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YJQ1_SCHPO
ID   YJQ1_SCHPO              Reviewed;         822 AA.
AC   Q9USH9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Uncharacterized ABC transporter ATP-binding protein C825.01;
GN   ORFNames=SPCC825.01;
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-27; SER-47; SER-51; SER-55;
RP   TYR-57; SER-97; SER-137 AND SER-163, AND IDENTIFICATION BY MASS
RP   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; CU329672; CAB58409.1; -; Genomic_DNA.
DR   PIR; T41622; T41622.
DR   RefSeq; NP_588051.1; NM_001023043.2.
DR   AlphaFoldDB; Q9USH9; -.
DR   SMR; Q9USH9; -.
DR   BioGRID; 276071; 4.
DR   STRING; 4896.SPCC825.01.1; -.
DR   iPTMnet; Q9USH9; -.
DR   MaxQB; Q9USH9; -.
DR   PaxDb; Q9USH9; -.
DR   PRIDE; Q9USH9; -.
DR   EnsemblFungi; SPCC825.01.1; SPCC825.01.1:pep; SPCC825.01.
DR   GeneID; 2539509; -.
DR   KEGG; spo:SPCC825.01; -.
DR   PomBase; SPCC825.01; -.
DR   VEuPathDB; FungiDB:SPCC825.01; -.
DR   eggNOG; KOG0927; Eukaryota.
DR   HOGENOM; CLU_000604_36_6_1; -.
DR   InParanoid; Q9USH9; -.
DR   OMA; MQFGAEP; -.
DR   PhylomeDB; Q9USH9; -.
DR   PRO; PR:Q9USH9; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; ISS: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..822
FT                   /note="Uncharacterized ABC transporter ATP-binding protein
FT                   C825.01"
FT                   /id="PRO_0000310289"
FT   DOMAIN          276..519
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          594..809
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         308..315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         627..634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         57
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   822 AA;  92690 MW;  74AD82CE8BC3D37C CRC64;
     MARGKRSTQR DADLELESLQ SEIESESPQP VTKSKAKKNK KKLNKASAFN SDNDSNYDLK
     PEDDEVDEEV VPVKKKPSKK SKKAKANAFE AFADEQSVEE EEEEDSEKPV RKNKKSSKKA
     SPKNAFDALA DDMDDLSLDE EESESSEKSK KKKKKSKSKD DGSEALDDGD IESSEKDKKK
     KKKSKENDDA PKKDRKTRKK EEKARKLASM LESENKDNDA NAAPLNKTDA FKDGLPSGRL
     IFAYASGQKV APDGSNPADG ITVTGNLLSP PNSRDLQVEK LSVSAWGKLL IKDSELNLIN
     GRRYGLIAPN GSGKSTLLHA IACGLIPTPS SLDFYLLDRE YIPNELTCVE AVLDINEQER
     KHLEAMMEDL LDDPDKNAVE LDTIQTRLTD LETENSDHRV YKILRGLQFT DEMIAKRTNE
     LSGGWRMRIA LARILFIKPT LMMLDEPTNH LDLEAVAWLE EYLTHEMEGH TLLITCHTQD
     TLNEVCTDII HLYHQKLDYY SGNYDTFLKV RAERDVQLAK KARQQEKDMA KLQNKLNMTG
     SEQQKKAKAK VKAMNKKLEK DKQSGKVLDE EIIQEKQLVI RFEDCGGGIP SPAIKFQDVS
     FNYPGGPTIF SKLNFGLDLK SRVALVGPNG AGKTTLIKLI LEKVQPSTGS VVRHHGLRLA
     LFNQHMGDQL DMRLSAVEWL RTKFGNKPEG EMRRIVGRYG LTGKSQVIPM GQLSDGQRRR
     VLFAFLGMTQ PHILLLDEPT NALDIDTIDA LADALNNFDG GVVFITHDFR LIDQVAEEIW
     IVQNGTVKEF DGEIRDYKMM LKQQIAKERE EERRIELEKQ KK
 
 
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