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PALB_CANAL
ID   PALB_CANAL              Reviewed;         717 AA.
AC   Q5AK25; A0A1D8PP42;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Calpain-like protease palB/RIM13;
DE            EC=3.4.22.-;
DE   AltName: Full=Cysteine protease RIM13;
GN   Name=RIM13; OrderedLocusNames=CAALFM_C505030CA;
GN   ORFNames=CaO19.11478, CaO19.3995;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   FUNCTION.
RX   PubMed=15189995; DOI=10.1128/ec.3.3.741-751.2004;
RA   Li M., Martin S.J., Bruno V.M., Mitchell A.P., Davis D.A.;
RT   "Candida albicans Rim13p, a protease required for Rim101p processing at
RT   acidic and alkaline pHs.";
RL   Eukaryot. Cell 3:741-751(2004).
CC   -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC       factor RIM101 in response to alkaline ambient pH. {ECO:0000250,
CC       ECO:0000269|PubMed:15189995}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP017627; AOW29907.1; -; Genomic_DNA.
DR   RefSeq; XP_721903.1; XM_716810.2.
DR   AlphaFoldDB; Q5AK25; -.
DR   SMR; Q5AK25; -.
DR   STRING; 237561.Q5AK25; -.
DR   MEROPS; C02.008; -.
DR   PRIDE; Q5AK25; -.
DR   GeneID; 3636487; -.
DR   KEGG; cal:CAALFM_C505030CA; -.
DR   CGD; CAL0000195739; RIM13.
DR   VEuPathDB; FungiDB:C5_05030C_A; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   HOGENOM; CLU_023416_0_0_1; -.
DR   InParanoid; Q5AK25; -.
DR   OrthoDB; 343870at2759; -.
DR   PRO; PR:Q5AK25; -.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IMP:CGD.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0071467; P:cellular response to pH; IMP:CGD.
DR   GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR   GO; GO:0044409; P:entry into host; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   InterPro; IPR036213; Calpain_III_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF49758; SSF49758; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..717
FT                   /note="Calpain-like protease palB/RIM13"
FT                   /id="PRO_0000207738"
FT   DOMAIN          85..352
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   717 AA;  83070 MW;  0C6A85A0294C0EB4 CRC64;
     MPTPCLEQFL HHLEKSHLYL SIDNTKQAKK ECLESIKILN SIAKTTPLPE IKVLSQYTLN
     HYESLDKPRT ISDKLEWISS KLTQETFFPP VIQFNENFTS HNELFVDTIS PIQDNDNKIF
     EKLPNKLAKF EYIEISNWDN DITHLKNLYQ DILPNCSFVS SFLAIIDANI PIIDTITPQK
     SSQKYKVSLR FNGALRNVIV DSKFPIMPNS RNLIIKSYSD TELYWPALIE KAYLTIMGNG
     YNFSGSNMAN DAYVLSGWLP QIIKLSNGQL PSNIDDLWRL RTQGKVTMGI GTGTLSKQLS
     SQLHLVSGHD YVIDNIKDGV ITVKNPWLDP KDRVVEIKNF NHFKYLYVNW KPDHKPYQHY
     FLYQAKPNTY NQPQFTIKCM EETWILLERH LSETSSSPSP HWMDMNVFET EYKIITPSQY
     KKYLSVETNN RLQLIKLKPG VFTIVISSNK PCRFTLSSFN AMFSKSKYKY DYTETVNGEW
     NSDINGGNWA MSTYINNPQY DIIAKQTTEL IMGMHGQGQI NFHLFHSSSD SMGERIQNFD
     KTKLINYQNY NASYQSSSYR LTPGHYKLVV SEYYRSIGTY QLVLNSSEPI TITKIPPFLG
     LYNISKSFNW DNTNRFKLKF ETTGYNSKVK IKIAYFNGES DFELQTSYRP AMRASLFNSQ
     TKQPIQINEQ FNDSLYGVFL HEILPSPEEY ILLIERFEIG YGRCVVEIGC NNKVILK
 
 
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