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Database: UniProt
Entry: A0A3P9BVC1_9CICH
LinkDB: A0A3P9BVC1_9CICH
Original site: A0A3P9BVC1_9CICH 
ID   A0A3P9BVC1_9CICH        Unreviewed;      1069 AA.
AC   A0A3P9BVC1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Unconventional myosin-Ie {ECO:0000313|Ensembl:ENSMZEP00005013586.1};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005013586.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005013586.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   AlphaFoldDB; A0A3P9BVC1; -.
DR   Ensembl; ENSMZET00005014045.1; ENSMZEP00005013586.1; ENSMZEG00005010166.1.
DR   GeneTree; ENSGT00940000165572; -.
DR   Proteomes; UP000265160; Unplaced.
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; cd01378; MYSc_Myo1; 1.
DR   CDD; cd11827; SH3_MyoIe_If_like; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 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; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR035507; Ie/If_SH3.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR010926; Myosin_TH1.
DR   InterPro; IPR036072; MYSc_Myo1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF747; ZGC:64042; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF06017; Myosin_TH1; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS51757; TH1; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   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:UP000265160};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          17..690
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          728..920
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1012..1069
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          567..589
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          917..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1004
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1069 AA;  122751 MW;  1FB5F79CEE06A952 CRC64;
     QGSKERYHWQ AQNVKVSGVD DMVLLSKINE DAITDNLKKR YMDDYIFTYI GPVLISVNPF
     KQLPYFTERE VELYQGAAQY ENPPHIYALA DNMYRNMMID SENQCVIISG ESGAGKTVAA
     KYIMSYVSKV SGGGDKVQHV KDIILQSNPL LEAFGNAKTV RNNNSSRFGK YFEIQFSRGG
     APDGGKISNF LLEKSRVVSQ NQGERNFHIY YQLLGGATTE QRENLGVTTP DYYNYLNQTG
     TYTVEDVNDK KEFSDTMEAM SVVGLSLEDQ DSVLQLVAGI LHLGNISFRE ENNYAVVESQ
     NFLAFPAYLL GISQDGLCSK LTSRIMDSKW GGKTESISVT LNTEQACFSR DALSKALYTR
     LFDFLVDCIN KAMQKEQEEL NIGVLDIYGF EIFQQNGFEQ FCINFVNEKL QQIFIELTLK
     AEQEEYVQEG IKWTPIEYFN NKVVCDLIES KLNPPGIMSI LDDVCATMHA KGEGADQTLL
     QKLQGQIGSH EHFSSWNKGF IVHHYAGKVS YDVSGFCERN RDVLFNDIIE LMQSSEFPFI
     RALFPENLEA EKRGRPTTAS SKIKKQANSL VQTLMKCTPH YIRCIKPNET KRSRDWEENR
     VRHQVEYLGL RENIRVRRAG YAYRRVFNKF LQRYAILTKE SWPQWRGDER QGVLHLLNSV
     NMDQDQFQLG KTKVFIKAPE SLFLLEEMRE RKYNGYARVI QKAWRKHVAV RKYVKMREEA
     SDVVLNKKER RRNSINRNFV GDYIGTDNHP EIRQFVGRRE RIDFADVVVK YDRRFRSVKR
     DLILTPKFLY MIGREKVKHG PDKGQIQEVL KRKIEINKIQ SVSLSTLQDD FFIIHEEEYD
     SVLQSVFKTE FLSLLVKRYE DKTQRKLPLK FNNLLEFKVK KGGWGPFSSS GSRQIQFQVG
     QGDEAVLKPS GKVLQVSIGP GLPKHSPSRS RGSGALKEGS AYSRGSLLRQ QSSMEQPTLP
     RLQNQRRHDS RPHQNQDMGF MDVPDQGAAG VHRRRSKEVK PPPGAGRPKP KPRTPHCRAL
     YAYDAQDTDE LSFNAEDLIE IVTEDPSGWW FGRLRGREGM FPGNYVEKI
//
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