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Database: UniProt
Entry: K1X1R2_MARBU
LinkDB: K1X1R2_MARBU
Original site: K1X1R2_MARBU 
ID   K1X1R2_MARBU            Unreviewed;      2005 AA.
AC   K1X1R2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Beta-Ala-His dipeptidase {ECO:0000313|EMBL:EKD18952.1};
GN   ORFNames=MBM_03194 {ECO:0000313|EMBL:EKD18952.1};
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:EKD18952.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD18952.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18952.1,
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01016}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; JH921432; EKD18952.1; -; Genomic_DNA.
DR   RefSeq; XP_007291083.1; XM_007291021.1.
DR   STRING; 1072389.K1X1R2; -.
DR   GeneID; 18759129; -.
DR   KEGG; mbe:MBM_03194; -.
DR   eggNOG; KOG2276; Eukaryota.
DR   HOGENOM; CLU_233831_0_0_1; -.
DR   InParanoid; K1X1R2; -.
DR   OrthoDB; 177966at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.490; -; 2.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF8; DI- AND TRIPEPTIDASE DUG2-RELATED; 1.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 2.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   REPEAT          190..221
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          348..374
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          1176..1297
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          1355..1494
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          74..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          912..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1627
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   2005 AA;  224778 MW;  18DC1A8806B0AD64 CRC64;
     MQNTYKTHLE DEEIFQLSLW NGCGQSPFEF AIPPTPLCDP DLPMLTSSAS GEEMEEMIWS
     DSDNSQMYGC QSERLAKGKD PPRDSSSPLA RAAKARSLHA QHTGVAAPRA DLSTAEARNE
     EPYEAEVLHR VADDTVPGVS LQEKPELAHH LQNDSSILTL AVGSRYIYAG TQDGEIVVWS
     LASFELVNRI QAHTRAVLCL FLSGDGNLLF SSAGDAIVNA WCPDSLNRLY HVYSTYDVGD
     VFSVAYSTQF QTVYLGAQNT SIQWCSLKES STRPSPCPDN HPDRRNHRFF DSVAVGGKHT
     PRPHTTRTGA DDGLVLEIDK SHMMQYAHFG YVYCMLLVRG ITRLVDADED VLISGGGDGT
     IKIWKLSYDN SQAIQEVARL GEDDAESVLS MAVDGSFLYS SKLEGVIELW DLDTKQKLRV
     IRAHKGDVMT LQMGWGYLFS AGSTGYARKY STVQYGKYQN SILFNQKYHC VNRWKAHEGR
     ILASALTTFN GQQLYITGAN DNSVSVWNIT GCDSTKAGKA EVAENQLLKS LQEFVSFKTI
     SSRPDHAEDC RRGATFLRTL FNKHGAQTEM LNTDGRHNPV VYARFKGKPA TSGERKKILF
     YGHYDVVPAD NKQNKWIIDP FDMKGINGYL YGRGVTDNKG PIMAALYGVV DLIHEKALEA
     DIIFLIEGEE ESGSRGFKEA VRRHKELIGD IDYIILANSY WLDDDVPCLT YGLRGVLHAT
     VKVDSSHPDV HSGVDGSYMM DEPLFDLTSI LAKLKGLHNR IQIPGFYDSI LPLTAVEEAR
     YDDITETLIR RNPENGPPET LKASLMARWR EPNLTVHRYK VSGPDGSLVS SHASAAISLR
     LVPNQEVEDV IQSLTAFLTD AFAKLDTHNH LSITIDNQAD AWLGDPDNEI FQTLEEAIMN
     VWGPIGEGRC SSVPGPRPKP QALKPGSPAM PSVSPSLKPT PATVTTLTNG SNHTSLAAIP
     LEPASLTSLV SSNSANGSKT KGRKPLYIRE GGSIPSIRFL EKEFDAPAAH LPCGQASDSA
     HMDNERLRIS NLYKSREIFR QVFKELPRNN PRKPDFSNLP LSEWSDFKGR SQKVGKTNIR
     RVPSQNVLGK TWVTPRIFKL WKFFYPNVME RVQLPGIAKG QRVVLESDSE DIMNELRTLV
     RDHTSSDAGA YRLGTQIWYN RKLDTQAFAS ITLGGVSYHP GDCVIVASEA QSEEPRFARI
     ISIFEDEDDE VSVHLRWFEV GSNTILGETA GPRELFLLTS CDSNPVNCIV AKVKVGFFGD
     QNSGRYDSVS DTIDHEDFGF YYRHHWNPNS KQFTSASDHE SNIYLGLGKK SLSGTCHCCK
     IMAERLQDEE TRILWDIVPD SKGRGIISGF CSRQVQYRTL DFVYLLPVDH SEPCRIGQIQ
     DIYLSRFSEV SKLTSTMVSD HDVRLKVAIY KRYDDLVPSR GQEHEPGRKF GIRDSRRLFF
     TGETIKIDGS IVDGVCYVLH RDHVDDLDSF KDQKDTFWVK DRLEEEIDWD SCVRPRDLRP
     LDSGSVRYSA TKFEHEKKMI LVREFLERGE KARTLELFNG IGGLTVAFKG ISGITNAVEI
     DPAACVTMRN NQPGVIVHKG DASNLLLRAI KRDQGAKLGK LFDGKGNLIP DLPFRDQVDF
     IKGGPPCPGY SVANCQKKDG EPKNSLVALY SAYVDFYRPK YSLIENVTGL IHHTLRTPES
     NDFKTKPETL ENGTIRMIYR TYTSMGYQVQ CAVLYAEEHG SPQSRPRVII WATQPGCRLP
     EYPQPEHLWK TRAACPIFMP GSKLNQSDFH WHRKRRSTPH RVVTLGDAWI DLPEYDIKNP
     HLIIPQTRFQ KFEAEQRRNK ITFYDSLDGE SYVGSDNQTY ASGPKSEYQR IMRKGTTDNV
     ITAHVTRKLT SINTERVCTI PLVTEANHES LPVALKFRSR NSTPVYSPKK CCRLALDGIH
     NVCMTELEVA GKYGNNWRVE DAIRGIGNAV PVPLGASLAE GFLDSWMQYI KNRDRIEPRY
     EEPAARNPVR VVHQEVIVIP DSEDE
//
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