ID A0A238YH82_9FLAO Unreviewed; 526 AA.
AC A0A238YH82;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:SNR69973.1};
GN ORFNames=SAMN06265376_10234 {ECO:0000313|EMBL:SNR69973.1};
OS Dokdonia pacifica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia.
OX NCBI_TaxID=1627892 {ECO:0000313|EMBL:SNR69973.1, ECO:0000313|Proteomes:UP000198379};
RN [1] {ECO:0000313|EMBL:SNR69973.1, ECO:0000313|Proteomes:UP000198379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25597 {ECO:0000313|EMBL:SNR69973.1,
RC ECO:0000313|Proteomes:UP000198379};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the VKOR family.
CC {ECO:0000256|ARBA:ARBA00006214}.
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DR EMBL; FZNY01000002; SNR69973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238YH82; -.
DR OrthoDB; 1100563at2; -.
DR Proteomes; UP000198379; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd12921; VKOR_4; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.20.1440.130; VKOR domain; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR038354; VKOR_sf.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR Pfam; PF07884; VKOR; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Isomerase {ECO:0000313|EMBL:SNR69973.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000198379};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 136..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 164..292
FT /note="Vitamin K epoxide reductase"
FT /evidence="ECO:0000259|Pfam:PF07884"
FT DOMAIN 369..507
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13462"
SQ SEQUENCE 526 AA; 61405 MW; BF025D33D49F2849 CRC64;
MAENISFNHV FLYLEKESIA FDKDEFLFQI QSHPDYPTLL SISDTLAFFN IDNGAIPFEA
SKIELLPDQF MGIMREANDE PQLYYIQKKD DKYITIKDKT PFEIDYETLE SRWYNLIFLV
EKPDIENTTV IKKDKTVMIL SFLCIALFSL FYFTSNSTIS KLLFILFPCV GILFSVAALK
ELFGTKSTLI NKFCNITAST NCTSVVSSNK WKFFNSINFS DLSILFFSSQ IFGLITFFLL
GNFLEYFAIQ KIVLITSIPV IVLSLYYQKF IEKKWCPICL TIASIVLLEI IYLFLLVDVG
ITISSKSLFI YAYILLVTII LWMVLKKMLS KQKKLKEFQI KTNRLLRNYS VFKNTLVITP
KVTIPQNIGM ILGNPKSNTH ITIITNPFCG HCKEVHEIVN TILDKYRDQI QVKILFKTAL
ELDNEETKRF FRILMTLYLE NGEKVFTNAL HDFFKSKDVK AWNQVYQIDT NNKAVDDIYD
SMNHWCLENQ INYTPEIYIN GFKYPSEYEK EYLAFYINDL IEDVNF
//
