ID A0A2G9GB41_9LAMI Unreviewed; 540 AA.
AC A0A2G9GB41;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Protein disulfide isomerase (Prolyl 4-hydroxylase beta subunit) {ECO:0000313|EMBL:PIN02415.1};
DE EC=5.3.4.1 {ECO:0000313|EMBL:PIN02415.1};
GN ORFNames=CDL12_25071 {ECO:0000313|EMBL:PIN02415.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN02415.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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:PIN02415.1}.
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DR EMBL; NKXS01005937; PIN02415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9GB41; -.
DR STRING; 429701.A0A2G9GB41; -.
DR OrthoDB; 314307at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF189; PROTEIN DISULFIDE ISOMERASE-LIKE 1-5-RELATED; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:PIN02415.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013634589"
FT DOMAIN 50..215
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 402..530
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60163 MW; 7B5C227093DC322A CRC64;
MYGSKFTSRS LLFPLILLLL LSAFIFTTVS SDEDADDLED IQELIAIDDE QEGEESSQTT
THYENKDAGK KSEAEVLSKA QRIVLELNSD VTKRVIEENE YVLVLGYAPW CSRSAELMPR
FAEAANVLKG LGSGVLFAKL DAERYPKAAS SIGIKGFPTL LLFVNGSSQP YTGGFSSEEI
VIWARKKTGT PVIRINSVAE ANEFLRQHAI YAVGLFDKYE GPEYGEFIKA AEDDNDFQFV
ETSSTEVADV LYPVVKPTKP FFGLVKDEPE HYTSLDGNLS SDRILQFLEN NKFPLVTVMT
ELNSAKVYSS TKKLQVYVFA EADDLKKLLE PLQDVAKKFK SKIMFVAVDI GEDNLAKPFL
TLFGLEESDE TAVIAFDYNS NSKYLLELDP TPRNIEDFCT GLLQGTLSPY YKSQPIPDNK
NASILTVVGK TFDDLVLSSL KNILLEVHTP WCVSCETTSK QVEKLAKHFK GLDELVFARI
DASANEHPKL LVEDYPTLLF YPASDKSNPI KLPTKSSLKE LATLINKNLK TQDSSAKDEL
//