVNSFEQLCINFANEHLqqff 465
Cdd:cd14894   487 LARLLYQLAFNYVVFVMNeatkmSALSTDGNKHQMDSNASapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKL---- 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  466 vrhvFKLEQEEYDLESIDWLHIEFTDNQDALDMIANKPMNIISLIDEeskfpkgtdTTMLHK---LNSQHKLNANYI--- 539
Cdd:cd14894   563 ----YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEE---------LTILHQsenMNAQQEEKRNKLfvr 629
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  540 ------------PPK--NNHETQ---------FGINHFAGIVYYETQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQAD 596
Cdd:cd14894   630 niydrnssrlpePPRvlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNES 709
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  597 VAMG------------AETR-KRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMME 663
Cdd:cd14894   710 SQLGwspntnrsmlgsAESRlSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIR 789

                  ....*.
gi 189083798  664 TIRIRR 669
Cdd:cd14894   790 QMEICR 795
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
2013-2115 3.43e-20

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 88.10  E-value: 3.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  2013 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF--EEDKSYFPSIPKLLReLVPQDLIRQVSPDDWKRSIVAYFNKHAG 2090
Cdd:pfam00373   14 LLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFgdYQPSSHTSEYLSLES-FLPKQLLRKMKSKELEKRVLEAHKNLRG 92
                           90       100
                   ....*....|....*....|....*
gi 189083798  2091 KSKEEAKLAFLKLIFKWPTFGSAFF 2115
Cdd:pfam00373   93 LSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
2013-2107 1.23e-18

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 83.06  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2013 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF-EEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGK 2091
Cdd:cd14473     4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYgDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83
                          90
                  ....*....|....*.
gi 189083798 2092 SKEEAKLAFLKLIFKW 2107
Cdd:cd14473    84 SPAEAKLKYLKIARKL 99
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
2111-2202 4.06e-16

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 75.49  E-value: 4.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2111 GSAFFEVKQTTEpnFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWS-SGNTYFHITIGNLVRGSKLLCETS--LG 2187
Cdd:cd00836     1 GVEFFPVKDKSK--KGSPIILGVNPEGISVYDELTGQPLVLFPWPNIKKISfSGAKKFTIVVADEDKQSKLLFQTPsrQA 78
                          90
                  ....*....|....*
gi 189083798 2188 YKMDDLLTSYISQML 2202
Cdd:cd00836    79 KEIWKLIVGYHRFLL 93
FERM_F1_DdMyo7_like cd17208
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium ...
1256-1351 1.11e-12

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins; DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340728  Cd Length: 98  Bit Score: 65.74  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1256 KPIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDR-FGFSLYIALFDKVSSLGSgSDHVMDAISQCEQYAKEQG 1334
Cdd:cd17208     2 RPIVARFYFLDGQFKALEFDSAATAAEVLEQLKQKIGLRSTaDGFALYEVFGGIERAILP-EEKVADVLSKWEKLQRTMA 80
                          90
                  ....*....|....*..
gi 189083798 1335 AQERNAPWRLFFRKEVF 1351
Cdd:cd17208    81 SCAAQQAVKFVFKKRLF 97
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1257-1348 6.96e-12

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 63.80  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1257 PIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVSSLGSGsDHVMDAISQCEQY-AKEQGA 1335
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEG-DFFFDFIRHLTDWiKKARPT 79
                          90
                  ....*....|....*..
gi 189083798 1336 QERNAP---WRLFF-RK 1348
Cdd:cd17093    80 KDGPKPsltYQVFFmRK 96
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
1363-1463 2.54e-10

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 59.18  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1363 ATNLIYQQVVRGVKFGEYRCeKEDDLAELASQQYFVDYG--SEMILERLLNLVPTYIPDREITPLKtLEKWAQLAIAAHK 1440
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPC-SEETAALLAALALQAEYGdyDPSEHKPKYLSLKRFLPKQLLKQRK-PEEWEKRIVELHK 78
                          90       100
                  ....*....|....*....|...
gi 189083798 1441 KgiyaQRRTDAQKVKEDVVSYAR 1463
Cdd:cd14473    79 K----LRGLSPAEAKLKYLKIAR 97
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
1902-1996 5.22e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 54.90  E-value: 5.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1902 IFHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKvlsvpeNDFFFDFVRHLTDWIKKARPikd 1981
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDG------QKHWLDLDKKISKQLKRSGP--- 71
                          90
                  ....*....|....*
gi 189083798 1982 givpsltYQVFFMKK 1996
Cdd:cd01765    72 -------YQFYFRVK 79
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
857-933 7.69e-09

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 56.59  E-value: 7.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   857 QRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQ---ERLAQL----------AREDAERELKEKE------ 917
Cdd:pfam05672   49 RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQreqEEQERLqkqkeeaeakAREEAERQRQEREkimqqe 128
                           90
                   ....*....|....*....
gi 189083798   918 -AAR--RKKELLEQMERAR 933
Cdd:pfam05672  129 eQERleRKKRIEEIMKRTR 147
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
1258-1348 9.95e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 54.13  E-value: 9.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1258 IMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVS-SLGSgSDHVMDAISqceqyakeqgaq 1336
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDL-DKKISKQLK------------ 67
                          90
                  ....*....|..
gi 189083798 1337 eRNAPWRLFFRK 1348
Cdd:cd01765    68 -RSGPYQFYFRV 78
FERM_F1_Myo10_like cd17110
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional ...
1256-1351 1.32e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X and similar proteins; Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Amoebozoan Dictyostelium discoideum myosin VII (DdMyo7) and uncharacterized pleckstrin homology domain-containing family H member 3 (PLEKHH3) are also included in this family. Like metazoan Myo10, DdMyo7 is essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin.


Pssm-ID: 340630  Cd Length: 97  Bit Score: 54.31  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1256 KPIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKD-RFGFSLYiALFDKVSSLGSGSDHVMDAISQCEQYAKEqG 1334
Cdd:cd17110     2 QELTVTVTCQGGRTCKVAIDSWTTCGEVSKDLARRLGLERsRNGFALF-ETSGDIERALEAKTRVVDVLSKWEKLAAT-G 79
                          90
                  ....*....|....*..
gi 189083798 1335 AQERNAPWRLFFRKEVF 1351
Cdd:cd17110    80 SSPGDDGWKLLFKLYLF 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1906-1966 1.60e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 54.18  E-value: 1.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189083798 1906 VYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVLSV-PENDFFFDFV 1966
Cdd:cd17092     6 VTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLgSGTDHVMDAI 67
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
857-935 6.66e-08

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 53.89  E-value: 6.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   857 QRLRAEYLWRLEAEKM-RLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQME-RARH 934
Cdd:pfam05672   33 ERLEKEEEERLRKEELrRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEaKARE 112

