ID A0A6G0ZKH9_APHCR Unreviewed; 401 AA.
AC A0A6G0ZKH9;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 24-JAN-2024, entry version 8.
DE SubName: Full=DnaJ subfamily A member 1 {ECO:0000313|EMBL:KAF0771173.1};
GN ORFNames=FWK35_00008250 {ECO:0000313|EMBL:KAF0771173.1};
OS Aphis craccivora (Cowpea aphid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC Aphidoidea; Aphididae; Aphidini; Aphis; Aphis.
OX NCBI_TaxID=307492 {ECO:0000313|EMBL:KAF0771173.1, ECO:0000313|Proteomes:UP000478052};
RN [1] {ECO:0000313|EMBL:KAF0771173.1, ECO:0000313|Proteomes:UP000478052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=180601 {ECO:0000313|EMBL:KAF0771173.1};
RC TISSUE=Whole Body {ECO:0000313|EMBL:KAF0771173.1};
RA Voronova N.V., Shulinski R.S., Bandarenka Y.V., Zhorov D.G., Warner D.;
RT "Whole genome of Aphis craccivora.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
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:KAF0771173.1}.
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DR EMBL; VUJU01000326; KAF0771173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G0ZKH9; -.
DR Proteomes; UP000478052; 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; 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:SF10; DNAJ-LIKE-2, ISOFORM A; 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; 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:UP000478052};
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 6..68
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 128..212
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 128..212
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 371..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 44842 MW; C258FA03BCB8D927 CRC64;
MVKETTYYDI LGVKPNCGND ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLTTPEK
RRLYDQGGEQ ALKEGGVGNS FSSPMDLFDM FFGQFGGSGG RGRGRHGPQK GKDVVHQLSV
SLEDLYNGCV RKLALEKNII CDKCEGRGGK KGAVEQCPGC QGSGIQVQIH QLGPGMIQQV
QSMCSECRGQ GERINPKDRC RNCNGKKVTR ERKILEVNVD KGMVDGQKIT FNGEGDQEPG
LEPGDIIIVL DEKEHRLYKR SGSDLILRLE IELVEALCGF KKVVKTLDER SLVINSDAGE
VLKHGDVKCV MGEGMPQYKN PFEKGRMIIQ FLVNFPETLS PSKVPLLETC LPPRPVETIP
ETFEEVSLIE MDPEYDSRRQ SRREAYNDED GPTRNVQCAS H
//
