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Database: UniProt
Entry: A0A0A2KC96_PENEN
LinkDB: A0A0A2KC96_PENEN
Original site: A0A0A2KC96_PENEN 
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
//
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