ID A0A368GCW3_ANCCA Unreviewed; 1393 AA.
AC A0A368GCW3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DnaJ homolog subfamily C member 2 {ECO:0000256|ARBA:ARBA00014469};
DE Flags: Fragment;
GN ORFNames=ANCCAN_12526 {ECO:0000313|EMBL:RCN41538.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN41538.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN41538.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN41538.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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:RCN41538.1}.
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DR EMBL; JOJR01000233; RCN41538.1; -; Genomic_DNA.
DR STRING; 29170.A0A368GCW3; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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 CDD; cd00167; SANT; 4.
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; 1.10.10.60; Homeodomain-like; 4.
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; IPR009057; Homeobox-like_sf.
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 InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
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 Pfam; PF13921; Myb_DNA-bind_6; 1.
DR Pfam; PF00249; Myb_DNA-binding; 3.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 5.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 3.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51294; HTH_MYB; 3.
DR PROSITE; PS50090; MYB_LIKE; 4.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000252519};
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 89..153
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 223..316
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT DOMAIN 790..842
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 849..895
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 849..895
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 896..951
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 896..947
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 899..941
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 954..1003
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 954..999
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT ZN_FING 223..316
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1393
FT /evidence="ECO:0000313|EMBL:RCN41538.1"
SQ SEQUENCE 1393 AA; 159415 MW; 9EF44FD4AA0F08F9 CRC64;
MKREEPPTWD VSSLTSWISL VTFHGMIVLS RTSLPAKRCA TLILNHIAPL SICSSNIQLK
RSTPERKRLS LQYLTRRSFH SSRPSNKEDY YKTLGVKKDA SAKEIKKAYF QLAKKYHPDV
NKSKEAQEKF QEISEAYEVL SDDNKRQEYD TFGSSTSPGG GPAGRGGEWQ YKGTVDVNEI
FRRAFGFGRD GGFNWDSFAD SQFGHSHAQE MVMDISFEEA VRGTQKNIFV NVVEDCPRCK
GTQVEPGYKK LDSLLAHTNT PFSHVSCPYC NGTGMISQRL QGGFFYQASC NRCGGSGHYN
KNPCQECEGH GQSVQRRQVS FNVPAGTNDK DRVRFQVGKN QIYMMFNVAP SLKFRRDKDD
IHCDVEINIA QAVLGGTVKV PGIMEDTYVH IPPGTNSHTK MRLSGKGVKR LHSAGYGDQY
IHIKVVVPSH LSADQRALML AWAATEKPKS GTVKGFDEYS AKSTSQSKQQ KQESKTQKSE
EHHSPRGESD AQPSETSRMI PRIPTRNVKQ RNIALLHSPN LLIIPCSIVI GVLAMLAVIR
CVSVRMDIPS TSFASIEEEA EDGHNAIYTT SGNFLGYDES EDPYPELLGF VEAQIEFCDQ
FLIRIGEARK RLAEKKAILE KKAEHERLSG ALAKAKVPVI QYLPPYFKDE NMMCPPQNEE
AKHKLQYTTY DPLIKEDKKW TPQELRMLRE AVKESVIHAG VQKFIDKKDV LRSKLQRAGV
DTAQEEIIAW KEELEAINRK IQHYRNGIVD SQQVDVIDYS CVDWLKISTI EFKGSRSAAT
LRYKWLNEQC PRWNSGPWTK EELEKLKEYR EDPSFTSWAA LAKKLQTQRS PYQCFERYRS
DLYNKSKDWT KEEDDRLIAL VKVMTVNGNV QWDKVTFYMP GRHRQQVRSR YQRTLDENVR
HGRWTDQEDL LLMSAVARFG AKDWGKIAKA VVGRSDGQCR ERWCNVLDRC TEAGDWTAEE
DERLLLGIHI FGRGKWSKIA EILPRHHADS VKRRYQQLLS AKIRMCTARL SGRSPNHFIS
SSLYSVAKAK RDVLRQQLTD DSLKGECYRA AKEQARRITK RRAPRTERSY LTPEEKAIVE
KGIEEIAEKF RNGEKTADLS EIIKKIDLSE SEIASIITAA KKRSQFRRAR QVMRIPGMVK
KIKKNSHLLP DSVMERTTFR EDETEEERIM CMTEALCQAV RKYDFHEWNN NFHASRDQPE
SVVSNYVSNM LNSKCEEVAI SLRECTNVPA DSTLPPTFTS SSAYRVLERV RPPLTNRASR
YFFPSNYNDL DIMSEFNGDI IRKFTVHDRL SIRLHPNILV DPNYLKLKAQ VRCLLFEPTL
LAMAIEPPEV EELRLKKQME LVQMEIDEEN YVADTVVMDD AVAGEVEVTT EDYEPLYYED
IVDDALNATV RTV
//
