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Database: UniProt
Entry: A0A0V1LQW1_9BILA
LinkDB: A0A0V1LQW1_9BILA
Original site: A0A0V1LQW1_9BILA 
ID   A0A0V1LQW1_9BILA        Unreviewed;      1306 AA.
AC   A0A0V1LQW1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   SubName: Full=Protein disulfide-isomerase {ECO:0000313|EMBL:KRZ61869.1};
GN   Name=P4HB {ECO:0000313|EMBL:KRZ61869.1};
GN   ORFNames=T02_15303 {ECO:0000313|EMBL:KRZ61869.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ61869.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ61869.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ61869.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ61869.1}.
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DR   EMBL; JYDW01000014; KRZ61869.1; -; Genomic_DNA.
DR   STRING; 6335.A0A0V1LQW1; -.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02961; PDI_a_family; 2.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR   InterPro; IPR040025; Znf622/Rei1/Reh1.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13182; ZINC FINGER PROTEIN 622; 1.
DR   PANTHER; PTHR13182:SF8; ZINC FINGER PROTEIN 622; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   Pfam; PF12756; zf-C2H2_2; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1306
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006882022"
FT   DOMAIN          1016..1038
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ61869.1"
SQ   SEQUENCE   1306 AA;  151064 MW;  56D5E32A4B7B7FFF CRC64;
     LLTAMKFSSF IIIFTFAQLY KTSSASVDKS EITERDNILV ATDANFDKII NTYDFVLTAF
     TMDRCGQCEP IHEAFVKLAR ILKERSSPIR VAEANITEEE ELTGKHIKRI IPTLKFYKKR
     HEFMVYDVEK TNPWKLLEWV ENKAAPAAFE IFTVLQANSH VDENEIAPFA FFKDENANEL
     AVFKEVADTF DNVKFAYTFN PDVYKAYKIQ KDGIYVIKVA DDTEMYKGNG TIEDIRSWIV
     MNSLPLVPTY GAKYSNLIYE SPLKSHVYLM IRGDDEDYDD LKIIMQKAAV HFKNKLMFVI
     IDGSTADAHS YLDFFRLDQA NLPEIRICNL TEEPFVKYKP DFEIITTDKL KQFASDYLDG
     KLKPHIASQE LPDDWNNKTV RVLSIAIFDD YIKNSTTYLA ICMHKPSNDE SKTMMKHWQK
     LGELFKNATD LVLASLDCEA NEVEFGVFDI TPTVVMFEPA SIYSGNKTFE DLRLFLDSRG
     LNSSSGYAET DDVVNGVQDG ELPEMPHNYF LQKSTVKLRN MMRFFDFENV ILKHQCFAYQ
     QNQRSLYFWR IFRRWQEAEK ALVEAEQTKK SQRAYIGPLF LTPEVEKFAP PGKDPGNLTI
     AEKGGMSYET ANKYSKYRYL DLSPSTIRQF YRYENLINLQ YDQRFLPERH LLLGPDLAAA
     HFIVHRGGAV KFFNDSRWHR VNNKGEYILP GRKLPEGIDA SNTALMFEGL SNLVNLEKIR
     FLSLKNCEYV NDWCMSQMKQ FENTLEFLDL SYCSKLTADG LSALSCLKKL KYLRLEGLDQ
     VKNIGVVAVR LEDTLPQLQV VGLDYELALE NFGKDLKLLS HENVYQDAKG NAFLKDNLDE
     LYYLAGNIPE QASLADDEMP IFVSQIRKDV PCLPDDVIEE VNRLSDGKLK HLLAGSPSGE
     WSQETERVLQ VEARRAADEN RFLHSFLMPA RPGGPTWKER VQQLAVKMEI LDKEDVLLEQ
     PKKSPTVRQH FHSEWHVYNL KREIADLKPV KLEEFEAKVV EHKAETSDNT SKVEFCKVCN
     KNFRSLESYQ AHIRSKLHQE NVIHYKQFLE ENGLDGEIDE NDIAFQDSNF VQSEVEEEPS
     KKSEVLQQCL FCTHKAADLE HNLEHMSLRH GFFIPEVDYC CNLQGLISHL NTKVYSSFEC
     LWCRDRGKAF HSAVSVQTHM RDKCHCKLYH DNDAMLEYSD FYNYEYETSS DDESDDGYDL
     SLLESGDPYH LTLPSGAVIG HRSLFRYFKQ NLRLLPPENG RNSNLNEIDR VVKKYKGLGW
     RSTTKEVATI RRKDQKFIQR HQTKHQLKVA LGSNKLQRHY RDPNGY
//
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