ID A0A162YSX8_DIDRA Unreviewed; 1385 AA.
AC A0A162YSX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=5-oxoprolinase (ATP-hydrolyzing) {ECO:0000313|EMBL:UPX10450.1};
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:KZM20209.1};
GN ORFNames=EKO05_0001110 {ECO:0000313|EMBL:UPX10450.1}, EKO05_001110
GN {ECO:0000313|EMBL:KAF9711601.1}, ST47_g8658
GN {ECO:0000313|EMBL:KZM20209.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM20209.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM20209.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM20209.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9711601.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9711601.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9711601.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9711601.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9711601.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9711601.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX10450.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX10450.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the oxoprolinase family.
CC {ECO:0000256|ARBA:ARBA00010403}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RYYQ01000003; KAF9711601.1; -; Genomic_DNA.
DR EMBL; JYNV01000284; KZM20209.1; -; Genomic_DNA.
DR EMBL; CP095289; UPX10450.1; -; Genomic_DNA.
DR STRING; 5454.A0A162YSX8; -.
DR OrthoDB; 674at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 2.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:KZM20209.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 12..233
FT /note="Hydantoinase/oxoprolinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05378"
FT DOMAIN 253..563
FT /note="Hydantoinase A/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF01968"
FT DOMAIN 578..757
FT /note="Acetophenone carboxylase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19278"
FT DOMAIN 782..1352
FT /note="Hydantoinase B/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF02538"
FT REGION 1285..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 150583 MW; 0342DEA63B181C2F CRC64;
MADIKKEGRG IRIAIDRGGT FTDCVGNPGS GKMEDDVVIK LLSVDPANYD DAPLEGIRRL
LERFTGAEIP RGQPLDTTKI ESIRMGTTVA TNALLERKGE AMAMVVTKGF KDCLEIGNQS
RPNIFALDIR KPEVLYKQVV EIDERVTLED YAEDPERNNT DAKSIEEAGA HAELVKGLSG
ETVRILQRPQ EDAIRKQLQD VYDSGIKSIA VCLMHGYTYP HHEALVGRIA KDIGFEHVSL
SHALMPMIKL VPRATSACAD AYLTPAIRKY IDGFSKGFEG GLGSESVKRE EGAKGARCEF
MQSDGGLVDV DIFSGLKAIL SGPAGGVVGY ALTSYDPETK TPVIGFDMGG TSTDVSRYGA
GRYDHVFETT TAGVTIQSPQ LDINTVAAGG GSRLFWKNGL FVVGPESASA HPGPACYRKG
GPLTITDANL FLGRLLPDFF PKIFGKNEDE GLDAQASEKL FQELAAQINK EVAGDNKDKE
MSLDDIANGF IKIANETMTR PIRSLTEARG HDTSKHRLAT FGGAGGQHAV AIAEALGVSQ
ILVHRYSSVL SAYGMALADV VDERQEPESK VWSDGNDVRQ YLQKKMDDLK SKSRTVLEAQ
GFDEQSIHFE EYLNLRYRGT ESALMIIKPT GEEAQKEYNG DDWAFGQAFI KQHEQEFGFT
LPDRDIIVDD VRARGIGKTF EGLEKTVDQQ LKEIKPKDLS NDEKRYDTRN VFFEGGRRET
SVYKLEDLEV GDRIRGPAII ADGTQTIVVT PGASALVIHT HVVINIGESD GSEKEISTKE
VDPILLSIFA HRFMAIAEQM GRALQKTSVS TNVKERLDYS CALFDAEGGL VANAPHLPVH
LGSMSTCVRK QAAIWKGKLK KGDVLVSNHP MFGGTHLPDI TVITPAFSGD NIIFYVASRA
HHADIGGILP GSMPPSSKEL YQEGAAIKSE KLVSEGHFNE KRIIELLSEE PAQYPGCSGT
RCLSDNLNDL KAQIAANQKG INLINTLMSD YGEQVVKFYM MNIQANAESS VRQLLKEVYK
RFEGQDLSAE EFMDDGSPIR LKVTIDPDKG EAVFDFSGTG PEVYGNINAP EAVTYSAIIY
CLRCLISEDI PLNQGCLKPI HVLIPKKSFL SPSDNAAVVG GNVLTSQRVT DVVLKAFKAC
AASQGDTNNL TFGFGGLSEG EDGGPRKETK GFGYYETIAG GSGAGPTWNG TNGVHTHMTN
TRITDSEVFE RRYPVLLREF SLRQGSAGKG MHIGGEGVIR DIEFRIPVQV SILSERRVYH
PYGMEGGGEA ACGLNIWARK VNRKNVDKNS DSKKQTEDSD ARTAGLGEVN GKDADTEDVE
YRFINLGAKN TASMQPGERI IIHTPGGGGW GAEGETSRVE DKKDPKAGWR GGSVAERQAA
GEASA
//