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Database: UniProt
Entry: K1W8C3_MARBU
LinkDB: K1W8C3_MARBU
Original site: K1W8C3_MARBU 
ID   K1W8C3_MARBU            Unreviewed;       634 AA.
AC   K1W8C3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=ATP dependent DNA ligase domain protein {ECO:0000313|EMBL:EKD13435.1};
GN   ORFNames=MBM_08518 {ECO:0000313|EMBL:EKD13435.1};
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:EKD13435.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD13435.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13435.1,
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).
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DR   EMBL; JH921450; EKD13435.1; -; Genomic_DNA.
DR   RefSeq; XP_007296407.1; XM_007296345.1.
DR   AlphaFoldDB; K1W8C3; -.
DR   STRING; 1072389.K1W8C3; -.
DR   GeneID; 18764453; -.
DR   KEGG; mbe:MBM_08518; -.
DR   eggNOG; ENOG502T390; Eukaryota.
DR   HOGENOM; CLU_431531_0_0_1; -.
DR   InParanoid; K1W8C3; -.
DR   OMA; HACRILE; -.
DR   OrthoDB; 2788069at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EKD13435.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN          11..202
FT                   /note="DNA ligase ATP-dependent N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04675"
FT   REGION          259..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  70501 MW;  2D18C03CD9C40947 CRC64;
     MSHKSHCNGI PFADFCMLLD KLEKIHDRTD TIALPKDRES RTYKALKKWF QTHKNRINTY
     HTADTSVLML LKPEYQVDRD YGFAEDFEQH LTTIFKLSSQ QCQYLKRWRE EPDYGDLGSR
     LCQVLKAKDH DPLRSCEIQP SVRGTDQKLL RLAIFNDGSA ETVKSLACQV EGIPSKISLL
     EDLYLDLLPT EAKWVTRMIQ KSYGVTKIPD EFEFLGEKSS LPDCLRVRII ASSEERILTR
     KHDVRARIQL PISPQDPLLW DSKTHVGANS KKPTALLDGQ RAPGRSTRAS AEVENSRKRK
     RFSHELDLKK SAACLLPTPP TSSPSTPHER SPTIGTRHGP RFRIGLDSAS SKLAPPVRID
     TPLTPAKSSP LPYSSSSHSA AISGSSKPTA AAKTNAPPTP VRSSPLPASS PTRSGGENRR
     SPVAKLGYSS TESSQGINHQ ALPSRSALSQ ISSNRSPGGS QKSQSKSTTK AIEAGSPPKV
     ITLHPARSPV TFSTGKCTLV SRIPKNRCRF ANTLIILSPC ISTFPYILED LILPHGAHYI
     TSLSQLSHPS VPRRSKSGRR LKKYILVEIN RPAQTVDFCK RAERKLRALG WKCDKGLDER
     IPIFDWRVLE DFARLDKGEQ LGHDPVGKHF QGAV
//
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