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Database: UniProt
Entry: A0A2W1BI13_HELAM
LinkDB: A0A2W1BI13_HELAM
Original site: A0A2W1BI13_HELAM 
ID   A0A2W1BI13_HELAM        Unreviewed;       404 AA.
AC   A0A2W1BI13;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PZC74692.1};
GN   Name=HaOG207361 {ECO:0000313|EMBL:PZC74692.1};
GN   ORFNames=B5X24_HaOG207361 {ECO:0000313|EMBL:PZC74692.1};
OS   Helicoverpa armigera (Cotton bollworm) (Heliothis armigera).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Helicoverpa.
OX   NCBI_TaxID=29058 {ECO:0000313|EMBL:PZC74692.1, ECO:0000313|Proteomes:UP000249218};
RN   [1] {ECO:0000313|EMBL:PZC74692.1, ECO:0000313|Proteomes:UP000249218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Harm_GR_Male_#8 {ECO:0000313|EMBL:PZC74692.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PZC74692.1};
RX   PubMed=28756777; DOI=10.1186/s12915-017-0402-6;
RA   Pearce S.L., Clarke D.F., East P.D., Elfekih S., Gordon K.H., Jermiin L.S.,
RA   McGaughran A., Oakeshott J.G., Papanikolaou A., Perera O.P., Rane R.V.,
RA   Richards S., Tay W.T., Walsh T.K., Anderson A., Anderson C.J., Asgari S.,
RA   Board P.G., Bretschneider A., Campbell P.M., Chertemps T.,
RA   Christeller J.T., Coppin C.W., Downes S.J., Duan G., Farnsworth C.A.,
RA   Good R.T., Han L.B., Han Y.C., Hatje K., Horne I., Huang Y.P., Hughes D.S.,
RA   Jacquin-Joly E., James W., Jhangiani S., Kollmar M., Kuwar S.S., Li S.,
RA   Liu N.Y., Maibeche M.T., Miller J.R., Montagne N., Perry T., Qu J.,
RA   Song S.V., Sutton G.G., Vogel H., Walenz B.P., Xu W., Zhang H.J., Zou Z.,
RA   Batterham P., Edwards O.R., Feyereisen R., Gibbs R.A., Heckel D.G.,
RA   McGrath A., Robin C., Scherer S.E., Worley K.C., Wu Y.D.;
RT   "Genomic innovations, transcriptional plasticity and gene loss underlying
RT   the evolution and divergence of two highly polyphagous and invasive
RT   Helicoverpa pest species.";
RL   BMC Biol. 15:63-63(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC       anchor {ECO:0000256|ARBA:ARBA00004635}.
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DR   EMBL; KZ150033; PZC74692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W1BI13; -.
DR   EnsemblMetazoa; XM_021339074.2; XP_021194749.1; LOC110379402.
DR   OMA; RVCPTCV; -.
DR   OrthoDB; 2785358at2759; -.
DR   Proteomes; UP000249218; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030544; F:Hsp70 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; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR044713; DNJA1/2-like.
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; PTHR43888:SF31; DNAJ HOMOLOG SUBFAMILY A MEMBER 2; 1.
DR   PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 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; PS00636; DNAJ_1; 1.
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:UP000249218};
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          5..67
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          125..209
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         125..209
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          374..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  44974 MW;  8B9FE76EFDCB8B7F CRC64;
     MADNKLYEIL GVSRSASESE IKRSYHKLAK EFHPDKNPAA GDKFKEISYA YEVLSDSKKR
     QIYDKYGLKG LQEGGQGGGF PPDDLFGHFF GDIFGMGGGS RGRGPARGED TMHPLKVSLE
     DMYMGKTTKL QLSKNVICGP CKGIGGKPGS VVTCKDCHGQ GIKVSYQQIA PHMTRQFQSR
     CPTCHGQGET INDKDKCPKC KGKKVLNETK ILEVHIEKGM CENQKIFFRG EGDQQPDTQP
     GDVIIVLQQK PHDIFQRTGD DLVIKHEITL TEALCGFEFV IKHLDGRDLL VRHTPGEVIK
     PGDLKGIQGE GMPQFKNPFE KGNLYIKFDV VFPENNFATE EQLKQIETVL PPRPAFVMPT
     GEDVEEVNLM EYTASERGRG REEAYASDDE EHMHTGPGVQ CAHQ
//
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