ID A0A423W572_9PEZI Unreviewed; 1371 AA.
AC A0A423W572;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=5-oxoprolinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VSDG_04236 {ECO:0000313|EMBL:ROV98497.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV98497.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROV98497.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROV98497.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the oxoprolinase family.
CC {ECO:0000256|ARBA:ARBA00010403}.
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:ROV98497.1}.
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DR EMBL; LJZO01000013; ROV98497.1; -; Genomic_DNA.
DR STRING; 252740.A0A423W572; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR InterPro; IPR049517; ACX-like_C.
DR InterPro; IPR008040; Hydant_A_N.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR003692; Hydantoinase_B.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365:SF2; 5-OXOPROLINASE; 1.
DR PANTHER; PTHR11365; 5-OXOPROLINASE RELATED; 1.
DR Pfam; PF19278; Hydant_A_C; 1.
DR Pfam; PF05378; Hydant_A_N; 1.
DR Pfam; PF01968; Hydantoinase_A; 1.
DR Pfam; PF02538; Hydantoinase_B; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000284375}.
FT DOMAIN 11..230
FT /note="Hydantoinase/oxoprolinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05378"
FT DOMAIN 250..555
FT /note="Hydantoinase A/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF01968"
FT DOMAIN 571..757
FT /note="Acetophenone carboxylase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19278"
FT DOMAIN 777..1339
FT /note="Hydantoinase B/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF02538"
FT REGION 1333..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 149902 MW; D35E2617EE60EFD6 CRC64;
MGSNQKERGI RIAIDRGGTF TDCVGNIEGE DIVIKLLSED PANYEDAPLE GIRRIMSHFL
KRDIPRGEPL DTSKIDSIRM GTTVATNALL ERKGEKIALV VTKGFKDCLV IGNQSRPKIF
DLAIRKPDVL YSEVVEVDER VTLEDYAEDP TRNTSKTEVR AGTAEAKNAD LVMGLSGEAV
RILQRPAEEE IRTKLQGIYD KGIRSIAVCL MHAYTFPDHE ALIGKIAQDI GFRHISLSSE
LMPMIKLVPR ATSVCADAYL TPAIRKYIDG FQRGFEGGLG TKSVRQGSGD KGARCEFMQS
DGGLVDVEKF TGLKAILSGP AGGVVGYAIT SYDPETKVPV IGFDMGGTST DVSRYGEGRY
DHTFETTTAG VTIQSPQLDI NTVAAGGGSR LFFRNGLFVV GPESAGAHPG PACYRKGGPA
TVTDANLYLG RLLPDFFPKI FGKHEDEGLD VEASRKVLQE LTDQVNQDMN KSMSIDEVAY
GFLAVANESM TRPIRSITEA KGHQSSKHRL ATFGGAGGQH AVAIAEALGI KQILVHRYSS
VLSAYGMALA DVVDERQEPE SAVWSNSGTV VGELKNKMEK LKEKSRKSLQ DQGFDDDEIV
FEEYLNMRYR GTESALMIVK PSQEDAKEHF GGQDWAFGEA FVKHHRYEFG FTLDDRDIII
DDVRVRGIGK SFRYSEETVD QQLKKLSRQE VSGKKKYSGA EVYFEEGRLD TPIYKLDDLE
VGDILKGPAV LADGTQTIVV TPKAEAVILQ THVIINIEDG EGIDESQGKD HSKLEVDPIM
LSIFGHRFMA IAEQMGRALQ KTSVSTNVKE RLDFSCAIFD STGGLVANAP HLPVHLGSMG
TCVKRQAEIW KGDLKKGDVI ISNHPSYGGT HLPDVTLTMP AFDEKGENIL FYAASRAHHA
DIGGISAGSM PPHSRELFQE GASIKSEKLV SEGKFNEERV VELFYKEPAK YPGCSGTRCL
ADNLSDLRAQ VSANQKGISL IENLIQEYGE DTVMFYMKQI QDNAEFCVRR LLKDVSKRFE
GKDLSAVDYM DDGSPIKLKV TIDADKGEAV FDFEGTGAEV YGNINAPEAV TYSAIIYCLR
CLISEDIPLN RGCLEPIHVK IPPKSLLSPS DHAAVVGGNV VTSQRVTDVI FKAFQACAAS
QGDCNNLTFG FGGNIAGQEE VKGFGYYETI AGGSGAGPDW DGTSGVHTHM TNTRITDQEV
FERRYPVILR EFSIREGSGG AGQHRGGDGV VRDIEFRIPV QVSILSERRV YHPYGLAGGE
DAQCGLNIWV RKVEKASWEK QLKRLKAGNS STSNGDHKDE DDDVVYEERH INLGAKNSAP
MKPGDRIIIN TPGGGGWGKV GQEKAHRKAA DPTQAWRKGS HAAREDTALQ V
//