                   .
gi 189083798   935 E 935
Cdd:pfam05672  113 E 113
FERM_C2_myosin_like cd13204
FERM domain C-lobe, repeat 2, of Myosin-like proteins; These myosin-like proteins are ...
2111-2197 6.66e-08

FERM domain C-lobe, repeat 2, of Myosin-like proteins; These myosin-like proteins are unidentified though they are sequence similar to myosin 1/myo1, myosin 7/myoVII, and myosin 10/myoX. These myosin-like proteins contain an N-terminal motor/head region and a C-terminal tail consisting of two myosin tail homology 4 (MyTH4) and twos FERM domains. In myoX the FERM domain forms a supramodule with its MyTH4 domain which binds to the negatively charged E-hook region in the tails of alpha- and beta-tubulin forming a proposed motorized link between actin filaments and microtubules and a similar thing might happen in these myosins. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The second FERM_N repeat is present in this hierarchy. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270025  Cd Length: 93  Bit Score: 52.05  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2111 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2190
Cdd:cd13204     1 GSTVFDVTQSYTSNLPKTLWLAIDQSGVHLLERRTKEPLCSYDYSSIVSYSPSLNSLMIVTGSLTKGSKFIFNTNQAFQI 80

                  ....*..
gi 189083798 2191 DDLLTSY 2197
Cdd:cd13204    81 ANLIRDY 87
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
843-935 8.61e-08

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 53.52  E-value: 8.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   843 VQAYARGMIARRLHQR---LRAEYLWRLEA-----EKMRLAEEEKLRK-EMSAKKAKEEAERKHQErlaQLAREDAEREL 913
Cdd:pfam15346   16 VEEAVAKRVEEELEKRkdeIEAEVERRVEEarkimEKQVLEELEREREaELEEERRKEEEERKKRE---ELERILEENNR 92
                           90       100       110
                   ....*....|....*....|....*....|.
gi 189083798   914 KEKEAARRKKE----LLEQ-----MERARHE 935
Cdd:pfam15346   93 KIEEAQRKEAEerlaMLEEqrrmkEERQRRE 123
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
795-933 1.45e-07

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 56.50  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   795 LRLQALHRSRKlhQQYRLARQRIIQFQ-ARCRAYLVRKAFRHRLwavltvqayargmiaRRLHQRLRAEYLWRLEAEK-- 871
Cdd:pfam15709  391 LRKQRLEEERQ--RQEEEERKQRLQLQaAQERARQQQEEFRRKL---------------QELQRKKQQEEAERAEAEKqr 453
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798   872 -----MRLAEEEKLRKEMsAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKEllEQMERAR 933
Cdd:pfam15709  454 qkeleMQLAEEQKRLMEM-AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALE--EAMKQAQ 517
FERM_C_MyoXV cd13201
FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based ...
2111-2209 2.46e-07

FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based motor proteins essential for a variety of biological processes in actin cytoskeleton function. Specifically MyoXV functions in the actin organization in hair cells of the organ of Corti. Mutations in Human MyoXVa causes non-syndromic deafness, DFNB3 and the mouse shaker-2 mutation. MyoXV consists of a N-terminal motor/head region, a neck made of 1-3 IQ motifs, and a tail that consists of either a myosin tail homology 4 (MyTH4) domains, followed by an SH3 domain, and a MyTH-FERM domains as in rat Myo15 or two MyTH-FERM domains separated by a SH3 domain as in human Myo15A. The MyTH-FERM domains are thought to mediate dimerization and binding to other proteins or cargo. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270022  Cd Length: 101  Bit Score: 50.68  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2111 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPKTKDILTTHPFT------KISNWSSGNTYFHITIGNLVRGSKLLCET 2184
Cdd:cd13201     1 GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKevqstrKLRPLEDGTPFLDIKYGNLMQQRTIRLET 80
                          90       100
                  ....*....|....*....|....*
gi 189083798 2185 SLGYkmddLLTSYISQMLTAMSKQR 2209
Cdd:cd13201    81 DQAH----EISRLIAQYIEEASENR 101
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
866-937 5.42e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 51.19  E-value: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   866 RLEAEKMRLA-------EEEKLRKEMSAKKAKEEAERKHQERLAQL---AREDAERELKEKEAARRKKElLEQMERARHE 935
Cdd:pfam05672   14 RILAEKRRQAreqrereEQERLEKEEEERLRKEELRRRAEEERARReeeARRLEEERRREEEERQRKAE-EEAEEREQRE 92

                   ..
gi 189083798   936 PV 937
Cdd:pfam05672   93 QE 94
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
851-923 6.30e-07

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 53.73  E-value: 6.30e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189083798   851 IARRLHqrLRAEYLWRleAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQ----LAREDAE--RELKEKEAARRKK 923
Cdd:pfam07946  248 LAKRAK--LRPEALKK--AKKTREEEIEKIKKAAEEERAEEAQEKKEEAKKKEreekLAKLSPEeqRKYEEKERKKEQR 322
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
853-924 9.24e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 53.31  E-value: 9.24e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189083798   853 RRLHQRLRAEYLWRlEAEKMRLAEEEKlRKEMSAKKAKEEAERKhqerlaqlAREDAERELKEKEAARRKKE 924
Cdd:TIGR02794   92 KELEQRAAAEKAAK-QAEQAAKQAEEK-QKQAEEAKAKQAAEAK--------AKAEAEAERKAKEEAAKQAE 153
PTZ00121 PTZ00121
MAEBL; Provisional
804-935 1.41e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  804 RKLHQQYRLARQRIIQFQarcRAYLVRKAFRHRLWAVLTVQAYARGMIArrlhQRLRAEYLWRLEAEKMRLAEEEKLRKE 883
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALR---KAEEAKKAEEARIEEVMKLYEEEKKMKA----EEAKKAEEAKIKAEELKKAEEEKKKVE 1636
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  884 MSAKKAKEE---AE--RKHQE----RLAQLAREDAE-----RELKEKEAARRKKEllEQMERARHE 935
Cdd:PTZ00121 1637 QLKKKEAEEkkkAEelKKAEEenkiKAAEEAKKAEEdkkkaEEAKKAEEDEKKAA--EALKKEAEE 1700
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
856-934 3.32e-06

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 51.53  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   856 HQ-RLRAEYlwrlEAEKMRLAEEEKLRKEMSAKKAK------EEAERK-HQERLAQLAREDAERELKEKeaaRRKKELLE 927
Cdd:pfam07767  197 HQeLLQKAV----EAEKKRLKEEEKLERVLEKIAESaataeaREEKRKtKAQRNKEKRRKEEEREAKEE---KALKKKLA 269

