MAS5_ENCCU
ID MAS5_ENCCU Reviewed; 398 AA.
AC Q8SRK0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mitochondrial protein import protein mas5;
GN Name=MAS5; OrderedLocusNames=ECU07_0760;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Probably involved in mitosomal protein import. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR EMBL; AL590447; CAD25608.1; -; Genomic_DNA.
DR RefSeq; NP_586004.1; NM_001041626.1.
DR AlphaFoldDB; Q8SRK0; -.
DR SMR; Q8SRK0; -.
DR STRING; 284813.Q8SRK0; -.
DR GeneID; 859433; -.
DR KEGG; ecu:ECU07_0760; -.
DR VEuPathDB; MicrosporidiaDB:ECU07_0760; -.
DR HOGENOM; CLU_017633_0_7_1; -.
DR InParanoid; Q8SRK0; -.
DR OMA; GNDLHMV; -.
DR OrthoDB; 1012379at2759; -.
DR Proteomes; UP000000819; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
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; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Lipoprotein; Metal-binding; Protein transport;
KW Reference proteome; Repeat; Stress response; Transport; Zinc; Zinc-finger.
FT CHAIN 1..398
FT /note="Mitochondrial protein import protein mas5"
FT /id="PRO_0000383329"
FT DOMAIN 7..88
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 152..159
FT /note="CXXCXGXG motif"
FT REPEAT 166..173
FT /note="CXXCXGXG motif"
FT REPEAT 192..199
FT /note="CXXCXGXG motif"
FT REPEAT 207..214
FT /note="CXXCXGXG motif"
FT ZN_FING 139..219
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT REGION 367..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144..146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 221..222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253..255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 43986 MW; 279B09606F6545F5 CRC64;
MSKDPKGYYK VLELSPGASV AEVRKAYAKQ QAKYHLDSPY MKNKLKNAAS DEEREKIKKE
CGEMSARLNS AKSVLFDEKK KKEYDSGMGE FGAHFSGGGY SDIFDIFSQF TGGRGHQRTN
KVSSTKYVIT VSLRESFVGK VSKFNVRTEK VCTTCDGKGG KDVETCKKCN GNGVYTSRRS
LGGFVTLAET RCDGCDGSGH KIKGKPCSTC NGAEYIQDKT MFEVNIKPGV RKGEKIVFEG
MGDQRRGHVP GDVIFIIDVQ EDSRFERCGN DLVGNIDIPL YTAIGGGVVY FTHIDGRQLE
INVSPFRTFD TALKIRNEGF KGSRTGNLIL KPNIIIGSES DRAKIMQVLS APSKKPYGTF
TKVNSEFGSM PEPERDHEDA SEEGAQSARS FFNNFSFF
