GenomeNet

Database: UniProt
Entry: A0A2A4ISX6_HELVI
LinkDB: A0A2A4ISX6_HELVI
Original site: A0A2A4ISX6_HELVI 
ID   A0A2A4ISX6_HELVI        Unreviewed;       613 AA.
AC   A0A2A4ISX6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   RecName: Full=J domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B5V51_14099 {ECO:0000313|EMBL:PCG62596.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG62596.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG62596.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG62596.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG62596.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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:PCG62596.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NWSH01008334; PCG62596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4ISX6; -.
DR   STRING; 7102.A0A2A4ISX6; -.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR44029; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR   PANTHER; PTHR44029:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          3..69
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          568..597
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          285..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          180..240
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        300..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..382
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  70369 MW;  255A3B9A93063A7E CRC64;
     MKCHYEVLCV PKEASASEIK KAYRRLALQW HPDKNLENLI EAKEQFQLVQ NAYEVLSDPQ
     ERAWYDNHRE QLLRGAGSSY NDDSLDVYPY FSPSCYKGFG DDPQGFYGVY NEVFSKLISE
     ETDFLDDPED VAKIPTFGNS TSPYEEVNEF YAYWMAFSTN KSYVWLDQYE ISQGDNRRVI
     KMMEKENNKI RQKARKERNE EIRRLVSFVR RKDKRVIEHT KLLQEKAEEN KRKAEQVRRE
     RIIQRQKEIE EAKKKEGESS FLQSEDYQKK LSEIESLLAE EFGLSSDDDT ISEGGMESSN
     EESSKTEEAS EASKTTAKSS KSKSAIKNLY CSACNKLFKN IKSFENHENS KKHKENVANM
     TLDDDIDISD NDDEEADVDV NEEVIVNEDK SDGDKMNGQM KDEGEHMGNS TSDIEDNEDN
     DFRETLSDDS DKVQALPKSQ KKKKNKKKFV PMPESEGNDS HDEMSFNEIE GPSRSRKAKK
     FNMLKSQIQA KKEANLKKGS QSQTSTENLY EVSSTTPTDD ALGEAALPKD RPALPKTQRN
     IKPKKMVDRK PVRTKTSETE DSSTALNLRC AVCQTDFPSK NKLFEHLKKT GHSVPLPQTS
     FTPPARKGKR ANR
//
DBGET integrated database retrieval system