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Database: UniProt
Entry: A0A072PUY4_9EURO
LinkDB: A0A072PUY4_9EURO
Original site: A0A072PUY4_9EURO 
ID   A0A072PUY4_9EURO        Unreviewed;      1136 AA.
AC   A0A072PUY4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ATP-dependent DNA ligase family profile domain-containing protein {ECO:0000259|PROSITE:PS50160};
GN   ORFNames=A1O9_01644 {ECO:0000313|EMBL:KEF63666.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF63666.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF63666.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF63666.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEF63666.1}.
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DR   EMBL; AMGV01000001; KEF63666.1; -; Genomic_DNA.
DR   RefSeq; XP_013266256.1; XM_013410802.1.
DR   AlphaFoldDB; A0A072PUY4; -.
DR   STRING; 1182545.A0A072PUY4; -.
DR   GeneID; 25276590; -.
DR   VEuPathDB; FungiDB:A1O9_01644; -.
DR   HOGENOM; CLU_278373_0_0_1; -.
DR   OrthoDB; 2788069at2759; -.
DR   Proteomes; UP000027920; 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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; 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   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45997:SF2; ATP DEPENDENT DNA LIGASE DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_5G02430); 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT   DOMAIN          384..529
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          715..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..772
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1136 AA;  127328 MW;  5D6A3660F8B3D52B CRC64;
     MAAKTEFQFR WLVELLDKLS LTNRGHPLSL DIARQHTLAW FKKHGDKIIR HGPSALAFLA
     CVLPNRLPHR TYGLREKRLA DIVANALRLP NPGRRRTKLE SWTTGADFAT LVEEVMHEAE
     NPPARKQVTL EELDAALCEL AANSGFLAPQ MQRFRTNRPR YRILEPILRR LSSKEAKWLM
     RMLLKAYSSA AIPEQAVLRS FHFLLPDLLA IQNSFEAAIN TLNHEDMQNI PHNPPMEDRD
     GFRQLAAKCM HPKLGVMIQR QPYDKGRSIK HCLNMAEGRT MSVERKYDGE YCQIHIDVLK
     PHDRRIQIFS KSGKDSTADR QGLHWAIKES LQLDDAQCKI KANCILEGEL LVWSRLKEKI
     QPFHAIRKHV LHGGRNIGTA ADSPRSKDDH LIIMYYDLLY LDNESFLNSP LRERRLCLEK
     VVNPMDGVGM IGTRNVVNFR LRDAQNILCT LFVRSIRETW EGLVLKGMQD PYFSWERRPR
     VIKLKRDYVT GLAQSVDLCI IGGFREQLVV DQLGVGDLSW TSFYLACFDN KDEVEEFQAL
     PKFRVVDVLN TNCISKADII HLNREGQYRR MDAAEASQCL DVSFERNGPR RSGQLFRKPF
     VVEVMGAGFE KPSDAAYFTL RFPRVRLHLD RTFVNTSSFD ELQAMAKESF KPVRNSDTED
     IVRRIQKANG KHAIVEEGWS QETCREAAAS SAASTPVMPI SRSNGLLIAH TTGSSSAQLG
     PISLSRPPPT IQTEGPIAPP GLNRRQPGSE VQSHHPEPTE ARDQDRRSSE GRDLYMGSSL
     SSITHLPLNE NPNPLNTRGN RRPLEQDPAG EIAQNPDSKR TKSQPCATVR CRVGASSLAM
     LNSTFLKKRF QCTVPNDSRW KEKGVQVLAH ICRTPSPTAV ASVSRILTSH WCTGTDNPVF
     GRQSGCKCSN CRLILIIVAD ESKLVDVARD LKETSAAVAD IRKQALEKLS LNPRFGKLTH
     QGGENDQKLV VFLLKSARPA ISEIEKEVKE ISTAYGWYVT RLNKVFKDHF AGAIFFSFPK
     PFFSPAMAWS LFQGVKGAPD FAIQDADGAH DHLRRLVALG LPMQSKNLAT HSVAALGSGS
     GVGPGPSHPG VEGTGSHFPA VTKASQLESQ GSTQLEWKWS KVCKLMGSLG CDADQV
//
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