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Database: UniProt
Entry: A0A0V1A3I8_9BILA
LinkDB: A0A0V1A3I8_9BILA
Original site: A0A0V1A3I8_9BILA 
ID   A0A0V1A3I8_9BILA        Unreviewed;       511 AA.
AC   A0A0V1A3I8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   SubName: Full=Mitochonrial uncharacterized protein {ECO:0000313|EMBL:KRY19052.1};
GN   Name=l(2)tid {ECO:0000313|EMBL:KRY19052.1};
GN   ORFNames=T12_14973 {ECO:0000313|EMBL:KRY19052.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19052.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY19052.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19052.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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:KRY19052.1}.
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DR   EMBL; JYDQ01000040; KRY19052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1A3I8; -.
DR   STRING; 990121.A0A0V1A3I8; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR44145; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR44145:SF3; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}.
FT   DOMAIN          63..130
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          210..288
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         210..288
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          492..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  56952 MW;  339DEBA60D4A7714 CRC64;
     MAHNFRLLFN PLVISARQAH RRLYFPFFYF SKFDGKELRH QRQSFLLLRD FHFTSTRFAE
     KLDYYEILGV PKNASAKDIK KAYYQLAKKY HPDVNKNDPQ AARKFQQVSE AYEVKVLSDE
     NKKAQYDQWG STDFGATSSG STSSGHNWQG FHSTIDPEEL FRKIFGDIKM GQSNADFSGW
     NFDEFAESKF GFGSTQEYVM HLSFQEAAKG VTKTASINTV DVCQKCGGKK TELGYKMVSC
     PYCNGSGMET FSQGPFIMRQ TCRKCSGTGQ FNKNPCLECE GTGHTVQRKT ISVPVPAGVE
     DGQTLRMQVG KKELFITFRV SKSDIFRRDG ADVHTDVSIS VSQAILGGTV RIPGIYEDVY
     LQIPPATSSH SRLRLAGKGI KKVNSYGYGD HYVHVKIEVP KKLSDAQRAI IMAYAEMETN
     TPGTIRGVTT TAGDPRVTKA TNVDANNSGV SGFLSKEFKL VKLFNDVNLG DKVCAEDPNG
     YVAGIRKIFN SSAEENGSEK KDKAEKEKPG S
//
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