ID G7XE80_ASPKW Unreviewed; 394 AA.
AC G7XE80;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=AKAW_03383 {ECO:0000313|EMBL:GAA85269.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85269.1};
RN [1] {ECO:0000313|EMBL:GAA85269.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85269.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388}.
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 Evidence={ECO:0000256|ARBA:ARBA00000971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000256|ARBA:ARBA00010898}.
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DR EMBL; DF126453; GAA85269.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XE80; -.
DR STRING; 1033177.G7XE80; -.
DR VEuPathDB; FungiDB:AKAW_03383; -.
DR eggNOG; KOG0546; Eukaryota.
DR InParanoid; G7XE80; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF07719; TPR_2; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000313|EMBL:GAA85269.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 11..195
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REPEAT 331..364
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 394 AA; 43406 MW; 9F9D2D2BD632B878 CRC64;
MADSERRPRV FFDIQIGKQK TGRIALELFN DVVPKTAENF RALCTGEKGM GKQGKPLHFK
GTVVQSGSFR FSSPSPAPAG PRSIFHRVIK QFMIQGGDFT AFNGTGGESI YGEKFPDENF
DLKHDRPFLL SMANSGPGTN GSQFFITTVP TPHLDGKHVV FGEVINGKSV VRKIENMSTQ
ADKPTIDVTI VDCGELTGDE YENADKQIPD ATGDPYEDFP DDHQGEELSA PVCFKIATEL
KNFGNTAFKS GNLTLGLEKY QKGLRYLNEF PEPDEQDPKD LDPQMKALRF TLHSNSSLLA
NKLGQFKNGQ TWATYALETA AAANAKDADK AKAYYRRAVA YSGLKEEDEA LKDLQEASQL
APGDAGITNE IARVKKAVKD RQARERATAQ KFFS
//
