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Database: UniProt
Entry: M3D9N9_SPHMS
LinkDB: M3D9N9_SPHMS
Original site: M3D9N9_SPHMS 
ID   M3D9N9_SPHMS            Unreviewed;       788 AA.
AC   M3D9N9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Isochorismatase hydrolase {ECO:0000313|EMBL:EMF14589.1};
GN   ORFNames=SEPMUDRAFT_132215 {ECO:0000313|EMBL:EMF14589.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF14589.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF14589.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF14589.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SIMILARITY: Belongs to the isochorismatase family.
CC       {ECO:0000256|ARBA:ARBA00006336}.
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DR   EMBL; KB456262; EMF14589.1; -; Genomic_DNA.
DR   RefSeq; XP_016762710.1; XM_016902482.1.
DR   AlphaFoldDB; M3D9N9; -.
DR   STRING; 692275.M3D9N9; -.
DR   GeneID; 27899619; -.
DR   eggNOG; ENOG502QRZN; Eukaryota.
DR   HOGENOM; CLU_005335_0_0_1; -.
DR   OMA; KMYHLSG; -.
DR   OrthoDB; 1644896at2759; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR   CDD; cd00431; cysteine_hydrolases; 1.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR032854; ALKBH3.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   PANTHER; PTHR31212:SF5; ISOCHORISMATASE FAMILY PROTEIN FAMILY (AFU_ORTHOLOGUE AFUA_3G14500); 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EMF14589.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT   DOMAIN          600..719
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          276..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..300
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  87073 MW;  14D690AD72A7BE8C CRC64;
     MSFLSALLSQ QTPNLQTRKG LIVVGLQNDF ILPDGKLPVK DAAFVNRIGS LVPAFREHGE
     IIWVRSEFQQ TRPVNGDDTP GDRVIAAGSL GTGLDRQRSG DVPAANKKYK FSASFEKPEA
     GKEEGDDEEL FLSRTSKREP CCIKGSHGAD FSDRIKPLIQ RKDLQVVKSH YSAFAGTSLL
     MTLRSKLITD VYICGCMTNL SVYATAMDAA RYGIEITLVE DCLGYRRFDR HQMAVQQLNH
     FMSANFWKSA RVLAQLLDPS LEFPSSDSGA IEVVVEEEDD DDDDDDDDED EDEEEQTEEQ
     QHKGEEEKQE KEATEGSTVM GDRRSTLLQA QADVLEVDSD EHSDEEVSLP TVGLPRRLLD
     RISERSFATR LSSKYSPRAA RRPRITTTQY ATPESPRSDP RHNDPGHESE KGAIEFGKLK
     FATASGHSRL ISTHSGSSRQ VSRLPWLDII PPNYKSSQDI GPPASSHQQG SPCAPSQSTA
     SPPSSGGKKP KAMSTCSQKS RPLFGEDKVA ESAGSRILHG LLPEDAAETA FEDVQSEVKW
     QSMFHQTGPV PRLVSCQATI CDDGSVPLYR HPSDQTPEVH AWTPTVDRIR KAAEQVAGHR
     LNHALIQLYR DGNDFISEHS DKTLDIAPDS NIVNVSMGAQ RTMRIRTKRG AGTGSGNTAE
     ARTTYRVPLP HNSMVTMSLQ TNAEYLHAIP WDRRPPCELV EAEKAFGGQR ISLTFRCIAT
     FLSQDRTMIW GQGAVGKSKD TARRVVHGDP EESQKLVDAF GKENAASSIE WKEIYGSGSD
     VLHLKQQQ
//
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