ID A0A178ETZ4_TRIRU Unreviewed; 442 AA.
AC A0A178ETZ4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE AltName: Full=Parvulin-14 {ECO:0000256|ARBA:ARBA00030737};
GN ORFNames=A7C99_5853 {ECO:0000313|EMBL:OAL63458.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL63458.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL63458.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) 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};
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily. {ECO:0000256|ARBA:ARBA00010242}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAL63458.1}.
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DR EMBL; LHPM01000018; OAL63458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178ETZ4; -.
DR VEuPathDB; FungiDB:TERG_00441; -.
DR VEuPathDB; FungiDB:TERG_00442; -.
DR Proteomes; UP000243015; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243015};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..442
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008085750"
FT TRANSMEM 208..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 348..440
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 240..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47485 MW; 254E0445EDE8A50C CRC64;
MGILLHILFL LSHSAIRSLA LDCRPVRIDG PSVGQRSNYT WEEGLPIQFG GWSDEEIKTC
IGVADADDIW LVSEDLDCPV VWPVSETSYN THIGTFLPKG DLKWSPFHFD LRKQADVWYV
DEKLFARSQA FFIHDGGDGA TTLYTTITST STSSYTTSTT AASTSASESS VRTIATVVVT
RTLEPTATGL VLIDHEGAGL STGVKAGIGT GVALGSIAIA AAVYIFILLR RRRNSDKVIP
MVSSEDSNKY SPPGPPEMHD EVPGSLPVVS ETNDPQKRPA SEMLGSIPVG KPTGRDPSIA
TSNTYLHILP MAPKNKGGDS KGAGGKGKGK GKESESSDIG KGKGLKAANS INVRHILCEK
HSKKEEALEK LRAGVKFDEV AREFSEDKAR QGGSLGWKVR GSLDAAFEKA AYELEPSTTG
SPKYVEVKTG FGYHIIMVEG RK
//