ID A0A0F8A247_9HYPO Unreviewed; 416 AA.
AC A0A0F8A247;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=Mitochondrial protein import protein MAS5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=HIM_04048 {ECO:0000313|EMBL:KJZ76712.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ76712.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ76712.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ76712.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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DR EMBL; KQ030510; KJZ76712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8A247; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030544; F:Hsp70 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; IPR044713; DNJA1/2-like.
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; PTHR43888:SF10; DNAJ-LIKE-2, ISOFORM A; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 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; 2.
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:UP000054481};
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 6..71
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 135..218
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 135..218
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 374..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 45561 MW; AFC5E6CE87C13985 CRC64;
MVKETKFYDT LGVSPTATEQ ELKKAYKMNA LKYHPDKNAH NPDAEEKFKE VSHAYEVLSD
SQKRQVYDQY GEAGLEGGAG GGGGMAAEDL FAQFFGGSGF GGMGGMFGGM NNRGPPKART
IHHTHKVSLE DVYRGKISKL ALQRSIICPK CEGAGGKAGA VKTCSGCDGH GMKTMMRQMG
PMIQRFQTVC PDCNGEGEII KEKDRCKQCN GKKTIVDRKV LHVHVDRGVR SGTKVEFRGE
GDQAPGVQAG DVVFEIEQKP HTRFTRKEDD LLYKCDIELV TALAGGTIYV EHLDDRWLSI
DILPGEAIAQ DSVKMVRGQG MPSPRHHDFG NLYIHFNVVF PEKNWTAEPA VFEELRKLLP
APSLQNVPPA EAMTEPADLE DLDNSTQSRV FSGAGMGEDE DEDGHPGAER VQCASQ
//
