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Database: UniProt
Entry: A0A2C9KA94_BIOGL
LinkDB: A0A2C9KA94_BIOGL
Original site: A0A2C9KA94_BIOGL 
ID   A0A2C9KA94_BIOGL        Unreviewed;      2093 AA.
AC   A0A2C9KA94;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-SEP-2023, entry version 32.
DE   RecName: Full=Unconventional myosin-IXb {ECO:0008006|Google:ProtNLM};
GN   Name=106064649 {ECO:0000313|EnsemblMetazoa:BGLB016873-PF};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB016873-PF, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB016873-PF}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB016873-PF};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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_013078701.1; XM_013223247.1.
DR   EnsemblMetazoa; BGLB016873-RF; BGLB016873-PF; BGLB016873.
DR   VEuPathDB; VectorBase:BGLB016873; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000076420; Unassembled WGS sequence.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd20818; C1_Myosin-IX; 1.
DR   CDD; cd01385; MYSc_Myo9; 1.
DR   CDD; cd22265; UDM1_RNF168; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 2.
DR   Gene3D; 3.30.60.20; -; 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; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR46184:SF5; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR   PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR   Pfam; PF00612; IQ; 3.
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; 2.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          20..126
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          156..977
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1613..1662
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1679..1867
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          858..880
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1089..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1133..1243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1272..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1390..1409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1422..1458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1582..1605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1895..1921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2000..2023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1133..1156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1277..1298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1394..1408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1895..1916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2000..2016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         249..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2093 AA;  240427 MW;  B383214ACAD0BD92 CRC64;
     MAGHEFKPSN VQLIRRLSMD SYMVRVYAGP LNEEVESVAI EADKGTTAED VVGLACRKLR
     LGGGDTKKHY ELAEVFSSGG QLCKERRLDS TESPVGLQLL WPKPNEIEPG KGLFDGYRFY
     LRKRDPEVQP GGWVVTNQSA VDSFLMAFLT QPLAGKEFPD LCSLPDLNEK TLLYNLKSRF
     NQKNIYTYVG SILIAVNPFK FFPIYNPKYV SMYQNKRLGE LPPHIFAVAD AAYHSMLREK
     QNQCIVISGE SGSGKTESTN LLLHHLTALS HKGLHGSGVE QTILGAGPVL EAFGNAKTVH
     NNNSSRFGKF IQVNYKQNGM VHGAIVEKYL LEKSRIVFQA KDERNYHVFY YLLAGADDKE
     KESLHLLKAD QYNYLSQSAC YSVEGVDEKH EFSRLRQSME MVGFSPETQR KIFSVLSAVL
     HLGNVEFKKK GDKHHDESVT IKAGDSVRII STLLKVKERY VLEALTQKKS TAGDETFVIN
     YKMEDAVATR DAMTKCIYGA LFDWIVLKVN QALLAKKHDS EHEGDSIGVL DIFGFEDFGN
     NSFEQFCINY ANEHLQYYFN QHIFKFEQEE YLREGIQWKN IEFIDNTGSL ELFSKRPSGL
     FYLLDEECNF PAATNETLLN KFTHHHKSNP HYQVPQLREG AFSIMHYAGR VKYLVKDFRE
     KNLDLVRPEI VDTLKKSSLA FVRELMGIDP VAVLRWSVVR AFFRCFFAFK KAGEVYRKNG
     GKESRRRQKR ASDPTLQDVL NDNLLNSAAM GAHLQQHHLG HDPAVLLQRL HKEEVNDEIL
     LYSSYGTNCS ESQVKVMRRT LRLLTKNKSF RPKPRPSLSF RDIKALKAIA SRTMPGSVRG
     TGSKKQPPTV GAQFQWSLNC LMMTLNQANP YFIRCIKSNK DKAPCVFDEE LVMRQLRYTG
     MLATVKIRQS GYNYRILLKE FTLMYKILLP VQTEFTKNDI SNFLTAKGLQ PENYQIGINK
     IFLRETEKLK LDEALHSAIM KRVITIQKWV KACLERRYFL RIRESTILMQ KHIRRFLAQR
     DFQQYQLYQL HTEAAIVIQT NFRRYLAWKQ FVSTRNAVVF LQAYIRTVLM RKRFLTLKEE
     KRKKLLQDAE KERLESEKRQ KEEDKRRLEE EYEKIERQAQ ELLAKDYEEK LAKEENQSYE
     ERLQLDRRKK EELQSTASDE GVLMKAPSTE ELEEDVRLPR RDSDESSGII EDSETESSEV
     LSRPILDTPP TTPQSQRRDL SKTTPIKTSQ ERSRGRAQTS RVLDRYKPSQ TSEIVDGRKT
     FVLPRSLHPT VRQKATAPLA RQESFSDREL TNATPEPMDT SNRPPPIHIP ERTTAYNDIN
     IRDIENSLAQ NKKRNELEQL QDQQASSHLS PLHKAKKHWK NWMGEFKGHH TLPHSCIPSS
     PGKTFKFFRH KSTKKKKEDS EEESEDSVSS LSRYSVESIG ISVLPASPQN KEPEEPSRFR
     RNKKQNQNKV TSSSPARSRS NIRINEWQYA DNMVISDVDE LRKLDQFIGQ KIRELYDDSN
     RRDTIFDRIF KGALEKFRKD LKTLIAVEVT KANPKVQYKE LFNQFRQVLT AEMKKMTDAP
     IVMSVNAFRG FLDEFRKQEE SRLRENKKDG NRNQKKVVKK DKKKNEEIVE HNGHRYMQVD
     FNIATYCEVC SSQKRIMEKG YVCQKCKQAI HKKCCSKMGA ACKGVADNKG RPNGQLFGAP
     LDTLVSENQK IPLVCERLMS TIEMTGLYME GVYRKSGAAP KVKELQNALE MDVEAVNLEE
     YPVHVLAATL KLYLRNLPEP LMTFELYDDF LRTMEIKEEK ELINSLFAII RKLPKANFDL
     FERLVFHLAR VAMHSDSNKM SPNALAVVFA PVLLGTNKKL QAQDAIALVP QQMMCIEYVL
     KEQMRTVKSK LDDIDTLESA EKTTGERLNA VRASLRTSRS PLSSPIKQQS VHANNENDSE
     ILEENLEDEE YIEEDVKLKI EEKALSRHLA SIHKEKDKIT YKLPALETRQ VSSDEDMLSG
     DEVDGDLDGE GQNEEYATGF EQPVTKSSLN HLSKTRTPAP HSRRLPQKFA KKVAASTKKP
     LFEDTSEACL PEPIPVIQIR PQAQCSKYLS SMTVESSYVT IPSVAGEEDE IMV
//
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