                   ....*..
gi 189083798   928 QMERARH 934
Cdd:pfam07767  270 QLERLKE 276
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
874-933 4.92e-06

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 46.11  E-value: 4.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  874 LAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERAR 933
Cdd:cd22249     1 LSKPGEIREEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRKREREEQLKQDE 60
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
857-935 5.66e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.58  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  857 QRLRAEylwrLEAEKMRLAEEEKLRKEMSAKKAKEEAERK---HQERLAQLAREDAERELK-EKEAARRKKELLEQMERA 932
Cdd:COG3064    25 KRAAAE----AEQKAKEEAEEERLAELEAKRQAEEEAREAkaeAEQRAAELAAEAAKKLAEaEKAAAEAEKKAAAEKAKA 100

                  ...
gi 189083798  933 RHE 935
Cdd:COG3064   101 AKE 103
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
868-935 6.38e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 50.61  E-value: 6.38e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798   868 EAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHE 935
Cdd:TIGR02794   79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKE 146
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
2111-2198 1.31e-05

FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in initiating actin filament growth in motile cell protrusions. It is responsible for linking the cytoplasmic domains of integrins to the actin-based cytoskeleton, and is involved in vinculin, integrin and actin interactions. At the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in transient adhesions, some of which become more stable focal adhesions (FA). During this maturation process, layilin is replaced with integrins, where localized production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. Talins are composed of a N-terminal region FERM domain which us made up of 3 subdomains (N, alpha-, and C-lobe; or- A-lobe, B-lobe, and C-lobe; or F1, F2, and F3) connected by short linkers, a talin rod which binds vinculin, and a conserved C-terminal region with actin- and integrin-binding sites. There are 2 additional actin-binding domains, one in the talin rod and the other in the FERM domain. Both the F2 and F3 FERM subdomains contribute to F-actin binding. Subdomain F3 of the FERM domain contains overlapping binding sites for integrin cytoplasmic domains and for the type 1 gamma isoform of PIP-kinase (phosphatidylinositol 4-phosphate 5-kinase). The FERM domain has a cloverleaf tripart structure . F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 269973  Cd Length: 92  Bit Score: 45.41  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 2111 GSAFFEVKQTTE-PNFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWSSGNTYFHITIGNLvRGSKLLCETSLGYK 2189
Cdd:cd10569     1 GVTFFLVKEKMKgKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDY-SENYYSVQTTEGEQ 79

                  ....*....
gi 189083798 2190 MDDLLTSYI 2198
Cdd:cd10569    80 ISQLISGYI 88
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
857-935 1.42e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 50.34  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   857 QRLRAEY--LWRLEAEKMRLAEEEKLR----KEMSAKKAKEEAERKHQERLAQ--LAREDAERELKEKEAARRKKELLEQ 928
Cdd:pfam15709  336 DRLRAERaeMRRLEVERKRREQEEQRRlqqeQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQRLQLQ 415

                   ....*....
gi 189083798   929 M--ERARHE 935
Cdd:pfam15709  416 AaqERARQQ 424
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
852-933 2.84e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 49.27  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  852 ARRLHQRLRAEylwRLEAEKMRLAEEEKLRKEMSAKKAKEEAErkhQERLAQL-AREDAERELKEKEAARRKKELLEQME 930
Cdd:COG3064     1 AQEALEEKAAE---AAAQERLEQAEAEKRAAAEAEQKAKEEAE---EERLAELeAKRQAEEEAREAKAEAEQRAAELAAE 74

                  ...
gi 189083798  931 RAR 933
Cdd:COG3064    75 AAK 77
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
857-925 3.40e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.65  E-value: 3.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083798  857 QRLRAEYLWRLEAEKMRLAEEEKlRKEMSAKKAKEEAERKHQERLAQLAREDAER----ELKEKEAARRKKEL 925
Cdd:PRK09510  116 QKKQAEEAAKQAALKQKQAEEAA-AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKkaeaEAAKKAAAEAKKKA 187
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
798-935 4.20e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  798 QALHRSRKLHQQYRLARQRIIQFQARC-RAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRLAE 876
Cdd:COG4717    78 EELKEAEEKEEEYAELQEELEELEEELeELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 189083798  877 EEKLRKEMsaKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHE 935
Cdd:COG4717   158 LRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
796-946 4.43e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   796 RLQALHRSRKLHQQYRlARQRIIQFQARCRAYLVRKAF-RHRLWAVLTVQAYARGMiarrlhQRLRAEYLwRLEAEKMRL 874
Cdd:pfam17380  308 KAREVERRRKLEEAEK-ARQAEMDRQAAIYAEQERMAMeRERELERIRQEERKREL------ERIRQEEI-AMEISRMRE 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   875 AEE---------EKLRKEM-SAKKAK---EEAERKHQERLAQLAREDAERE-LKEKEAARRKKELLEQMERARHEPVNHS 940
Cdd:pfam17380  380 LERlqmerqqknERVRQELeAARKVKileEERQRKIQQQKVEMEQIRAEQEeARQREVRRLEEERAREMERVRLEEQERQ 459

                   ....*.
gi 189083798   941 DMVDKM 946
Cdd:pfam17380  460 QQVERL 465
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
796-966 4.69e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  796 RLQALHRSRKLHQQYRLARQRiiQFQARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRLA 875
Cdd:PRK09510  110 RLAAQEQKKQAEEAAKQAALK--QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  876 EEEKLRKEMSAKKAKEEAERKhqERLAQLAREDAERELKEK--EAARRKKELLEQMERA----RHEPVNHSDMVDKMFGF 949
Cdd:PRK09510  188 EAEAAAKAAAEAKKKAEAEAK--KKAAAEAKKKAAAEAKAAaaKAAAEAKAAAEKAAAAkaaeKAAAAKAAAEVDDLFGG 265
                         170       180
                  ....*....|....*....|...
gi 189083798  950 LGTSGGLPGQ------EGQAPSG 966
Cdd:PRK09510  266 LDSGKNAPKTgggakgNGAQGAG 288
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
795-1042 5.70e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  795 LRLQALHRSRKLHQQYRLARQRIIQFQARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRL 874
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  875 AEEEKLRKEMSAKKAKEEAERKHQERLAQLA-REDAERELKEKEAARRKKELLEQMERARHEPVnhSDMVDKMFGFLGTS 953
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLElLAELLEEAALLEAALAELLEELAEAAARLLLL--LEAEADYEGFLEGV 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  954 GGLPGQEGQAP-SGFEDLERGRREMVEEDLDAAL-----PLPDEDEEDLSEY-KFAKFA----ATYFQGTTTHSYTRRPL 1022
Cdd:COG1196   511 KAALLLAGLRGlAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAiEYLKAAkagrATFLPLDKIRARAALAA 590
                         250       260
                  ....*....|....*....|
gi 189083798 1023 KQPLLYHDDEGDQLAALAVW 1042
Cdd:COG1196   591 ALARGAIGAAVDLVASDLRE 610
growth_prot_Scy NF041483
polarized growth protein Scy;
857-941 6.21e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.67  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  857 QRLRAEylwrlEAEKMRLAEE--EKLRKEmsAKKAKEEAERKhQERLAQLAREDAERELKE--KEAARRKKELLEQMERA 932
Cdd:NF041483  971 ERLRAE-----AAETVGSAQQhaERIRTE--AERVKAEAAAE-AERLRTEAREEADRTLDEarKDANKRRSEAAEQADTL 1042

