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Database: UniProt
Entry: K1XMT9_MARBU
LinkDB: K1XMT9_MARBU
Original site: K1XMT9_MARBU 
ID   K1XMT9_MARBU            Unreviewed;      2466 AA.
AC   K1XMT9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Hydantoinase B/oxoprolinase {ECO:0000313|EMBL:EKD13784.1};
GN   ORFNames=MBM_07985 {ECO:0000313|EMBL:EKD13784.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13784.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD13784.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13784.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SIMILARITY: Belongs to the oxoprolinase family.
CC       {ECO:0000256|ARBA:ARBA00010403}.
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DR   EMBL; JH921448; EKD13784.1; -; Genomic_DNA.
DR   RefSeq; XP_007295874.1; XM_007295812.1.
DR   STRING; 1072389.K1XMT9; -.
DR   GeneID; 18763920; -.
DR   KEGG; mbe:MBM_07985; -.
DR   eggNOG; KOG1939; Eukaryota.
DR   HOGENOM; CLU_000894_0_0_1; -.
DR   InParanoid; K1XMT9; -.
DR   OrthoDB; 674at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd06093; PX_domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
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   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR013937; Sorting_nexin_C.
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.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF02194; PXA; 1.
DR   SMART; SM00313; PXA; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS51207; PXA; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN          136..318
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2422..2466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          369..403
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1548..1575
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        472..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..795
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2433..2456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2466 AA;  268255 MW;  DC7A50BAAEC86EFE CRC64;
     MDGISEETKQ EEGPGAVANA PESTHHIMPD EEDLMTRTLN FLSTASSETI VGIAVGLAAC
     TYMILGRVGL ILIGALGGVV LHATWEGEIS AAVEDGRREK SLDVVSRILD LRAVQQRINE
     DNENNEMVGN SFEGFQPETA AALNELVDAV IRDYVKRWYQ PLLPAEASFP AASRQTLTKF
     IVAISQHLSR KRHADTFLDF LTNSSSIVIV FLNELSTALS VSQGNNVSPA EAIQIYLSTN
     PESNLANVLN EKQQSRKFKI VAEDILQNFL EKSTYDCDPA RAFLREILAG LILQMSLETF
     SNPEFINGCI VYLLEDGEPD LSQAIDVGMG GSNVNNSLGA SSYDVDGNLG NIGLAKPSRL
     QSEQQTQEDK GHQKRLSKAE EAMEEAMEEA KRLSQLIAEE DAKRLFVEQG PLDDDSEALV
     AAAQHNAHCQ HLDTSGLMRK EASALAKTAE LISNGAATPM ALQSAGDKHK LSTDVTTPEP
     PDAAHRESQD LVSPPHPSAS LTSASAPAFT SFDQIIPQST PVALQEEPPV HRSKSFSLTL
     HNANIIIDDD SMVSDKGRLR SKPSTDYLVQ IEPASSDFPG WMIVRRYPDF ESLHEVLRRI
     AQIAGVKAFV EQHHTLPNWK EHTKPSLRGE LERYLRDALW YKELAESEGM KRFLDKDRGQ
     SASTTTTKNG FPGLGWSTPS AFENMGKGML DVLTSAPKGV AEGGKAIGGG ISGVFTNIGN
     LGQKKPATGS SINLVQHTAA RSSTSALPKM DSMNSVIAPK TSRMSEDSFR PTSIVQMQPS
     PMPSMERQPS NNLLAEGDNE REPHVSASAR SSMSSRRSVT YNRDLSRASS RLATPLSSPT
     QGILGEMKLP PLPDDIPDDY GSSIDASSFS NLRTESSAAT ARTSTSTAPS SQSPGCPPLS
     AANRSSIQSA TPIRKQSREQ TPITEAETRV AVELLFAVVS EVYTLTSVWN IRRTLLNGAK
     AFLLRPSNPS LAAIQSLIQE SIIASNTSDA GLSSHLRKLR ENTMPTEDEL KVWPAAMSAE
     EKEKLRIKAR KLLVERGMPA ALTGVMGQAA SGEAVGKIFD CLQVEEVAKG LMYGLLLQAS
     QQGLGLTASS KSKSVFLVFS DTASKMCSQA EARGIRIAID RGGTFTDCVA NPGSGKMSDN
     IVIKLLSEDP SNYDDAPLEG IRRIMSRFLN KEIPRGEPLD TSKIESIRMG TTVATNALLE
     RKGERIALVV TKGFKDCLEI GNQSRPKIFD LAIRKPDVLY ECVVEIDERV TLEDYAEDPE
     RGSTKVEGNG SEKDLVKGLS SEAVRILQRP VKEKIQSQLQ EVWDRGVKSI AVCLMHGYTF
     SEHEALVGKI ARDMGFHHVS LSHELMPMIK LVPRATSVCA DAYLTPIIKK YIAGFQTGFE
     GGLGTESVKH ENGSKGARCE FMQSDGGLVD VDKFSGLKAI LSGPAGGVVG YALTSYDPET
     KTPVIGFDMG GTSTDVSRYG LGRYEHVFET TIAGVTIQSP QLDINTVAAG GGSRLFFRNG
     LFVVGPESAG AHPGPGCYRK GGPATVTDAN LFLGRLLPDF FPKIFGKNED QGLDVEASEK
     LLKELTEQIN KETGKNMTAD EVAYGFLTVA NEAMTRPIRS LTEAKGHDTS KHRLATFGGA
     GGQHAVAIAE SLGIRQTLVH RYSSVLSAYG MSLADVVEER QEPDSKIWAD KGDSRDALLK
     KIEDLKQKSF TALKEQGFKD DSIVFEEYLN MRYRGTESAL MVVRPSKEDA EKEFDGDDNS
     FGKAFVKQHQ QEFGFTFDRD IIVDDVRVRG IGKSFEDLGK TVDQQLKEIK PTDVKTGDKE
     YKRSKVYFDG ARHDTPIYKL EDLHVGDRVN GPAILCDGTQ TIVVPPETSA LIIETHVVIN
     IREKELNNEA SKSDSTKETD PVMLSIFAHR FMAIAEQMGR SLQKTSVSTN VKERLDYSCA
     LFDSTGGLVA NAPHLPVHLG SMSTCVKRQA EIWRGKLVKG DVLVSNHPEF GGTHLPDITV
     ITPAFDQAGE NILFYCASRA HHADIGGILP GSMPPHSREL FQEGAAIKSE KLVSAGKFNE
     ERITELLLSE PAKHPGCSGT RCLSDNISDL KAQISSNMKG INLISSLIEE YSEDVVNSYM
     VAIQANAELS VRNLLKDVSK RFEGQDLTAI DYMDDGSPIK LKITIDAEKG EAVFDFDGTG
     PEVYGNTNAP QAVTYSAIIY CLRCLISEDI PLNQGCLKPI RVLIPPKSFL SPSDKAAVVG
     GNVLTSQRVT DVILKAFQAC AASQGDCNNL TFGFGGNLEG QQSVKGFGYY ETIAGGSGAG
     KDWEGISGVH THMTNTRITD AEVFERRYPV LLREFSLRPG SGGAGKHRGG DGVVRDIEFR
     IPVQVSILSE RRVYHPYGLE GGEDGECGLN IWVRKVETSN AERSDRMLNG SVDGIEEATY
     EERWINMGGK NTAAMRAGER IIINTPGGGG WGKTGERKEE RERERDPKHG WRGGSHTNRE
     ETALQA
//
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