ID A0A0A2KC96_PENEN Unreviewed; 727 AA.
AC A0A0A2KC96;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE SubName: Full=Peptide methionine sulfoxide reductase MrsB {ECO:0000313|EMBL:KGO61980.1};
GN ORFNames=PEX2_014760 {ECO:0000313|EMBL:KGO61980.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO61980.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO61980.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO61980.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000256|ARBA:ARBA00007174}.
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:KGO61980.1}.
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DR EMBL; JQFZ01000027; KGO61980.1; -; Genomic_DNA.
DR RefSeq; XP_016602646.1; XM_016738752.1.
DR AlphaFoldDB; A0A0A2KC96; -.
DR STRING; 27334.A0A0A2KC96; -.
DR GeneID; 27674171; -.
DR HOGENOM; CLU_023589_0_0_1; -.
DR OrthoDB; 2728202at2759; -.
DR PhylomeDB; A0A0A2KC96; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd14279; CUE; 1.
DR Gene3D; 3.30.1370.110; -; 1.
DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
DR NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR PANTHER; PTHR46081; PEPTIDE METHIONINE SULFOXIDE REDUCTASE 2; 1.
DR PANTHER; PTHR46081:SF8; PEPTIDE METHIONINE SULFOXIDE REDUCTASE 2; 1.
DR Pfam; PF01641; SelR; 1.
DR SMART; SM00463; SMR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR SUPFAM; SSF160443; SMR domain-like; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS51790; MSRB; 1.
DR PROSITE; PS50828; SMR; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 130..173
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 459..545
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT DOMAIN 592..716
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT REGION 59..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 79812 MW; ABA195252459A424 CRC64;
MGDCGDELFK ELESTYCPPI DPALFVAIVS DFDLAIPTQV EQLRETLDVL NASAVEQENL
PFDPTGTTNL RNSDVSGSLI GESSDDASSN FTSWPSLENY EQENGDSNST SREAERIKGS
KLAYTFLGMT TADKAQNLIS MFPTITRLEA ERILEDCHDN LSRSMDVLLN LAFIEETQIA
REIPQQTPKE AAQDSQSSIP KSIDGFQAKE NQNGGGQKSR KKKKQKQRRV DLASHAMNNT
TNKWEAGKKD IEFLSSRACA LQREKIASTY HENSMSLCAT IRVLAQAHAP TDIHEIEDDP
VLVTQVGELS HKYPGINPLT LSGLIRIANN EIPAADELAD TLARRPDLTS VSNIISFVSS
PVALGDEEEN LAPTQQTDSA SDFMDFNEAA AAANSHFAAR SVALAQASQA ARRARSNPLY
GGASAYYRDV GNEQRQLAMR HLATASDRLV ARQSTQYDLD LHGVTVANAI RIARERVQAW
WDGLGDQKYV RGGGQHSHGG FNIVCGVGHH SLDRKSHIGP AVWNMLLKEG WRVELNRGSI
LLSSTRKPPH SKTSTKALIA APTIPFFGAF FSSNRTPEQT TETMSPPNQR SEDEWRAVLN
PEQFRILREK GTERAGTGEY DSHYPSKGVY NCAGCDAPLY TADHKFKSGC GWPAYFDSIP
GAVTRHVDTT FGMKRTEIVC TNCGGHLGHV FEGEGYQTPT DERHCVNSVS LRFTEDASAA
KNPRAKA
//