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Database: UniProt
Entry: A0A0G2GGI4_9PEZI
LinkDB: A0A0G2GGI4_9PEZI
Original site: A0A0G2GGI4_9PEZI 
ID   A0A0G2GGI4_9PEZI        Unreviewed;       886 AA.
AC   A0A0G2GGI4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=dihydroorotase {ECO:0000256|ARBA:ARBA00012860};
DE            EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860};
GN   ORFNames=UCDDS831_g03453 {ECO:0000313|EMBL:KKY22738.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY22738.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY22738.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY22738.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY22738.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY22738.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004880}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003945}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU003945}.
CC   -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family.
CC       {ECO:0000256|RuleBase:RU003945}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class II DHOase subfamily.
CC       {ECO:0000256|ARBA:ARBA00005631}.
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:KKY22738.1}.
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DR   EMBL; LAQI01000073; KKY22738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2GGI4; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000034182; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd20069; 5TM_Oxa1-like; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   HAMAP; MF_00219; PyrC_classII; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR028055; YidC/Oxa/ALB_C.
DR   NCBIfam; TIGR00856; pyrC_dimer; 1.
DR   PANTHER; PTHR43137; DIHYDROOROTASE; 1.
DR   PANTHER; PTHR43137:SF1; DIHYDROOROTASE; 1.
DR   Pfam; PF02096; 60KD_IMP; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Transmembrane {ECO:0000256|RuleBase:RU003945, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        315..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          159..352
FT                   /note="Membrane insertase YidC/Oxa/ALB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02096"
FT   DOMAIN          523..785
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          396..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  96583 MW;  115335F1521E3528 CRC64;
     MMKSRGLRPA NCARLALQNP LRAPRQFSTH ASLRAPVLLR ARNPSLDLRS ALNAPGLRTP
     FAVGSAASAI RFASTSPAAA TSSVLENSKA AAADATSSAP VEAAASSVDG VTDEFLANLA
     NMPEQIGYLK AVGLDYGWGP TSCIEWLLEH VHIWMGIPWW SSIVVTAIIV RTSLFPLFAR
     TSDVTARQQA LKEITDPLNA KMNAARIAGN TDQMMMARTE LMGVYKHAGI NPWKAFYAPV
     AQAVTGYCTW KLLRAMAALP VPGLENGGFL WLSDLTVPDP WFILPISFGA LIHVVAKSGG
     ETGALKQFTG LQKKFLFYFM PGLAILFTIA QPATVQFSFF AASTLGMLQA KLLRSPTVRD
     WLSLAPIVGG PQPNPSNPGV IDVQARVTSP GEFKWEPPTV QSSISKSGPI NKKINKKPVS
     KGPFDGLKKS YMETRQELQD FKDGIMKRAG MYEDNTKGRT QSKQFLKRAE EYENRRQAER
     DMDFFSIGRA VDFMCIYLYT DDAFVHTADD PTMPLDKFDG LELPAAADMH VHLRDNAMME
     TVTPTIRQGG VNTVYVMLTR PLSSLCPGQP NLVPPLTTVD ATLAYRARLQ AVEPNVTFLS
     SLYLHPDITP DTIVAAKKAG VTGVKSYPAG VTTNSAAGVV DYAAFYPVFA EMERQDMVLN
     LHGELPPSAA SADAEDITVL NAEERFLPTL RELHARFPRL RIILEHCTSK AAIEAVEACG
     PTVAATITAH HLYLTVDDVV GNAFHFCKPV AKLPADRLAL LRAAARGGSK FFFGTDSAPH
     PITAKSGPGA AAGVFTQPYA VQLVLDAFEA AVTKGWLKEE EVTRESLEGF LSGYGRAFYK
     VGDERGERIV LRRKGEKVVE VVRHKEGEVE VVPFRKGQNT WSVEWK
//
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