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YBP8_SCHPO
ID   YBP8_SCHPO              Reviewed;         618 AA.
AC   O42943;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Uncharacterized ABC transporter ATP-binding protein C16H5.08c;
GN   ORFNames=SPBC16H5.08c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-53; THR-54; SER-55
RP   AND SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CU329671; CAA17906.1; -; Genomic_DNA.
DR   PIR; T39617; T39617.
DR   RefSeq; NP_595939.1; NM_001021847.2.
DR   AlphaFoldDB; O42943; -.
DR   SMR; O42943; -.
DR   BioGRID; 276616; 9.
DR   STRING; 4896.SPBC16H5.08c.1; -.
DR   iPTMnet; O42943; -.
DR   MaxQB; O42943; -.
DR   PaxDb; O42943; -.
DR   PRIDE; O42943; -.
DR   EnsemblFungi; SPBC16H5.08c.1; SPBC16H5.08c.1:pep; SPBC16H5.08c.
DR   GeneID; 2540078; -.
DR   KEGG; spo:SPBC16H5.08c; -.
DR   PomBase; SPBC16H5.08c; -.
DR   VEuPathDB; FungiDB:SPBC16H5.08c; -.
DR   eggNOG; KOG0927; Eukaryota.
DR   HOGENOM; CLU_000604_36_6_1; -.
DR   InParanoid; O42943; -.
DR   OMA; DWMGQWT; -.
DR   PhylomeDB; O42943; -.
DR   PRO; PR:O42943; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISO:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR   GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..618
FT                   /note="Uncharacterized ABC transporter ATP-binding protein
FT                   C16H5.08c"
FT                   /id="PRO_0000310286"
FT   DOMAIN          76..325
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          388..609
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         423..430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         54
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   618 AA;  69213 MW;  2F547D71A7986CA4 CRC64;
     MSSKSASKLK REAKKAERLA AKGESVKPSK KNGTKNGKDK EVDGVTKDLS ELSTSDPIFE
     RSASGVLTSQ PMSRDIKIDS YTLSFHGRLL IENATIELNH GQRYGLLGDN GSGKSTFLES
     VAARDVEYPE HIDSYLLNAE AEPSDVNAVD YIIQSAKDKV QKLEAEIEEL STADDVDDVL
     LESKYEELDD MDPSTFEAKA AMILHGLGFT QEMMAKPTKD MSGGWRMRVA LSRALFIKPS
     LLLLDEPTNH LDLEAVVWLE NYLAKYDKIL VVTSHSQDFL NNVCTNIIDL TSKKQLVYYG
     GNFDIYMRTK EENETNQMKA YLKQQEEIAH IKKFIASAGT YANLVRQAKS KQKIIDKMEA
     AGLVEKPEPP RQFSFEFDEV RKLPPPIIAF NDVAFSYDGN LDHALYRDLS FGIDMDSRVA
     IVGKNGTGKS TLLNLITGLL IPIEGNVSRY SGLKMAKYSQ HSADQLPYDK SPLEYIMDTY
     KPKFPERELQ QWRSVLGKFG LSGLHQTSEI RTLSDGLKSR VVFAALALEQ PHILLLDEPT
     NHLDITSIDA LAKAINVWTG GVVLVSHDFR LIGQVSKELW EVKDKKVVKL DCSIEEYKKS
     MAKEVQSRDT TAKVKHLI
 
 
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