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PPID_CRYNB
ID   PPID_CRYNB              Reviewed;         375 AA.
AC   P0CP81; Q55QB1; Q5KFV5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
DE            Short=PPIase D;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase D;
GN   Name=CPR6; OrderedLocusNames=CNBF4260;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAEY01000032; EAL20100.1; -; Genomic_DNA.
DR   RefSeq; XP_774747.1; XM_769654.1.
DR   AlphaFoldDB; P0CP81; -.
DR   SMR; P0CP81; -.
DR   EnsemblFungi; EAL20100; EAL20100; CNBF4260.
DR   GeneID; 4936978; -.
DR   KEGG; cnb:CNBF4260; -.
DR   VEuPathDB; FungiDB:CNBF4260; -.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   Proteomes; UP000001435; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..375
FT                   /note="Peptidyl-prolyl cis-trans isomerase D"
FT                   /id="PRO_0000410200"
FT   DOMAIN          7..169
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          217..250
FT                   /note="TPR 1"
FT   REPEAT          270..307
FT                   /note="TPR 2"
FT   REPEAT          312..345
FT                   /note="TPR 3"
SQ   SEQUENCE   375 AA;  40995 MW;  2756FC18EC2156CE CRC64;
     MSNTIAYFDI TIANEPAGRL TFELFDDVVP KTANNFKHLC IGDKTNEAGV KLAYAGSSFH
     RCIKGFMLQG GDFTRGDGTG GESIYGEKFE DENFELKHDK PMLLSMANAG PGTNGSQFFI
     TTVPTPHLDG KHVVFGRVIY NRSLVRRIEN IPTTSDRPDQ EVTISSAGVL SPDEFAQLEA
     ERQAKQAGSD GGDIWEDWPQ DEEGVDAEKP EEALVVAGKL KEVGTKEFKA GNFAVALDKY
     QKALRYLDVH PVLPNDSPAE LVESFRSLRL PLLTNAALCA LKLPASPNTS SLVVSLTSRA
     LTLPNLSASE KGKALYRRAQ AYVLKKDDEA AEKDLKGALE CVPGDAGVIK LLKDVEAKRK
     ARREKERQAF AKMFG
 
 
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