                  ....*....
gi 189083798  933 RHEPVNHSD 941
Cdd:NF041483 1043 ITEAAAEAD 1051
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
887-933 8.50e-05

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 47.56  E-value: 8.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 189083798  887 KKAKEEAERKHQERLaQLAREDAERELKEKEAARRKKELLEQMERAR 933
Cdd:PLN03086    6 RRAREKLEREQRERK-QRAKLKLERERKAKEEAAKQREAIEAAQRSR 51
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
874-933 1.10e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 44.39  E-value: 1.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189083798  874 LAEEEKLRKEmsAKKAKEEAERKHQE------RLAQLAREDAERELKE------KEAARRKKELLEQMERAR 933
Cdd:COG0711    40 LAEAERAKEE--AEAALAEYEEKLAEaraeaaEIIAEARKEAEAIAEEakaeaeAEAERIIAQAEAEIEQER 109
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
795-935 1.12e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.84  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   795 LRLQALHRSRKLHQQYRLARQRIIQFQARCRAYLVRKAFRHRlwAVLTVQayargmIARRLHQRLRAEYLWRLEAEKM-- 872
Cdd:pfam13868   34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYR--QELEEQ------IEEREQKRQEEYEEKLQEREQMde 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   873 ---RLAEEE------------KLRKEM--------SAKKAKEEAERKHQERLAQLAREDAERELK---EKEAARRKKE-- 924
Cdd:pfam13868  106 iveRIQEEDqaeaeeklekqrQLREEIdefneeqaEWKELEKEEEREEDERILEYLKEKAEREEEreaEREEIEEEKEre 185
                          170
                   ....*....|....
gi 189083798   925 ---LLEQMERARHE 935
Cdd:pfam13868  186 iarLRAQQEKAQDE 199
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
791-933 1.23e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  791 RLGFLRLQAlhRSRKLHQQYRLARQRIIQFQARCRAYLVRKAFrhrlwavltvqayargmIARRLHQRLRAEYLWRLEAE 870
Cdd:COG1196   273 RLELEELEL--ELEEAQAEEYELLAELARLEQDIARLEERRRE-----------------LEERLEELEEELAELEEELE 333
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083798  871 KMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERAR 933
Cdd:COG1196   334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
PTZ00121 PTZ00121
MAEBL; Provisional
784-935 1.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  784 RKNYGLMRLGFLRLQALHRSRKLHQQYRL-----ARQRIIQFQARCRAYLVRKAFRHRLWAVLTVQAYARGMiaRRLHQR 858
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEekkmkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK--KKAEEL 1652
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798  859 LRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAKEEaERKHQERLAQLAREDAE-RELKEKEAARRKKEllEQMERARHE 935
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKaEELKKKEAEEKKKA--EELKKAEEE 1727
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
802-932 1.60e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.38  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   802 RSRKLHQQYRLARQRIIQFQARCR--------AYLVRKAFRHRLWAVLTVQAyargmiARRLHQRLRAEYLWRLEAEKMR 873
Cdd:TIGR02794   69 RQKKLEQQAEEAEKQRAAEQARQKeleqraaaEKAAKQAEQAAKQAEEKQKQ------AEEAKAKQAAEAKAKAEAEAER 142
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 189083798   874 LAEEEKLRKEMSAKKAKEEAERKHQerlAQLAREDAERELKEKEAARRKKELLEQMERA 932
Cdd:TIGR02794  143 KAKEEAAKQAEEEAKAKAAAEAKKK---AEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA 198
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
582-638 1.91e-04

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: 44.26  E-value: 1.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798  582 HSSR-NKFIKQIFqaDVAmGAETrkrsptlssqFKRSLELLMRTLGACQPFFVRCIKP 638
Cdd:cd01363   126 NSSRfGKFIEILL--DIA-GFEI----------INESLNTLMNVLRATRPHFVRCISP 170
Caldesmon pfam02029
Caldesmon;
856-937 2.01e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 46.40  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   856 HQRLRAEylWRLEAEKMRLAEEE-----KLR-KEMSAKKAKEEAERKHQERLAQLARED-------AERELKEKEAARRK 922
Cdd:pfam02029  241 EVFLEAE--QKLEELRRRRQEKEseefeKLRqKQQEAELELEELKKKREERRKLLEEEEqrrkqeeAERKLREEEEKRRM 318
                           90
                   ....*....|....*
gi 189083798   923 KellEQMERARHEPV 937
Cdd:pfam02029  319 K---EEIERRRAEAA 330
growth_prot_Scy NF041483
polarized growth protein Scy;
857-935 2.05e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 46.74  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  857 QRLRAEyLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLARE-------------DAERELKE--KEAARR 921
Cdd:NF041483  527 ERTRAE-AERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEEltrlhteaeerltAAEEALADarAEAERI 605
                          90
                  ....*....|....
gi 189083798  922 KKELLEQMERARHE 935
Cdd:NF041483  606 RREAAEETERLRTE 619
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
796-943 2.17e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.80  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   796 RLQALHRSRKLHQQYRLARQriiqfQARCRAYLVR-KAFRHRLWAVL-TVQAYARGMIARRLH----QRLRAEYLWRLEA 869
Cdd:pfam15558   16 RHKEEQRMRELQQQAALAWE-----ELRRRDQKRQeTLERERRLLLQqSQEQWQAEKEQRKARlgreERRRADRREKQVI 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   870 EKM----RLAEE-EKLRKEMSAKKAKEEAERKH--------QERLAQLAREDAERELKEKEA-ARRKKELLEQMERARHE 935
Cdd:pfam15558   91 EKEsrwrEQAEDqENQRQEKLERARQEAEQRKQcqeqrlkeKEEELQALREQNSLQLQERLEeACHKRQLKEREEQKKVQ 170

