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Database: UniProt
Entry: A0A2Y9M5C9_DELLE
LinkDB: A0A2Y9M5C9_DELLE
Original site: A0A2Y9M5C9_DELLE 
ID   A0A2Y9M5C9_DELLE        Unreviewed;      2168 AA.
AC   A0A2Y9M5C9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Unconventional myosin-IXb isoform X4 {ECO:0000313|RefSeq:XP_022414397.1};
GN   Name=MYO9B {ECO:0000313|RefSeq:XP_022414397.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022414397.1};
RN   [1] {ECO:0000313|RefSeq:XP_022414397.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022414397.1};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_022414397.1; XM_022558689.2.
DR   Proteomes; UP000248483; 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:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR   GO; GO:0030048; P:actin filament-based movement; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR   CDD; cd20884; C1_Myosin-IXb; 1.
DR   CDD; cd01385; MYSc_Myo9; 1.
DR   CDD; cd04407; RhoGAP_myosin_IXB; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 2.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR046987; Myo9.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036023; MYSc_Myo9.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR028557; RhoGAP_myosin_IXB.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR46184:SF2; UNCONVENTIONAL MYOSIN-IXB; 1.
DR   PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 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}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000248483};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          15..118
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          150..988
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1656..1705
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1727..1912
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          870..892
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1081..1326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1339..1435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1480..1508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1627..1650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1944..1971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1991..2168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1372..1402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1482..1508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1991..2008
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2036..2054
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2135..2149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         243..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2168 AA;  244700 MW;  FB29D705447167EB CRC64;
     MSVKEAGSSG HRGQAAYHLH IYPQLATSES QTPCQASCRV TATKDSTTSD VIQDAITSLQ
     LDGSKRYVLV EVKETGGEEW VLDANDSPVH RVLLWPRRAQ DEHPQEDGYY FLLQERNADG
     TIKYVHMQLV SQATATRRLV ERGLLPRPQA DFDDLCNLPE LTEENLLKNL KHRFLQQKIY
     TYAGSILVAV NPFKFLPIYN PKYVKMYENQ QLGKLEPHVF ALADVAYYAM LRKHVNQCIV
     ISGESGSGKT QSTNFLIHCL TALSQKGYAS GVERTILGAG PVLEAFGNAK TAHNNNSSRF
     GKFIQVNYLE SGIVRGAVVE KYLLEKSRLV SQEKDERNYH VFYYLLLGVS EEERQEFQLK
     QPEDYFYLNQ HNLKIEDGED LKHDFERLKQ AMEMVGFLPA TKKQIFSILS AILYLGNVTY
     KKKATGRDEG LEVGPPAALD TLSQLLKVKR EILVEVLTKR KTVTSNDKLI LPYSLSEAIT
     ARDSMAKSLY SALFDWIVLR INHALLNKKD MEESVSCLSI GVLDIFGFED FERNSFEQFC
     INYANEQLQY YFNQHIFKLE QEEYQSEGIS WHNIDYTDNV GCIHLISKKP TGLFYLLDEE
     SNFPHATSQT LLAKFKQQHE DNRYFLGTPV MEPAFIIQHF AGKVKYQIKD FREKNMDYMR
     PDIVALLRGS DSSYVRELIG MDPVAVFRWA VLRAAIQAMA VLREAGRLRA ERAEKAAAGL
     GSSGARGHLG ELQRGASTPS EKLYRCSMLD FSFDGSEEFD INAFEDIIAF YESKNDLHDQ
     IIKTIKGLPW QGDDPRRLLQ SLSRLQKPRT FILKSKGIKQ KQIIPKNLLD SKSLKLIISM
     TLHDRTTKSL LHLHKKKKPP SISAQFQTSL NKLLEALGKA EPFFIRCIRS NAEKKELCFD
     DELVLQQLRY TGMLETVRIR RSGYSAKYTF QDFTEQFQVL LPKNARPCRE VISALLEKMD
     IDKRSYQIGK TKVFLKETER QALQETLHRE VVRKILLLQS WFRMVLERRH FLQMRRAAVT
     IQACWRSYRV RRALERTQAA VYLQAAWRGS RQRAAYQLQR QTIIRLQSLC RGHLQRRSFS
     QMVAEKQKAA EKEREAQRAA KQETAETGPG WAAAQEPSQG PEPSKDGEHL ELEPEVWPSD
     GSPVESSQPE KAPPAQKNAA ESHEKVPSSR EKRESRRQRG LEHVKLQNKH IESCKEEHAL
     REPSGRAVPG PQESLAEDRK EDREDESPRD ARTDTGMAPP EKQLEEPPQP TPGSLVSTEA
     QGGSPRPGHV ERPTSLALDS RVGVPAPGAT PETPKDKSKL GVGPRAQDRP ESPGGSTQIQ
     RYRDPDAERL ASAVELWRGK KLMTAGPSTM LSQSLDLSER HRAEGVTLTP TKERRISLST
     SDVSKLLSSS SQTKTQPPAE TMDGEPSTKK LAIQKKKSGD ASLGTDAGLS PGSVDSKSTF
     KRLFLHKNKD KKYSLEGTEE TENTVPGQVV LEAAAMKKNL EAPSSHQHRH ATGEKHAKEP
     GGKGKKNRNL KIGKITVSEK WRESVFRKIT NANELKYLDE FLLNKINDLR SQKTPIESLF
     IEATEKFRSN LKTMYSVPNG KIHVGYKDLM ENYQIVVSNL AAERGEKDTN LVLNLFQSLL
     DEFTRGHTKN DFEPPKQSKA QKKKRKQERA VQQHNGHVFA SYQVSIPQSC EQCLSYIWLM
     DKALLCSVCK MTCHKKCVHK IQTYCSYTSG KKIEPGTEPG HFGVCVDSLT SDKVSVPIVL
     EKLLEHVEMH GLYTEGLYRK SGAANRTREL RQALQTDPTA VKLENFPIHA ITGVLKQWLR
     ELPEPLMTFA QYGDFLRAVE LPEKQEQLAA IYAVLEHLPE ANHNSLERLI FHLVKVALLE
     DVNRMSPSAL AIIFAPCLLR CPDNSDPLTS MKDVLKITTC VEMLIKEQMR KYKVKMEEIT
     QLEAAESIAF RRLSLLRQNA IKNPKTRMSS SGGLEELGVL PEEEVAGGEE DREKEILIER
     IQSIKEEKED ITYRLPELDP RGSDEENLDS ETSASTESLL EERAGRGASE GPLAPALPCP
     SAPTPSPLPE AAAPPRRRPS SFMTVRVKTP RRTPIMPTAN IKLPPGLPSY LPGRAPGAQE
     AATPVRRREP PARRPDQVHS VYITPGTHLP TQGPQEPLDK DDRPPGTKRR YSDPPTYCLP
     PASGQANG
//
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