ID W9DUI0_METTI Unreviewed; 141 AA.
AC W9DUI0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=MettiDRAFT_2964 {ECO:0000313|EMBL:ETA69463.1};
OS Methanolobus tindarius DSM 2278.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=1090322 {ECO:0000313|EMBL:ETA69463.1, ECO:0000313|Proteomes:UP000019483};
RN [1] {ECO:0000313|EMBL:ETA69463.1, ECO:0000313|Proteomes:UP000019483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2278 {ECO:0000313|EMBL:ETA69463.1,
RC ECO:0000313|Proteomes:UP000019483};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (AUG-2013) 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, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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:ETA69463.1}.
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DR EMBL; AZAJ01000001; ETA69463.1; -; Genomic_DNA.
DR RefSeq; WP_023846595.1; NZ_AZAJ01000001.1.
DR AlphaFoldDB; W9DUI0; -.
DR STRING; 1090322.MettiDRAFT_2964; -.
DR OrthoDB; 8615at2157; -.
DR Proteomes; UP000019483; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IEA:UniProt.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR47861; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR PANTHER; PTHR47861:SF3; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915}.
FT DOMAIN 6..73
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 141 AA; 15535 MW; 4A9D4A7DDE983EAF CRC64;
MAIKDGDTVK IEYVGLLDDG SVFDASETHG QPLEFTVGEG NVIKGFDEAV KGLEVGEEKE
FRIEAKDAYG EYNDALKDTV SRDLVRSDME MEVGKTFWVQ SPHGQTIPAK IVELTEDEVT
FDLNHPLAGK ALTFKIIVVE A
//