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Database: UniProt
Entry: L5K009_PTEAL
LinkDB: L5K009_PTEAL
Original site: L5K009_PTEAL 
ID   L5K009_PTEAL            Unreviewed;      2155 AA.
AC   L5K009;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Putative Polycomb group protein ASXL1 {ECO:0000313|EMBL:ELK04086.1};
GN   ORFNames=PAL_GLEAN10024216 {ECO:0000313|EMBL:ELK04086.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK04086.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the Asx family. {ECO:0000256|ARBA:ARBA00006391}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; KB031072; ELK04086.1; -; Genomic_DNA.
DR   STRING; 9402.L5K009; -.
DR   eggNOG; ENOG502QWT2; Eukaryota.
DR   InParanoid; L5K009; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   InterPro; IPR026905; ASX-like_PHD.
DR   InterPro; IPR024811; ASX/ASX-like.
DR   InterPro; IPR028020; ASX_DEUBAD_dom.
DR   InterPro; IPR044867; DEUBAD_dom.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13578; ADDITIONAL SEX COMBS LIKE PROTEIN ASXL; 1.
DR   PANTHER; PTHR13578:SF19; POLYCOMB GROUP PROTEIN ASXL1; 1.
DR   Pfam; PF13919; ASXH; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF13922; PHD_3; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51916; DEUBAD; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          9..290
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          873..982
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          324..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1255..1351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1366..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1516..1549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1604..1674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1741..1793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1856..1916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          386..529
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        342..362
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1051
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1336..1351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1389..1409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1447..1472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1535..1549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1644..1658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1856..1906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   2155 AA;  236766 MW;  73128F74626F5CDE CRC64;
     MSKLKSSESV RVVVRCRPMN GKEKAASYDK VVDVDVKLGQ VSVKNPRGVA HEMPKTFTFD
     AVYDWNAKQF ELYDETFRPL VDSVLQGFNG TIFAYGQTGT GKTYTMEGVR GDPEKRGVIP
     NSFDHIFTHI SRSQNQQYLV RASYLEIYQE EIRDLLSKDQ TKRLELKERP DTGVYVKDLS
     SFVTKSVKEI EHVMNVGNQN RSVGATNMNE HSSRSHAIFV ITIECSNVIS ALVDGKSTHI
     PYRDSKLTRL LQDSLGGNAK TVMVANVGPA SYNVEETLTT LRYANRAKNI KNKPRVNEDP
     KDALLREFQE EIARLKAQLE KRSIGRRKRR EKRREGGGSG GGGEEEEEEG EEGEEEGDDK
     DDYWREQQEK LEIEKRAIVE DHSLVAEEKM RLLKEKEKKM EDLRREKDAT EMLGAKIKAM
     ESKLLVGGKN IVDHTNEQQK ILEQKRQEIA EQKRREREIQ QQMESRDEET LELKETYSSL
     QQEVDIKTKK LKKLFSKLQA VKAEIHDLQE EHIKERQELE QTQNELTREL KLKHLIIENF
     IPLEEKSKIM NRSFFDEEED HWKLHPITRL ENQQMMKRPV SAVGYKRPLS QHARMSMMIR
     PEARYRAENI VLLELDMPSR TTRDYEGPAI APKVQAALDA ALQDEDEIQV DASSFESTAN
     KKSKASGTSP LACLNAMLHS NSRGGEGLFY KLPGRISLFT LKKDALQWSR NPAAVEGEEP
     EDTADVESCG SNETSTVSGE NDVSLDETSS NASCSTESQS RPLSSPRDSC RASSQANKQK
     KKTGVMLPRV VLTPLKVNGA HVESASGFSG RHADGESGSP SSSSSGSLAL GSAAIRGQAE
     VARDPAPLLR GFRKPATGQM KRNRGEEIDF ETPGSILVNT NLRALINSRT FHALPSHFQQ
     QLLFLLPEVD RQVGTDGLLR LSSSALNNEF FTHAAQSWRE RLADGEFTHE MQVRIRQEME
     KEKKVEQWKE KFFEDYYGQK LGLTREELLQ QNVVKEEAEI KSDLRVPGES ARPQRGPATR
     QRDGHFKKRS RPDLRTRARR NLYKKQEPEQ GGNAKDTQSA TPDTPHYQHR EAKSDSAEAG
     SPHLSDTSSA APDPKGPDFS AETGASRIQT NPDDLARACE SPDRIPTLPQ ETVDQEPKDQ
     KRKSFEQAAS ASFPEKKPRL EDRQSFRNTI ESVHTEKPQP TKEEPKVPPI RIQLSRIKPP
     WVVKGQPTYQ ICPRIVPITE PSCRAWTSAR TLADIKARAL QVRGARGHHC HREAATTAIG
     GGGGPGGGDG RATDEGGGRG GSIGDGGETC GHPEPRGAPS TLGECASDLQ RTQLLPPHPL
     NGEHTQAGTA TPRARREDLA SLREEDRCPL QRVPDILTSG LEDASQLPVV PTGDQPCQAL
     PPVSSKTPAP ESVVEQPTSH PSVRTEYESS PTSWEKDNEE QEPTLPPENG LIQSLVGNVV
     LEEETGQALD SDSNLTMKDP VNVTPSSTPE SSLVSCLQDR QFDDELGLGD SCPPTRESAT
     RQEDLKAEAL ISSGAVPWMP GLSNDTVGQP ESDSRENVPS REPKVGEEWE EAAPLIPTLP
     EGLTAEEGLH FPDNCPSLWT VPSQECVDSG GGDYKQVEVE KLKISGDSKA PSPHSESTDT
     ASDFEGHLSE DSSEAAPSEA TVMKRSSVDK EEKHNRSGSA SLCKVNGDPS PVTRTDRMVA
     SQSWVSRVCA IPPKIPDSLL LASTEYQPRP MPLGRPGSSV EATNPLVMQL LQGNLPLEKV
     LPPALSDSKP KSPRLPLVKE QGMGSLHDPR ESSCAVDRNS PGSLRASKEP LLHDSREASS
     GLARLEVIQA PGTPQKISKT VPSLDSLYPV TNSTTVSRKA EVDSKEQFSP FNFEEQKEAG
     NLSQGSNSNA APDKSPGNHT TSRAPCFLSP NVVSLGPSQT GRPLGGQDSA GGQGKKLFGS
     INEAAALPCP RPVEPMPLPA DAPPGFPSRK LGATKNSVSG GVQTAREDWA PKPPPASVGS
     IKSEKSFVGV PLKMNAENRN AAGLGPRELV DHLQAMPFVL DLPFWKLPRE PGKGLSQPLE
     PSSISSQLNI KQAFYGKLSK LQLSSTSFNY SSSSPTFPKG LAGSVVQLSH KANFGASHSA
     SLSLQMFTDS STVESISLQC ACSLKAMIMC QGCGAFCHDD CIGPSKLCVL CLVVR
//
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