ID A0A2N1JH86_9BASI Unreviewed; 557 AA.
AC A0A2N1JH86;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=MVES_000186 {ECO:0000313|EMBL:PKI85909.1};
OS Malassezia vespertilionis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI85909.1, ECO:0000313|Proteomes:UP000232875};
RN [1] {ECO:0000313|EMBL:PKI85909.1, ECO:0000313|Proteomes:UP000232875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI85909.1,
RC ECO:0000313|Proteomes:UP000232875};
RA Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA Weller T.J., Blehert D.S.;
RT "A novel species of cold-tolerant Malassezia isolated from bats.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PROSITE-
CC ProRule:PRU00277};
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DR EMBL; KZ454987; PKI85909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1JH86; -.
DR STRING; 2020962.A0A2N1JH86; -.
DR OrthoDB; 1369725at2759; -.
DR Proteomes; UP000232875; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 4.10.1000.40; -; 2.
DR Gene3D; 1.10.340.40; Nuclear abundant poly(A) RNA-bind protein 2, N-terminal domain; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR043094; Nab2/ZC3H14_N_sf.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR45779:SF6; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF14608; zf-CCCH_2; 4.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000232875};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..557
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014994357"
FT DOMAIN 42..120
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 213..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 60499 MW; 4332C8C5C61BBDD0 CRC64;
MRVFATSLLL FVLPVLAKAP PKELQIGVTH SVAECPYKSQ NGDTLLMHYT GRLWDGTKFD
ASYDRGKPFM GVGHVIKGWD FGLRDMCIGE KRRLKIPSDL AYGPVGAGDV IPPDAALVFD
CVGDAAVFDL RKSYGLGTAA ASRVQDAVQG VLIAHDMASN DDQVMAEYVT VMIANSKSMD
AIAEELRELV GGELDASVPA QIWARAEAAA RESQADMRAA SPRARSPSQM QDAEFKERTR
ARWNDTARPA RAERGAERSL HHERELFPAK GRRNAKIERG MHSDAMPAQL SIFGRAGVPD
PHAMPFVPEG MPPFSEMMAA MGGPSLFTRL DPMMPNNPPV DLHPTVTNVP RDMAAFPSRP
EQRALCRYSV HCTNPLCVYS HPTPANAGNA LDERALVLSE EACENGDACT HRECVKSHVS
PSVTLIKAKG VAPPPPAARC RFQQQCLNPG CTYTHYDDSG RLTAAPAATQ GPCRFSTQCT
RPDCHYTHPP RSKTVCRYGD ACKRFDCVFT HPRDPPVHAT ADRLAAFAAT HEGKRERILP
GESAGQSAGA MSVTNSA
//