                   ....*...
gi 189083798   936 PVNHSDMV 943
Cdd:pfam15558  171 ENNLSELL 178
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
857-931 2.22e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.19  E-value: 2.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083798  857 QRLRAEylwrlEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREdAERELK-EKEAARRKKELLEQMER 931
Cdd:COG3064    58 REAKAE-----AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE-AEAAAAaEKAAAAAEKEKAEEAKR 127
PTZ00121 PTZ00121
MAEBL; Provisional
804-924 2.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  804 RKLHQQYRLARQRIIQfQARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYlwRLEAEKMRLAEE----EK 879
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE--ARKADELKKAEEkkkaDE 1294
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 189083798  880 LRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKE 924
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE 1339
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
842-935 2.87e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  842 TVQAYARGMIARRLHQRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQL---------AREDAERE 912
Cdd:COG4717    38 TLLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeleeleaELEELREE 117
                          90       100
                  ....*....|....*....|...
gi 189083798  913 LKEKEAARRKKELLEQMERARHE 935
Cdd:COG4717   118 LEKLEKLLQLLPLYQELEALEAE 140
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
853-935 2.90e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 45.71  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   853 RRLHQ-------RLRAEylwrLEAEKMRLAEEEKLRKEM--SAKKAKEEAERKhQERLAQLAREDAER---ELKEKEAAR 920
Cdd:pfam15709  361 RRLQQeqleraeKMREE----LELEQQRRFEEIRLRKQRleEERQRQEEEERK-QRLQLQAAQERARQqqeEFRRKLQEL 435
                           90
                   ....*....|....*
gi 189083798   921 RKKELLEQMERARHE 935
Cdd:pfam15709  436 QRKKQQEEAERAEAE 450
SH3_PI3K_p85beta cd11909
Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol ...
1625-1671 3.23e-04

Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85beta binds CD28 and may be involved in the activation and differentiation of antigen-stimulated T cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212842  Cd Length: 74  Bit Score: 40.97  E-value: 3.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 189083798 1625 LSFAKGDLIILD-HDTGEQVMNS-GWANGINERTKQRGDFPTDSV-YVMP 1671
Cdd:cd11909    25 LTVSRAALQALGvKEGGEQCPQSiGWILGLNERTKQRGDFPGTYVeFLGP 74
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
866-931 3.24e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.81  E-value: 3.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083798  866 RLEAEKMRLAEEEKL---RKEMSA--KKAKEEAERKHQERLAQlAREDAERELK--EKEAARRKKELLEQMER 931
Cdd:cd06503    46 KEEAEELLAEYEEKLaeaRAEAQEiiEEARKEAEKIKEEILAE-AKEEAERILEqaKAEIEQEKEKALAELRK 117
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
877-935 3.67e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 3.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189083798  877 EEKLRKEM-SAKKAKEEAERKHQERLAQL--AREDAERELKE--KEAARRKKELLEQ--------MERARHE 935
Cdd:cd06503    32 EEKIAESLeEAEKAKEEAEELLAEYEEKLaeARAEAQEIIEEarKEAEKIKEEILAEakeeaeriLEQAKAE 103
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
1607-1663 3.69e-04

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 40.14  E-value: 3.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798 1607 YVVALQDNpnpAGEESGFLSFAKGDLIILDHDTgeqvmNSGWANGINERtKQRGDFP 1663
Cdd:cd00174     1 YARALYDY---EAQDDDELSFKKGDIITVLEKD-----DDGWWEGELNG-GREGLFP 48
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
866-935 3.78e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.21  E-value: 3.78e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083798   866 RLEAEKMRLAEEEKLRK-EMSAKKAKEEAERKHQ--ERLAQLARE-DAERELKEKEAarrkKELLEQMERARHE 935
Cdd:pfam20492    1 REEAEREKQELEERLKQyEEETKKAQEELEESEEtaEELEEERRQaEEEAERLEQKR----QEAEEEKERLEES 70
FERM_F1_PLEKHH2 cd17179
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
1257-1351 4.03e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 2 (PLEKHH2); PLEKHH2 is a novel podocyte protein downregulated in human focal segmental glomerulosclerosis. It is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. PLEKHH2 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PLEKHH2 is involved in matrix adhesion and actin dynamics. It directly interacts through its FERM domain with the focal adhesion protein Hic-5 and actin.


Pssm-ID: 340699  Cd Length: 103  Bit Score: 41.88  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1257 PIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKD--RFGFSLYIalfDKVSslGSGSDHVM-------DAISQCE 1327
Cdd:cd17179     1 PFSIPVHFMNGTYQVVGFDASTTVEEFLNTLNQDTGMRKpgQSGFALFT---DDPS--GKDLEHCLqgnikicDIISKWE 75
                          90       100
                  ....*....|....*....|....*.
gi 189083798 1328 QYAKEQ--GAQERNAPWRLFFRKEVF 1351
Cdd:cd17179    76 QASKEQhpGKCEGTRTVRLTYKNRLY 101
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
870-930 4.42e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 43.50  E-value: 4.42e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189083798   870 EKMRLAEEEKLRKEmSAKKAKEEAERKHQERLAQLAREDAER-----------ELKEKEAARRKKELLEQME 930
Cdd:pfam15927    1 ARLREEEEERLRAE-EEEAERLEEERREEEEEERLAAEQDRRaeeleelkhllEERKEALEKLRAEAREEAE 71
PTZ00121 PTZ00121
MAEBL; Provisional
852-937 6.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  852 ARRLHQRLRAEYLWRleAEKMRLAEEekLRKEMSAKKAkEEAERKHQERLAQLAR--EDAERELKEKEAARRKKELLEQM 929
Cdd:PTZ00121 1515 AKKAEEAKKADEAKK--AEEAKKADE--AKKAEEKKKA-DELKKAEELKKAEEKKkaEEAKKAEEDKNMALRKAEEAKKA 1589

                  ....*...
gi 189083798  930 ERARHEPV 937
Cdd:PTZ00121 1590 EEARIEEV 1597
growth_prot_Scy NF041483
polarized growth protein Scy;
796-941 6.30e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.20  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  796 RLQAlhrsrKLHQQYRLARQRIIQFQARCRAYLVRKAFRHRLWAVltvQAYARG-MIARRLHQRLRAEY---LWRLEAEK 871
Cdd:NF041483  116 RLQA-----ELHTEAVQRRQQLDQELAERRQTVESHVNENVAWAE---QLRARTeSQARRLLDESRAEAeqaLAAARAEA 187
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  872 MRLAEEEKLRKEMSAKKAKEEAERkhqerLAQLAREDAERELkeKEAARRKKELLEQMERARHEPVNHSD 941
Cdd:NF041483  188 ERLAEEARQRLGSEAESARAEAEA-----ILRRARKDAERLL--NAASTQAQEATDHAEQLRSSTAAESD 250
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
862-924 6.71e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 44.94  E-value: 6.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083798  862 EYlWRLEAEKMRLAEEEKlrkemsaKKAkEEAERKHQERLAQLAREDAERELKEKEAARRKKE 924
Cdd:PRK05035  429 QY-YRQAKAEIRAIEQEK-------KKA-EEAKARFEARQARLEREKAAREARHKKAAEARAA 482
SH3_PI3K_p85alpha cd11910
Src Homology 3 domain of the p85alpha regulatory subunit of Class IA Phosphatidylinositol ...
1625-1663 7.20e-04

