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Database: UniProt
Entry: A0A4S2KAR2_9HYME
LinkDB: A0A4S2KAR2_9HYME
Original site: A0A4S2KAR2_9HYME 
ID   A0A4S2KAR2_9HYME        Unreviewed;       488 AA.
AC   A0A4S2KAR2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 12.
DE   RecName: Full=Protein tumorous imaginal discs, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DBV15_04458 {ECO:0000313|EMBL:TGZ46425.1};
OS   Temnothorax longispinosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Temnothorax.
OX   NCBI_TaxID=300112 {ECO:0000313|EMBL:TGZ46425.1, ECO:0000313|Proteomes:UP000310200};
RN   [1] {ECO:0000313|EMBL:TGZ46425.1, ECO:0000313|Proteomes:UP000310200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:TGZ46425.1};
RX   PubMed=30967075;
RA   Kaur R., Stoldt M., Jongepier E., Feldmeyer B., Menzel F.,
RA   Bornberg-Bauer E., Foitzik S.;
RT   "Ant behaviour and brain gene expression of defending hosts depend on the
RT   ecological success of the intruding social parasite.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20180192-20180192(2019).
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:TGZ46425.1}.
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DR   EMBL; QBLH01002884; TGZ46425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S2KAR2; -.
DR   STRING; 300112.A0A4S2KAR2; -.
DR   Proteomes; UP000310200; 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; IPR018253; DnaJ_domain_CS.
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; 1.
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:UP000310200};
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          37..102
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          183..261
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         183..261
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          431..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  53868 MW;  E374ACF008CC58B4 CRC64;
     MVIVASTVGG WNREKNIGTI VQPHRAVHLT NRLLRRNYYE ILGVSKNASS KDIKKAYYQL
     AKKYHPDTNK GDPDANKKFQ EVSEAYEVLS DDTKRKEYDT WGATSEQMGM GMGQGQGGPK
     SYNQHWQYRS TINAEELFRK IFGDAGFQSG AFSDFEDFTE TKYGFGAAQE VIMNLTFSQA
     ARGVNKDINV NVVDTCPKCG GSRCEIGTKP AKCFYCNGTG METISTGPFV MSSTCRYCQG
     TKMHIKFPCT ECNAKGQTVQ RKKITVPVPA GVEDGQTIRM ALGRKEIFVT FRVEKSRYFR
     RDGPDVHTDA EVSLAQAVLG GTIRVEGVYE DQTIQIMPGT SSHTRIRLTG KGLKKVDGMG
     YGDHYVNVKI TVPKQLTEKQ RALFQAYAEL ETNTPGSIHG VTYKTDGTKE CYSGPLHLVE
     SIRIALGNTP NREIQSSSSE PEHPGDKPLD NRSVHTKDTS DVVGKNDTNA GNATTESAPV
     IASVKRNL
//
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