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Database: UniProt
Entry: A0A1D2MCN8_ORCCI
LinkDB: A0A1D2MCN8_ORCCI
Original site: A0A1D2MCN8_ORCCI 
ID   A0A1D2MCN8_ORCCI        Unreviewed;       611 AA.
AC   A0A1D2MCN8;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=DnaJ subfamily C member 2 {ECO:0000313|EMBL:ODM90758.1};
GN   ORFNames=Ocin01_15923 {ECO:0000313|EMBL:ODM90758.1};
OS   Orchesella cincta (Springtail) (Podura cincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX   NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM90758.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODM90758.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODM90758.1};
RX   PubMed=27289101; DOI=10.1093/gbe/evw134;
RA   Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA   Smit S., van Straalen N.M., Roelofs D.;
RT   "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT   in the Genome of the Collembolan Orchesella cincta.";
RL   Genome Biol. Evol. 8:2106-2117(2016).
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:ODM90758.1}.
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DR   EMBL; LJIJ01001804; ODM90758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2MCN8; -.
DR   STRING; 48709.A0A1D2MCN8; -.
DR   OMA; SFWYDFD; -.
DR   OrthoDB; 168809at2759; -.
DR   Proteomes; UP000094527; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:InterPro.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd00167; SANT; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.10.8.840; Ribosome-associated complex head domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR032003; RAC_head.
DR   InterPro; IPR042569; RAC_head_sf.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR044634; Zuotin/DnaJC2.
DR   PANTHER; PTHR43999; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR   PANTHER; PTHR43999:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF16717; RAC_head; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   4: Predicted;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094527}.
FT   DOMAIN          62..134
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          536..592
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   DOMAIN          539..596
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          396..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          266..328
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   611 AA;  70917 MW;  A18AE466643DF472 CRC64;
     MTHILFHPLS NVGENVLTWV KSQHDRRLFK WARELEPEQE IDGESDLTYL RGLDPVQWKD
     QDHYQVVGLR HLRERASEED IKKSYRLRVL KHHPDKRQAA GELINTEGDY FACIVKAYEI
     LSNPAKRRAY DSVDPLFDDY TPPKSVKSPE EFFTVYGKWF ALNARWSNDQ PTPLLGNMFS
     TRNQVDDFYQ FWFDFDSWRE YSYLDEEDKE KGQSREERRW IEKQNKAQRA KLKKEEMARI
     RAVVEQAWSL DPRIALFKEI SRREKIEKKL AKQKVVQEQK DELEKVRLEE ERIAREELER
     QQAEDRERDA AAKKIKEAQK RALKKERKTF RTLCKSSNYY SEDEKSTVEN MASMEELCEI
     LQLEELTRLN ESLAKLSIDE GRTEFERTVQ TVAQRISDEN AKTAQDAYKD SDNSGGGGGG
     SRRGKGDEQW CHEELQLLIK AVNLFPAGTA QRWEVVANFL NQHYQGSSGK KRSAKEVLAK
     AKDLNSSDFS KNSLKEEANQ KAYEFFEKNI KNPGAAVVVE SEETKREEGV VNNKSGPVAE
     PNAWTAAEQK LFEQALKTYS ASAHPADRWD RIAECVPGRS KKECVARYKE LAALVKAKKS
     AQVVKQDNLH M
//
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