ID A0A0N5AD52_9BILA Unreviewed; 432 AA.
AC A0A0N5AD52;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=J domain-containing protein {ECO:0000313|WBParaSite:SMUV_0000208701-mRNA-1};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000208701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000208701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the HscB family.
CC {ECO:0000256|ARBA:ARBA00010476}.
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DR AlphaFoldDB; A0A0N5AD52; -.
DR STRING; 451379.A0A0N5AD52; -.
DR WBParaSite; SMUV_0000208701-mRNA-1; SMUV_0000208701-mRNA-1; SMUV_0000208701.
DR Proteomes; UP000046393; Unplaced.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd12247; RRM2_U1A_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR HAMAP; MF_00682; HscB; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50102; RRM; 2.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 8..87
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 151..225
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 259..331
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 111..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 49303 MW; CE2B249E8839EB48 CRC64;
MADVKPNHTI YINNLNEKTK KDELKKALYA IFSQFGQIID IMAFKTLKMR GQAHVIFKEV
SSATNALRAM QGFPFYDKPM RIQFAREDSD VIAKAKGTYV DRPKKYLLAR QARQEKRKKA
SEGGSAKKPR TDKTAGSKAT NPPEKTNPPN KILFCTNLPE ETTEQMLSLL FNPYPGLKDI
RRIPNRPNIA FVEFESEGEA TAARNGLNNF KIAPGQCIKI KKGCEELKDC WKCKKAMDCL
KQTYFCPTCS AIQPVEDKNF FECLGVGQSF NIDPAVLKRN FLQLQAKIHP DKFSKCSNEE
RHISELCSSH LNEAYKTIME PLRRATYLLQ LKGENLADGI NLVKHLDTSS AFLIEMMELN
EEVDSLKDEK SIEALLRVVE EKIDNLCQQF KESYESGDLH ESKEAVLKMG FYYRIKDNLV
KKLQQLQDKS SL
//
