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Database: UniProt
Entry: A0A2K6RVK5_RHIRO
LinkDB: A0A2K6RVK5_RHIRO
Original site: A0A2K6RVK5_RHIRO 
ID   A0A2K6RVK5_RHIRO        Unreviewed;      2565 AA.
AC   A0A2K6RVK5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Myosin XVIIIB {ECO:0000313|Ensembl:ENSRROP00000045059.1};
GN   Name=MYO18B {ECO:0000313|Ensembl:ENSRROP00000045059.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000045059.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000045059.1}
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   RefSeq; XP_010373893.1; XM_010375591.1.
DR   STRING; 61622.ENSRROP00000045059; -.
DR   Ensembl; ENSRROT00000069579.1; ENSRROP00000045059.1; ENSRROG00000045452.1.
DR   Ensembl; ENSRROT00000069582.1; ENSRROP00000045062.1; ENSRROG00000045452.1.
DR   GeneTree; ENSGT00940000158067; -.
DR   OMA; CISSEGP; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
DR   GO; GO:0016461; C:unconventional myosin complex; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
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:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   CDD; cd01386; MYSc_Myo18; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
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; 4.10.270.10; Myosin, subunit A; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036064; MYSc_Myo18.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF8; UNCONVENTIONAL MYOSIN-XVIIIB; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000233200}.
FT   DOMAIN          571..1333
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          12..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2139..2191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2220..2245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2357..2379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2448..2556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1401..1668
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1700..1774
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1889..1958
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2021..2083
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        41..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2139..2156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2170..2185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2224..2240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2357..2372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2503..2519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2537..2556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         660..667
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2565 AA;  285447 MW;  79DDCE2F9A235A73 CRC64;
     MAISSRLALW EQKIREEDKS PPPSSPPPLF SVIPGGFIKQ LVRETEKEAK EARQRKQLAL
     AAPERETPEI SISEPNSKSS SGTRSGSQQI SQDNQSSSPG SSDILSKESE GTGSPNPERM
