ID E2LSA1_MONPE Unreviewed; 469 AA.
AC E2LSA1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 13-SEP-2023, entry version 54.
DE RecName: Full=Carboxyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MPER_09905 {ECO:0000313|EMBL:EEB91700.1};
OS Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS disease fungus) (Marasmius perniciosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB91700.1, ECO:0000313|Proteomes:UP000000741};
RN [1] {ECO:0000313|EMBL:EEB91700.1, ECO:0000313|Proteomes:UP000000741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT "A genome survey of Moniliophthora perniciosa gives new insights into
RT Witches' broom disease of cacao.";
RL BMC Genomics 9:548-548(2008).
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:EEB91700.1}.
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DR EMBL; ABRE01014979; EEB91700.1; -; Genomic_DNA.
DR AlphaFoldDB; E2LSA1; -.
DR STRING; 554373.E2LSA1; -.
DR KEGG; mpr:MPER_09905; -.
DR HOGENOM; CLU_020207_4_2_1; -.
DR InParanoid; E2LSA1; -.
DR OMA; EVHFNSD; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000000741; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR010016; PxpB.
DR PANTHER; PTHR34698; 5-OXOPROLINASE SUBUNIT B; 1.
DR PANTHER; PTHR34698:SF2; 5-OXOPROLINASE SUBUNIT B; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000741}.
FT DOMAIN 1..172
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000259|SMART:SM00797"
FT DOMAIN 216..450
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000259|SMART:SM00796"
SQ SEQUENCE 469 AA; 51465 MW; E4CB1D6F3016944E CRC64;
MAWSLYGEVV CGAATPMAQT PGLSKGSIPV YPSHWTIHVL PGPHGDSEYV TPAGIEKFYA
TTWQVAASSN RMGIRLDGPG RIAWARENGG EGGSHPSNIL DNGYALGTLN INGDTPVILT
HEGPDMGGYM CFCTIASADL WKTGQLSPGS TVQFERLTWE QARSLHQSIE SWLREVQTAV
EQGGVAELKS VPLPVHEEAC YDPKLRVISS PNRPQVVFRQ AGDSCILVEL GPMKLDFTIR
ARIHAFEEEV KQRKIPGVVR FCPCVRSTMC HYEPSAVSSV SELVDALVDA EAALGDDVAD
MTFPGRRITF PVVLDDSWSR DAITRYMRTT RSKAVYLPSN IEYLAINNGL NSAQEALRKL
VGSDWVAFGV GFYLGCPFLV PVDPRCRLVG QKMNPSRTYT PRGAIGIAGV VAAIYPVESP
GGYQLYGRTL PTWQTWGRGG DFAPDRPWLL GPFDQCNSNF EHIYEEEYS
//