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SBE22_CANGA
ID   SBE22_CANGA             Reviewed;         813 AA.
AC   Q6FKH3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protein SBE22;
GN   Name=SBE22; OrderedLocusNames=CAGL0L11572g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: With SBE2, is involved in cell wall integrity and polarity
CC       processes like bud growth. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SBE2 family. {ECO:0000305}.
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DR   EMBL; CR380958; CAG62245.1; -; Genomic_DNA.
DR   RefSeq; XP_449271.1; XM_449271.1.
DR   AlphaFoldDB; Q6FKH3; -.
DR   STRING; 5478.XP_449271.1; -.
DR   PRIDE; Q6FKH3; -.
DR   EnsemblFungi; CAG62245; CAG62245; CAGL0L11572g.
DR   GeneID; 2890971; -.
DR   KEGG; cgr:CAGL0L11572g; -.
DR   CGD; CAL0135442; CAGL0L11572g.
DR   VEuPathDB; FungiDB:CAGL0L11572g; -.
DR   eggNOG; ENOG502QR4N; Eukaryota.
DR   HOGENOM; CLU_019068_0_0_1; -.
DR   InParanoid; Q6FKH3; -.
DR   OMA; WWNILER; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR031403; Sbe2/Sbe22.
DR   Pfam; PF17076; SBE2; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cytoplasm; Golgi apparatus;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..813
FT                   /note="Protein SBE22"
FT                   /id="PRO_0000320508"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  92043 MW;  F3A11057F4F23FBF CRC64;
     MIRPRSNLGT LPEEPSVESK SGRTLAGITS SRKESGMRSR TSSGSAQAVG LGLGRRPSDN
     LFHGHADPLD TMQMLSEALP QPPKIEHGMR RERPISNDSI MTTKSSEIFS TSSSDTQSNI
     SVATNDSEDH SFGMDKSVDN SSTNATLTNR SIENRSNGDS YSIGEKSDVS VNRSTKSGNN
     PLQRTQSETI SVNMSHNRSM NGAMKQPTPP FMGKNSSIPN LRYNSQPQQD NRSVPNGEFG
     SKLYNLSNST SAIIPNAGTG SKLALTPSQR YRLRKEQSEH ALRDVIKRKE KLYDEQDGII
     ELQEGDIDGS FIFNVPMSSY STTSFLNTTR QKDSATNSSS TITERITPGE NQSQNNRESN
     MSFASTISST SMLDFFEMPT SPIPGVNKVS DFQYLQDTTK HLSSVYLHSS TKLSKSKLSE
     RTASADCLPL EFKEASEKGM EDLLLVSENK LDAVSHTRPS WLPPKDPEEK KLHEREISKT
     LSMASLDQLE KNKDRDSKII KDETNKQKYV LLVDRNITRK SSLQSLKKII WETPINAELR
     NHIYDMVLQS EARLVTERFT ESFDDIIKLS NRIELTKTKE IEIRNLITAN IENKAGGKYD
     VSDDLVLMLK LKSISQQGIL PGDELLFHHL LIDDSFENLN QVWEMVNLIQ MTCFNEITKD
     KFDSKILEKS GVVASYMLQD DSFKHEFNAN CLNSNTWWNI LERVNHDLFM WIIDIIVTMN
     SQPFKNSPIN KEKYSEVNWD VYRDNKVLIN YQILISFALN VLLNYHFGFN DLKSLADVKD
     KNFCIPISEE NYLDIDEINS LFVGKWKHYF KKF
 
 
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