     TSINGEKAQE LGSTATPAKK TLPFKRGMRR GDVLLMVAKL DLDSAKPERT HPHDTSPCKT
     PPPVTDTGKE RKGETSRAPC GPQASTEILA PKAEKTRTGG LGDAGQGTVA LKKGEKGQSI
     VGKGGGTPKT KELKEAEPQG KDRQGTRPQA QGPSEGVRPG KAEKEGGEPT SPVEKENVSK
     NVGSEGKHIG PHIPGRKWGG FLGRRSKWDG PQNKKDKEGV LLSKAEKTGE PQTQTEKKSQ
     MQGELGDDLR MGEKAGELRS MTGKAGESWD KKEKIGQPQG KSGKAGEARS QTEKGCEAPK
     EVSTMVESPV AAGKGGWSGR SGQEAEGPCS REDVGSGALE TELEGPSQPA LEKDAERPRI
     QKENQDGPAP QEAGKGGQSR NSEQAPEDRW YEAEKVWLAQ KDGFTLATVL KPDEGTADLP
     AGRVRLCIDA DKSITEVDEE HVHRANPPEL DQAEDLASLI SVNESSVLNT LLQRYRAQRP
     HTCTGPDLIV LQPRGPSVPS AGKVPKGRWD GLPAHIGSMA QRAYWALLNQ RRDQSIVALG
     RSGAGKTACC EQVLEHLVGM AGSMDGKVSV EKIRATFTVL WAFGSVSMAH SCSATRFSMV
     MSLDFNATGR ITAAQLQTML LEKSRVARQP EGESNFQVFS QMLAGLDLDL RMELNLHQMA
     DSSSFGMGMW SKPEDKQKAA AAFAQLQGAM ETLGISESEQ RAIWRVLAAI YHLGAAGACK
     VGRKQFMRFE WANYAAEALG CEYEELNTAT FKHHLRQIIQ QMTFGPSQRD LEDEETSSGL
     KMTGVECVEG MASGLYQELF AAVVSLINRS FSSHHLSMAS IMVVDSPGFQ NPRHQGKDRA
     ATFEELCHNY AHERLQLLFY QRTFVSTLQR YREEGVPVQF DLPDLSPGTT VAAVDHNPSQ
     VRLPAGGGAQ DAKGLFWVLD EEVRVEGSSD SVVLERLCAA FEKKGAGTEG SSALRTCEQP
     LQCEIFHQLG WDPVRYDLTG WLHRAKPNLS ALDAPQVLQQ SKREELRSLF QSRAKLPPVC
     QAVAGLEGTS QQALQRNRMV RRTFASSLAA VRRKAPCSQI KLQMDALTSM IKRSRLHFIH
     CLVLNPVVES RSEQESPTPP QPGRDKPGAD APLALDIPAL RVQLAGFHIL EALRLHRTGY
     ADNMGLTHFR RQFQVLDPPL LKKLMSTSEG IDERKAVEEL LETLDLEKKA VALGHSQVFL
     KAGVISRLER QREKLVSQSI VLFQAACKGF LSRQEFKKLK IRRLAAQCIQ KNVAMFLAVK
     DWPWWQLLGS LRPLLSATIG NEQLRAKEEE LTTLRRKLEK SEKLRNELRQ NTDLLESKIA
     DLTTELADER FKGDVACQVL ESERAERLQA FREVQELKSK HEQVQKKLGD VNKQLEEAQQ
     KIQLNDLERN PAGGADEWQM RFDCAQMENE FLRKRLQQCE ERLDSELTAR KELEQKLGEL
     QSAYDGAKKM AHQLKRKCHH LTCDLEDTRV LLENQQSRNH ELEKKQKKFD LQLAQALGES
     VFEKGLREKV TQENTSVRWE LGQLQQQLKQ KEQEALQLKQ EVEMLQDHKW ELLGSPSLGE
     NCIAGLKERL WKLESSALEQ QKVQSQQENT IKQLEQLRQR FELEIERMKQ IHQKDREDQE
     EELEDVRQSC QKRLRQLEMQ LEQEYEEKQM VLHEKQDLEG LIGTLCDQIG HRDFDVEKRL
     RRDLRRTHAL LSDVQLLLGT MEDGKTSVSK EELEKVHSQL EQSEAKCEEA LKTQKVLTAD
     LESMHSELEN MTRNKSLVDE QLYRLQFEKT DLLKRIDEDQ DDLNELMQKH KDLIAQSAAD
     IGQIQELQLQ LEEAKKEKHK LQEQLQVAQM RIEYLEQSTV DRAIVSRQEA VICDLENKTE
     FQKVQIKRFE VLVIRLRDSL IKMGEELSQA ATSESQQRES SQYYQRRLEE LKADMEELVQ
     REAEASRRCM ELEKYVEELG AVRQTLQTDL ETSIRRIADL QAALEEVASS DSDTESVQTA
     VDCGSSGRKE MDNVSILSSQ PEGSLQSWLS CTLSMATDTM RTPSRQSATS SRILSPRINE
     EAGDAERTQS ALSRAWSTDV RSKTSGDKPV SPHFVRRQKY CHFGDGEGLA VQRKSAERLE
     AASSPLASRS TNTSPLSREK LPSPSAALSE FVEGLRRKRA QRGQGSTLGL EDWPTLPIYL
     TTGASTLRRG RAGSDKGNLS LRVGAKSPLE IEGAAGGLLR STSLKCISSD GVGGTTLLPE
     KAKTRFSSCE SLLESRPSMG RKLSSPTTPR DMLLSPTLRP RRRCLESSVD DAGCPDLGKE
     PLVFQNRQFA HLMEEPLGSD PFSWKLPSLD YERKTKVDFD DFLPAIRKPQ MPTSLAGAAK
     DGQDGSQRSS VHFETEEADR SFLSGIKTIL KKSPEPKEDP AHLSDSSSSS SSIVSFKSAD
     SIKSRPGIQR LAGDGGEGTS PEHREPGAGR KDDDVTSIMK KYLQK
//
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