Src Homology 3 domain of the p85alpha regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85alpha interacts with activated FGFR3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212843  Cd Length: 75  Bit Score: 40.27  E-value: 7.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 189083798 1625 LSFAKGDLIILDHDTGEQVMNS--GWANGINERTKQRGDFP 1663
Cdd:cd11910    26 LTVNKGSLLALGFSEGQEARPEeiGWLNGYNETTGERGDFP 66
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
866-932 7.24e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 42.37  E-value: 7.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083798   866 RLEAEKMRLAEEEKLRKEmsakKAKEEAERKHQErlaqlaredaERELKEKEaaRRKKELLEQMERA 932
Cdd:pfam11600   33 AEKEEKERLKEEAKAEKE----RAKEEARRKKEE----------EKELKEKE--RREKKEKDEKEKA 83
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
857-935 7.43e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 7.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   857 QRLRAEYLWRLEA--EKMRLAEEE-------KLRKEMSAKKAKEEAER---KHQE------RLAQLA------REDAERE 912
Cdd:pfam20492    5 EREKQELEERLKQyeEETKKAQEEleeseetAEELEEERRQAEEEAERleqKRQEaeeekeRLEESAemeaeeKEQLEAE 84
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 189083798   913 LKEKEA-------ARRKKE-----LLEQMERARHE 935
Cdd:pfam20492   85 LAEAQEeiarleeEVERKEeearrLQEELEEAREE 119
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
844-1006 8.65e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 43.13  E-value: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   844 QAYARGM-IARRLHQRLRAEYL----WRLEAEKMRLAEEEKLRKEMSAKKAKEE--AERKHQER------LAQLAREDAE 910
Cdd:pfam04012   43 QALAQTIaRQKQLERRLEQQTEqakkLEEKAQAALTKGNEELAREALAEKKSLEkqAEALETQLaqqrsaVEQLRKQLAA 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   911 RELKEKEAARRKKELLEQMERARHEpvnhsDMVDKMFGFLGTSGglpgqegqAPSGFEDLERGRREMvEEDLDAALPLPD 990
Cdd:pfam04012  123 LETKIQQLKAKKNLLKARLKAAKAQ-----EAVQTSLGSLSTSS--------ATDSFERIEEKIEER-EARADAAAELAS 188
                          170
                   ....*....|....*.
gi 189083798   991 EDEEDlseykfAKFAA 1006
Cdd:pfam04012  189 AVDLD------AKLEQ 198
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
850-935 9.76e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  850 MIARRLHQRLRAEYLWRlEAEKMrLAEEEKLRKEMSAKKAK----EEAERKHQERLAQLAREDAERELKEKEAARRKKEL 925
Cdd:PRK00409  521 LIASLEELERELEQKAE-EAEAL-LKEAEKLKEELEEKKEKlqeeEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
                          90
                  ....*....|
gi 189083798  926 LEQMERARHE 935
Cdd:PRK00409  599 GGYASVKAHE 608
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1604-1667 1.00e-03

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 39.06  E-value: 1.00e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083798   1604 RSKYVVALQDNPnpaGEESGFLSFAKGDLIILDHDTgeqvmNSGWANGINERtKQRGDFPTDSV 1667
Cdd:smart00326    1 EGPQVRALYDYT---AQDPDELSFKKGDIITVLEKS-----DDGWWKGRLGR-GKEGLFPSNYV 55
PTZ00121 PTZ00121
MAEBL; Provisional
858-935 1.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  858 RLRAEYLWRLEAEKMRLAEEekLRKEMSAKKAKEEAERKHQE--RLAQLAREDAERELKEKEAARRKKEL----LEQMER 931
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKK 1737

                  ....
gi 189083798  932 ARHE 935
Cdd:PTZ00121 1738 EAEE 1741
FERM_F1_PLEKHH1 cd17178
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
1257-1351 1.06e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 1 (PLEKHH1); PLEKHH1 is a homolog of Caenorhabditis elegans MAX-1 that has been implicated in motor neuron axon guidance. PLEKHH1 is critical in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH1 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340698  Cd Length: 106  Bit Score: 40.72  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1257 PIMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLK--DRFGFSLYIalfDKVSSLG-----SGSDHVMDAISQCEQY 1329
Cdd:cd17178     1 PFSIPVHFMNGTYQVVGFDGSTTVDEFLQTLNQETGMRkpSHSGFALFT---DDPSGKDlehclQGSVKICDVISKWEQA 77
                          90       100
                  ....*....|....*....|....
gi 189083798 1330 AKE--QGAQERNAPWRLFFRKEVF 1351
Cdd:cd17178    78 LKElhPGKYEGTRTVRLTYKSRLY 101
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
868-935 1.09e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.87  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  868 EAEKMRlAEEEKLRKEMSAKKAKE--EAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHE 935
Cdd:COG3064    56 EAREAK-AEAEQRAAELAAEAAKKlaEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEE 124
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
1359-1441 1.11e-03

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 40.72  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  1359 EDNVATNLIYQQVVRGVKFGEYRCEkEDDLAELASQQYFVDYG---------SEMILERllnlvptYIPDREITPLKTlE 1429
Cdd:pfam00373    7 QDEVTRHLLYLQAKDDILEGRLPCS-EEEALLLAALQLQAEFGdyqpsshtsEYLSLES-------FLPKQLLRKMKS-K 77
                           90
                   ....*....|..
gi 189083798  1430 KWAQLAIAAHKK 1441
Cdd:pfam00373   78 ELEKRVLEAHKN 89
growth_prot_Scy NF041483
polarized growth protein Scy;
804-933 1.12e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.43  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  804 RKLhQQYRLARQRIIQ----FQARCRAYLVRKAF--RHRLWAVL-----TVQAYARGMIArrLHQRLRAeylwRLEAEKM 872
Cdd:NF041483   94 REL-RDARAQTQRILQehaeHQARLQAELHTEAVqrRQQLDQELaerrqTVESHVNENVA--WAEQLRA----RTESQAR 166
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083798  873 RLAEEEKLRKEMSAKKAKEEAERkhqerlaqLAREDAERELKEKEAARRKKELLeqMERAR 933
Cdd:NF041483  167 RLLDESRAEAEQALAAARAEAER--------LAEEARQRLGSEAESARAEAEAI--LRRAR 217
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
766-809 1.22e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 41.34  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 189083798  766 KLKN-------AATLIQRHWRGHNCRKNYGlmrlgfLRLQALHRSRKLHQQ 809
Cdd:cd21759    36 KLKNkilyrreALIKIQKTVRGYLARKKHR------PRIKGLRKIRALEKQ 80
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
766-787 1.26e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 38.08  E-value: 1.26e-03
                            10        20
                    ....*....|....*....|..
gi 189083798    766 KLKNAATLIQRHWRGHNCRKNY 787
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
866-934 1.38e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 43.05  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189083798  866 RLEAEKMRL--AEEEKLRKEmsaKKAkeEAERKHQ----ERLAQLAREDAERELKEKEAARRKKELLEQMERARH 934
Cdd:cd03406   170 AMEAEKTKLliAEQHQKVVE---KEA--ETERKRAvieaEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLARE 239
SH3_BAIAP2L1 cd11913
Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1, ...
1615-1664 1.42e-03

Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1, also called Insulin Receptor Tyrosine Kinase Substrate (IRTKS); BAIAP2L1 or IRTKS is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. IRTKS mediates the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRTKS has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212846  Cd Length: 58  Bit Score: 38.74  E-value: 1.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 189083798 1615 PNPAGEESGFLSFAKGDLIIL----DHDtgeqvmnsGWANGINERTKQRGDFPT 1664
Cdd:cd11913     8 PHTAGNNKTLLSFAQGDVITLlipeEKD--------GWLYGEHDTTKARGWFPS 53
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
796-930 1.49e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  796 RLQALHRSRKLHQQYRLARQRIIQFQArCRAYLvrkafrhRLWAvltvqayargmiARRLHQRLRAEyLWRLEAEKMRL- 874
Cdd:COG4913   250 QIELLEPIRELAERYAAARERLAELEY-LRAAL-------RLWF------------AQRRLELLEAE-LEELRAELARLe 308
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083798  875 AEEEKLRKEMSAKKAK-EEAERKHQE----RLAQLARE--DAERELKEKEAARRK-KELLEQME 930
Cdd:COG4913   309 AELERLEARLDALREElDELEAQIRGnggdRLEQLEREieRLERELEERERRRARlEALLAALG 372
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
854-933 1.51e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   854 RLHQRLRAEYLWRLEAEKMRLAEE--EKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMER 931
Cdd:pfam13868  246 ELKERRLAEEAEREEEEFERMLRKqaEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325

                   ..
gi 189083798   932 AR 933
Cdd:pfam13868  326 ER 327
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
1471-1523 1.56e-03

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 39.67  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 189083798 1471 SRFYEAYKFSGPslpKNDVIVAVNWTGVYFVDEQE-QVLLELSFPEIMAVSSSR 1523
Cdd:cd00836     2 VEFFPVKDKSKK---GSPIILGVNPEGISVYDELTgQPLVLFPWPNIKKISFSG 52
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
874-933 1.59e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 40.88  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083798  874 LAEEEKLRKEMSAKKAK-----EEAERKHQERLAQlAREDAERELKE------KEAARRKKELLEQMERAR 933
Cdd:cd06503    39 LEEAEKAKEEAEELLAEyeeklAEARAEAQEIIEE-ARKEAEKIKEEilaeakEEAERILEQAKAEIEQEK 108
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
866-931 1.72e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.93  E-value: 1.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083798  866 RLEAEKMRLAEEEKL---RKEMSA--KKAKEEAERKHQERLAQlAREDAERELK--EKEAARRKKELLEQMER 931
Cdd:COG0711    47 KEEAEAALAEYEEKLaeaRAEAAEiiAEARKEAEAIAEEAKAE-AEAEAERIIAqaEAEIEQERAKALAELRA 118
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
851-932 1.81e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.32  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  851 IARRLHQRLRAEYLWRLEAEKMRLAEEEK---------LRKEMSAKKAKEEA-----ERKHQE--RLAQLAREDAERELK 914
Cdd:COG2268   216 IAQANREAEEAELEQEREIETARIAEAEAelakkkaeeRREAETARAEAEAAyeiaeANAEREvqRQLEIAEREREIELQ 295
                          90
                  ....*....|....*....
gi 189083798  915 EKEAARRKKELL-EQMERA 932
Cdd:COG2268   296 EKEAEREEAELEaDVRKPA 314
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
811-935 1.85e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  811 RLARQRII-----QFQARCRAYLVRKAFRHRLWAVLTVQAYARgmIARRLHQRLRAEYLWRLEAEKMRLAEEEKLRKEMS 885
Cdd:COG1196   204 PLERQAEKaeryrELKEELKELEAELLLLKLRELEAELEELEA--ELEELEAELEELEAELAELEAELEELRLELEELEL 281
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 189083798  886 AKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHE 935
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
868-935 1.91e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.21  E-value: 1.91e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798   868 EAEKMRLaEEEKLRKEmsaKKAKEEAERKHQERLAQLAREDAERelKEKEAARRKKELLEQMERARHE 935
Cdd:pfam11600   12 EKEKQRL-EKDKERLR---RQLKLEAEKEEKERLKEEAKAEKER--AKEEARRKKEEEKELKEKERRE 73
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
868-935 1.99e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.94  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  868 EAEKMRLAEEEKLRKEMSAKKAKEEAERK--------HQERLAQLAREDAERELKEKEAARRK-----KELLEQMERARH 934
Cdd:COG2268   250 KAEERREAETARAEAEAAYEIAEANAEREvqrqleiaEREREIELQEKEAEREEAELEADVRKpaeaeKQAAEAEAEAEA 329

                  .
gi 189083798  935 E 935
Cdd:COG2268   330 E 330
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
794-935 2.22e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   794 FLRLQALHRsRKLHQQYRLARQRIIQF----QARCRAY----LVRKAFRHRLWAVLTVQAYARgMIARRLHQRLRAEYLW 865
Cdd:pfam13868  135 FNEEQAEWK-ELEKEEEREEDERILEYlkekAEREEEReaerEEIEEEKEREIARLRAQQEKA-QDEKAERDELRAKLYQ 212
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   866 RLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHE 935
Cdd:pfam13868  213 EEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE 282
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
791-935 2.53e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  791 RLGFLRLQALH-RSRKLHQQYRLARQRIIQFQA------------RCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQ 857
Cdd:COG1196   228 ELLLLKLRELEaELEELEAELEELEAELEELEAelaeleaeleelRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189083798  858 RLRAEylwRLEAEKMRLAEEEKLRKEMSAKKAKEEAERkhQERLAQLAREDAERELKEKEAARRKKELLEQMERARHE 935
Cdd:COG1196   308 EERRR---ELEERLEELEEELAELEEELEELEEELEEL--EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
853-935 2.66e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   853 RRLHQRLRAEYLWRLEAEKMrlaEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERA 932
Cdd:pfam13868    9 RELNSKLLAAKCNKERDAQI---AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER 85

