ID U7PZP2_SPOS1 Unreviewed; 127 AA.
AC U7PZP2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
GN ORFNames=HMPREF1624_03294 {ECO:0000313|EMBL:ERS99925.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS99925.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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 ECO:0000256|RuleBase:RU363014};
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily. {ECO:0000256|ARBA:ARBA00010242}.
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DR EMBL; KI440844; ERS99925.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PZP2; -.
DR STRING; 1391915.U7PZP2; -.
DR eggNOG; KOG3258; Eukaryota.
DR HOGENOM; CLU_090028_2_0_1; -.
DR OrthoDB; 5484803at2759; -.
DR Proteomes; UP000018087; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR043323; PIN4.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR PANTHER; PTHR45995; -; 1.
DR PANTHER; PTHR45995:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 4; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014}.
FT DOMAIN 32..125
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 127 AA; 13603 MW; 517710008B110785 CRC64;
MAKGKADTKK GDAKKGAADK KGDKGDKDVK GAQQINVRHI LCEKHAKKEE ALAKIRDEGA
KFDDVARTHS EDKARQGGAL GWKVRGSLDP AFEAVAFELP ASTTASPVVG EAKTSFGYHI
IMVEGRK
//
