ID M2SS69_COCSN Unreviewed; 1060 AA.
AC M2SS69;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0000259|SMART:SM00849};
DE Flags: Fragment;
GN ORFNames=COCSADRAFT_199303 {ECO:0000313|EMBL:EMD65110.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD65110.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD65110.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000256|ARBA:ARBA00006759}.
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DR EMBL; KB445642; EMD65110.1; -; Genomic_DNA.
DR RefSeq; XP_007699603.1; XM_007701413.1.
DR AlphaFoldDB; M2SS69; -.
DR STRING; 665912.M2SS69; -.
DR GeneID; 19134091; -.
DR KEGG; bsc:COCSADRAFT_199303; -.
DR eggNOG; KOG0813; Eukaryota.
DR eggNOG; KOG2844; Eukaryota.
DR HOGENOM; CLU_007884_11_2_1; -.
DR OMA; PMKHAYI; -.
DR OrthoDB; 1815533at2759; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000016934; Unassembled WGS sequence.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 655..982
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMD65110.1"
SQ SEQUENCE 1060 AA; 116778 MW; 4F037E85860138A7 CRC64;
MATSQRVVII GAGIVGTNLA DELVSRGWKD ITVVEQGPLS MPGGSTSHAP GLVFQTNPSK
TMTLLAKYTV EKLSALEKDG QNCFNQLGGL EVATTPERLE ELKRKHGYAQ SWGIEARLIT
PEECLEKYPL LNKDIVLGGL HIPSDGLALA ARATQILIEN TRNAGVKYLE HTLVTGIEQA
NGQVTGVTTN NGSIPADIVV SCAGFWGVEI GAMIGLKVPL LPLGHQYAKT TPVPGLENRE
VNRKINAMNA EYPILRHQDQ DLYYREHGEQ FGIGYYGHRP MPVKASELGV TPKHVDEKSM
PSRLDFTPED FEPAWQATKE LLPALRQTEI VDGFNGIFSF TPDGGSVVGQ APNLDNFWVA
EAVWVTHSAG VARAVAETLT EGRSTVDISE CELTRFEEVQ LSPEYVSETS QQNFVEIYDI
IHPLAPKESP RNLRVSPFYA RQKEQGAFFL EIGGWERPHW YEANAGLVQT LPDEWKPVDR
DAWSSKFYSP IAAAEAWKTR NAVALYDMTT FHRFEVSGPG AVHLLQRLIT SDVSAQPGSI
VHTLLVNAHG GVLSDLFVSR IEEDLFQVGA NTATDLAYLI REGRRQEKHT PGKWVQVRDI
TGSTCCLGLW GPRARDVIQT ISSDDFSNKG LPYMGVKKTS IAGIPVTMFR KSFVGEYGWE
IQTTPDFGLR LWDLLWQAGR PHGLIAAGRA AFNGLRIEKG IRASGSDMNS EHNPWEAGVT
YAIQLDKKAE YVGKSALERL SKKAAPRRLK CLTVDDGRSM VLGKEPVFVE GQRAGYVTSA
AFGYTVRKPV AYAWLPSNIS EGASVEIEYF GKKIKATVTR DPLHDPQERR LRGEGSTAQP
ELQKRVLPVL KEQTTTGGLK LTKIINTHHH DDHAGGNTEI LEAFNVPVIG GRDCKKVSTT
PGHNDTFNLG SINVKALHTP CHTQDSICFY FEDGNDRAVF TGDTLFIGGC GRFFEGTPEQ
MYKALNETLA ALPDDTKVFP GHEYTKGNVK FAKTVLNNDA IKKLDTFSQE NKETQGKFTI
GDEKQHNVFM RVTDPELQKV TGKTAPVDVM GALRALKDKS
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