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Database: UniProt
Entry: A0A3Q1FHC1_9TELE
LinkDB: A0A3Q1FHC1_9TELE
Original site: A0A3Q1FHC1_9TELE 
ID   A0A3Q1FHC1_9TELE        Unreviewed;      2084 AA.
AC   A0A3Q1FHC1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Unconventional myosin-VIIb-like {ECO:0000313|Ensembl:ENSAPOP00000015287.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000015287.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000015287.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   Ensembl; ENSAPOT00000033165.1; ENSAPOP00000015287.1; ENSAPOG00000019103.1.
DR   GeneTree; ENSGT00940000157247; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd17092; FERM1_F1_Myosin-VII; 1.
DR   CDD; cd17093; FERM2_F1_Myosin-VII; 1.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13198; FERM_C1_MyoVII; 1.
DR   CDD; cd13199; FERM_C2_MyoVII; 1.
DR   CDD; cd01381; MYSc_Myo7; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 1.20.80.10; -; 3.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 1.25.40.530; MyTH4 domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR041793; MyoVII_FERM_C1.
DR   InterPro; IPR041794; MyoVII_FERM_C2.
DR   InterPro; IPR036106; MYSc_Myo7.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR   PANTHER; PTHR22692:SF24; UNCONVENTIONAL MYOSIN-VIIB ISOFORM X1; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 2.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 2.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 2.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51016; MYTH4; 2.
DR   PROSITE; PS01179; PID; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..2084
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018641741"
FT   DOMAIN          77..741
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1003..1205
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          1612..1762
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          1768..2072
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          1996..2025
FT                   /note="PID"
FT                   /evidence="ECO:0000259|PROSITE:PS01179"
FT   REGION          629..651
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2084 AA;  239928 MW;  8CF740EC8D6A6E6C CRC64;
     MKLQIPWSKF GFAAFTLIIL PLGDFVWVDS GAGVPLGAEV KVTDTGQLRL IDDEGKEHKI
     NKKNEGSIRP MHPTSVKGVD DMISIGDLNE AGLLRNLLVR HKEGIIYTYT GSILVAVNPY
     QLLPLYTTDH VHMYTDRRLG ELPPHVFALA DACFFNMRRN KKNQCCVISG ESGAGKTEST
     KLMLQFLAAV SGQHSWIEQQ ILEANPILEA FGNAKTVRND NSSRFGKYID VNFTKGGAIE
     GARVDQYLLE KSRVCRQAPE ERNYHIFYYM LMGMPADQKK ILSLGSAAEY KYLTMGNCTR
     CEGRDDVKEF AHFRAALKIL MFTENDSWEI CKLLAAVLHI GNVEFEGTIV NNLEGCEIHR
     SSHFDMACQL LEVDPNALDK SLTQRSFTTA RESVIKGLTS AQALDGRDAF VKGIYGRLFI
     WVVDKINSAI YKPPEDENEV RPSIGLLDIF GFENFNINSF EQLCINFANE QLQQFFVKHV
     FKLEQEEYSR ENIVWKHIDY QDNQRTLDVL AVKPLNMLSL IDEESSFPKG TDSTMLQKMN
     QLHGKGDIYI PPKNNYETQF GIQHFAGVVY YDSEGFLEKN RDTLSLDLIQ LVETSGNKLL
     KQAFHNELST GSNTIKSMPT LVGQFRQSLD ALMKALTACQ PYFIRCIKPN DFKKPMLFDR
     ELVMRQLRYS GMMETIRIRK AGYPVRYTFD EFLNRYRVLL KKKCCESICE SMLSGKGDWK
     TGKTKIFLKD FHDTMLEVER IKELNHKALL IQKVMRGFKF RREFLRKRAA AIMIQKHWRG
     HKGRKLYKVV QLGFARLQAQ VRSRQLHFQY KRQREAALVL QAQIRGYLAR KDWKRKRDAA
     ILLQAQTRGM LARKALKKMK RDVTNWNSLR SQKFINDNIQ NMYLSAKEKE EEQRLALQRQ
     KHLEEVLRKK REEEEKAQSA AISAEEIVDD IFGFLPSIVG GQEGQAPVGF ENLEGKRRTF
     EEIDIDDIPM EEDLSKDDYD DLDEYSFSKF ASMYFQGAAT PTHIRQRLLQ PLLYHEDEGD
     ILASLTVWWI ILRFMGDLPE PKKQVNVQAA SRREQFMPQE LVSRADRRFS NMHVCLVLCL
     LYNTDPDVMI GEGPTLDRPL TSLEKLHIIV GYAIVRRDLR DEIYCQICKQ LQDNKNRNSY
     FRGWILMSLC LGVFPPTEPF QKYLQSFIRS APRGYASYCA NRLRRTVMNG MRGEPPSWLE
     LQATKTLQPM IVTVTLLDRR SINLPVDSAT TSREICQLLA SKVKLIDTFG FSLYVALYEK
     VWALGSGREH VMDAISQCEQ EVKKRGGQEQ HAPWRLLLRK EIFTPWHNCK EDKISTDLIY
     RQIIHGLKFG EYQTEKVEAV QDCINNRLLE AKSEAKWTQM ISTAHAQVKK ADSVKAEMVD
     YAREKWPIFF SRFFEVTKLS GPLPKSKFIV AINWTGITFL DEREKRLLEL SFPEVTAVNS
     ISQGKSSEQT VSLLTLKGDF TLTGSTVEDM SELITMFLSG LKERSRYAVA LKDVDRGPSK
     GELIILIKDD EFSEQRGWVK GQRENLKHTG AVPIEAILIL PTLSKPSNEV MSLLTLTPNQ
     RKTILQTMQK ETATMERMAP FSLKEFSHQY FRYLEMLSVI SRNAAPERLW VSSREPIRQP
     LLMKLVGNSE FSPKACLTFT DILYTRYMGD YPTRQIQSPL ELTDQIFGPA TQHEALRDEI
     YCQIMKQMTN NNNRFSMEQG WQLLWLCCGL FPPSQALLKH AQRFLESRRR MPMASDCLQR
     LQSSLRYPRK FPPHQVEVDA IQQNSTQIFH KIHFPNDTDE IFEVSTSTRI RDLIQSISKK
     LGLASADGFS IFVKTHDKVL SLNDTDYFFD SLRQITDWSK RAKRIRDGGG PLNISYLVFF
     MRKLWFNVIP GRDTEADLIF HFPQEMPKYL RGFHVCTKED MINIAGLLFR VKVGSDKSQV
     AMIPKMIKDL VPADQLKAMS ENEWKKGIAA SYNKYAGFTV EEAKVAFLKA ICRWPTFGCA
     FFEVKQTSEQ NFPDIVRISI SKQGVTVINP KTKDVLATHP FNRIANWSSG STYFHMTVGN
     LVKGNKFLCE TSLGYKMDDL IASYVNMYNR ERRAMQTRNQ RFDM
//
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