ID M2T6S1_COCSN Unreviewed; 1584 AA.
AC M2T6S1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCSADRAFT_198911 {ECO:0000313|EMBL:EMD64662.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD64662.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD64662.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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; KB445642; EMD64662.1; -; Genomic_DNA.
DR RefSeq; XP_007699271.1; XM_007701081.1.
DR STRING; 665912.M2T6S1; -.
DR GeneID; 19134082; -.
DR KEGG; bsc:COCSADRAFT_198911; -.
DR eggNOG; KOG0256; Eukaryota.
DR eggNOG; KOG2179; Eukaryota.
DR HOGENOM; CLU_003639_0_1_1; -.
DR OMA; DKRQPWD; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000016934; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR018327; BHD_2.
DR InterPro; IPR004583; DNA_repair_Rad4.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR InterPro; IPR042488; Rad4_BHD3_sf.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR PANTHER; PTHR12135:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-C CELLS; 1.
DR PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF10403; BHD_1; 1.
DR Pfam; PF10404; BHD_2; 1.
DR Pfam; PF10405; BHD_3; 1.
DR Pfam; PF03835; Rad4; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SMART; SM01030; BHD_1; 1.
DR SMART; SM01031; BHD_2; 1.
DR SMART; SM01032; BHD_3; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934}.
FT DOMAIN 1060..1117
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 1119..1182
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 1189..1263
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 415..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..496
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1584
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1584 AA; 176900 MW; 99574A7CF15F1C4E CRC64;
MLSARGRQYA ALDLAAGYTK VRGPLYNKDT HPDGLVSFKN AENFLMHDEA LDYIKTKCIP
SLEPESLTYH DGPFGSKRLR AAMASFINKR FSPASTVAIE HVSFVSGVTA LNDILSLCMT
DGENDALLLG MPIYGSFVPD LQSMSSCKLV YASFGDVDQF GVNSVECYER TLLQAEQSGI
KVRALVLANP HNPLGQCYSL DALKAILSFC NKYKIHLISD EIYAYSVYHT DASSPGFTSI
LSLDTAGFID NDLVHVMYGM AKDFAAAGLR LGCLITRNTE LGQALQSLSR FHGASPMADA
IATCILEDEE WHLQFFNKSA HILREHRKIA AEAFDSAGIP YERKAPTWEA EDDLKDRLYD
FGMEMAAARG YHGEMPGHFR FLFSVDKDTV EEAARRIVEF YKNNKVGRID MPPILARKRL
HSTSPVPESP PKRARTTRKP SAPARTGKVS VFQTLDAPPK TKRTLLQTKA LLEEEEEEED
GDGESSEPES TEDEFEDVPL NGATKDKGKP KARPDEDSDE SEDGDWEDAL GTHHHTKPDH
GPAPVITGDI ALTLSAAPKT VFETKPDGKK GPSKVQRQIR TVTHCMHVQF LMFHNLIRNA
WIQDKEVQKT LVQAMSPGCW RELEKYWNDA GIRDGSSRVV VQKPPSPKKK EPKASKGKWK
ESGKAGVKVY ESPQKRIDVR NKAKGKGEKP SERDKKTRDW GAAAEPLEPN SPNLSAGDPL
IRLLKYLSAY WKSKFQITAP SLRKRGYLSP SVLEAEIKAW KDDPNHPDTF GERVEDIAAF
RECAKKCQGS RDIGEQLFTA LIRGLGIEAR MVVSLQPVGF GWSQNEEGKP KNLKKLNNSK
SADNQNTEKE TPTSSKAKKP ATAKKTDGSV DVSMDGSSDL SSVISISSDS EDNRPPKRSP
RARNYGEELP YPTYWTEAIS HLTHTPISVS PLPRTIIASA ASPDKLVDFY ARGAAVDKAK
QILAYLIAFS SDGSAKDVTT RYLPKHQWPG RTKGFRMPVE KVPIHNKHGK VKRWEEWDWC
KSLMRPYTRA HDKRQPWDEV EDECDLVPAQ AERKKGMDEE GGKETLQGYK NSTEYVLERH
LRREEALRRG AKIVRFFITG KGDNEKSEPV YRRKDVVLCK TQESWHKEGR EVLEGQQPLK
LVPMRAVTVT RKREIEERER IEGGKVKQGL YSKEQTDWII PDPIVDGKIP RNAFGNIDVY
VPTMVPKGAV HVPLKGTARI CRKLNIDYAE ACTGFEFGKQ RAVPVITGVV VAAEHEDMLI
DAWEAEEVEK QRKEREKREK FLLGLWRRFA SGLRIVDRMR EEYGEDMELP VKEEVLPSKD
EEEKPKTGQS QWEVFEAQTD FEGGFVREDV ELSGGGGFVP DKAHQTAGRD LDMAGSFLPA
SQEEDVELTI DHGEKKDVRA PVVETAYRTP ISLTQALQRP PSEPSENPDA NEATSIDQDT
EDEGKRNDED EEYEHSKLES DHRKSTTATS GGRGRGRPRG RGTKAPARLT RKPNSTGDEL
SNGALSDAPS NPQSPPPSRR SAPRRKAARK SDAHVRSHFF AEASEDETDL TDMTDRTSPK
KKSTRGRGTG RGRGRGRGKA GKAK
//