                   ...
gi 189083798   933 RHE 935
Cdd:pfam13868   86 EQK 88
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
867-935 2.67e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 2.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189083798  867 LEAEKMRLAEEekLRKEmsAKKAKEEAER------KHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHE 935
Cdd:COG2268   186 LDALGRRKIAE--IIRD--ARIAEAEAEReteiaiAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERRE 256
SH3_PI3K_p85 cd11776
Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; ...
1647-1663 2.80e-03

Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212710  Cd Length: 72  Bit Score: 38.26  E-value: 2.80e-03
                          10
                  ....*....|....*..
gi 189083798 1647 GWANGINERTKQRGDFP 1663
Cdd:cd11776    49 GWLEGKNERTGERGDFP 65
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
866-935 2.81e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 40.83  E-value: 2.81e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083798   866 RLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKE----LLEQMERARHE 935
Cdd:pfam11600   53 KEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEeekrLKEEEKRIKAE 126
SH3_Irsp53 cd11915
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known ...
1618-1663 2.85e-03

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 can also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRSp53 has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212848  Cd Length: 59  Bit Score: 38.07  E-value: 2.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 189083798 1618 AGEESGFLSFAKGDLIILDHDTGEqvmnSGWANGINERTKQRGDFP 1663
Cdd:cd11915    11 AGDNSTLLSFKEGDYITLLVPEAR----DGWHYGECEKTKMRGWFP 52
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
1619-1663 2.93e-03

Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212724 [Multi-domain]  Cd Length: 64  Bit Score: 38.08  E-value: 2.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 189083798 1619 GEESGFLSFAKGDLI-ILDHDTGEQvMNSGWANGINERTKQRGDFP 1663
Cdd:cd11790    13 AEDTDELTFEKGDVIlVIPFDDPEE-QDEGWLMGVKESTGCRGVFP 57
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
866-928 3.05e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.14  E-value: 3.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189083798   866 RLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQL-AREDAERELKEKEAARRKKELLEQ 928
Cdd:TIGR02794   56 QQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELeQRAAAEKAAKQAEQAAKQAEEKQK 119
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
768-787 3.55e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.53  E-value: 3.55e-03
                           10        20
                   ....*....|....*....|
gi 189083798   768 KNAATLIQRHWRGHNCRKNY 787
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRY 20
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
859-922 3.73e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 37.92  E-value: 3.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189083798  859 LRAEY---LWRLEAEKMRLAEEEklrkemsaKKAKEE------AERKHQERLAQLAREDAERELKEKEAARRK 922
Cdd:cd22265     7 LRQEYeeeISKLEAERRALEEEE--------NRASEEyiqkllAEEEEEEKLAEERRRAEEEQLKEDEELARK 71
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
1625-1663 3.82e-03

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 37.69  E-value: 3.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 189083798 1625 LSFAKGDLIILdhdTGEQVMNsGWANGINERTKQRGDFP 1663
Cdd:cd11779    17 LSFEEGDVITL---LGPEPRD-GWHYGENERSGRRGWFP 51
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
882-934 4.59e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 41.50  E-value: 4.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 189083798   882 KEMSAKKAKEEAERKHQERLAQLAREDAER-ELKEKEAARRKKELLEQMERARH 934
Cdd:pfam02841  204 KAIEAERAKAEAAEAEQELLREKQKEEEQMmEAQERSYQEHVKQLIEKMEAERE 257
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
852-933 5.71e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 40.31  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  852 ARRLHQRLRAEYlwRLEAEKMRLAEEEKLRKEMSA--KKAKEEAERKHQERLAQlaredAERELKeKEAARRKKELLEQ- 928
Cdd:COG1390    15 AEAEAEEILEEA--EEEAEKILEEAEEEAEEIKEEilEKAEREAEREKRRIISS-----AELEAR-KELLEAKEELIEEv 86

                  ....*
gi 189083798  929 MERAR 933
Cdd:COG1390    87 FEEAL 91
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
846-932 6.14e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 39.39  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798   846 YARGM--------IARRLHQRLRAEYLWRleAEKMRLAEEEKLRKEMSAKKAKEEAERkhQERLAQLAREDAE------R 911
Cdd:pfam15236   31 FLRGQnalldpaqLEERERKRQKALEHQN--AIKKQLEEKERQKKLEEERRRQEEQEE--EERLRREREEEQKqfeeerR 106
                           90       100
                   ....*....|....*....|...
gi 189083798   912 ELKEKEAARRKK--ELLEQMERA 932
Cdd:pfam15236  107 KQKEKEEAMTRKtqALLQAMQKA 129
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
859-934 7.66e-03

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 39.46  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  859 LRAEYLwR--LEAEKMRLAEEEKLRKEMSAKKAKEeaerkHQERLAQLARED----------------------AERE-L 913
Cdd:cd23703    58 LRRQNL-RegLRELEERKLKTEELRAKRSERKQAE-----RERALNAPEREDerltlptiesallgplmrvrtdPEREeR 131
                          90       100
                  ....*....|....*....|.
gi 189083798  914 KEKEAARRKKELLEQMERARH 934
Cdd:cd23703   132 AAKRRANREAKELAKKEARAD 152
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
796-940 7.77e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  796 RLQALH-RSRKLHQQYRLARQRIIQFQ---ARCRAYLVRKAFRHRLWAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEK 871
Cdd:COG4913   700 ELEELEeELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798  872 MRLA-EEEKLRKEMSAKKAK-----------EEAERKHQERLAQLAREDAERelKEKEAARRKKE--------LLEQMER 931
Cdd:COG4913   780 ARLNrAEEELERAMRAFNREwpaetadldadLESLPEYLALLDRLEEDGLPE--YEERFKELLNEnsiefvadLLSKLRR 857
                         170
                  ....*....|....*
gi 189083798  932 ARHE------PVNHS 940
Cdd:COG4913   858 AIREikeridPLNDS 872
FERM_F1_DdMyo7_like cd17208
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium ...
1902-1998 9.26e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins; DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340728  Cd Length: 98  Bit Score: 37.62  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083798 1902 IFHKVYFPDDTDEAFEVESSTKAKDFCQNIATRL-LLKSSEGFSLFVKIADKVLSVPENDFFFDFVRHLTDWIKKARpik 1980
Cdd:cd17208     4 IVARFYFLDGQFKALEFDSAATAAEVLEQLKQKIgLRSTADGFALYEVFGGIERAILPEEKVADVLSKWEKLQRTMA--- 80
                          90
                  ....*....|....*...
gi 189083798 1981 dGIVPSLTYQVFFMKKLW 1998
Cdd:cd17208    81 -SCAAQQAVKFVFKKRLF 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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