ID A0A371DNQ0_9APHY Unreviewed; 1066 AA.
AC A0A371DNQ0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP-dependent DNA ligase family profile domain-containing protein {ECO:0000259|PROSITE:PS50160};
GN ORFNames=OH76DRAFT_1479204 {ECO:0000313|EMBL:RDX54175.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX54175.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX54175.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX54175.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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DR EMBL; KZ857385; RDX54175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DNQ0; -.
DR STRING; 139420.A0A371DNQ0; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:UniProtKB-KW.
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; IPR016059; DNA_ligase_ATP-dep_CS.
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; DNA LIGASE 4; 1.
DR PANTHER; PTHR45997:SF1; 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; PS00697; DNA_LIGASE_A1; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 456..568
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 763..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 117257 MW; FF31D7BA70EFA04C CRC64;
MSALTDDSGI PFAFFTELVD AIAKVRPHKA SEKQPRTTRY ADTPVCKTFR RWVERLRELY
APLPPGTAAM IFRLLFPEED VKRKYSLQEA GLAQYLVKIL GVSSETHGRG ERLKKWKEED
AKGCLGDEVR DVMLGTAHSQ GSTFAVTIAQ VDALLTELAA KCGFSAAGVH ASFSATNSPR
RSRQAILTTL YHSLSPAESA VVTQIILKDL RPLLYPIPRS ANHYTAALLQ YNSNAIAQLS
KESAMYAWDP SGRMAVIYKT RADLDEAAQT YERLKPGDPM PDPVCGTPIQ IPKCSKGQGI
VQALKLLQGA DKVWVETKYD GERAQIHVRL DETGNPHIKI YSKSGRDSTR DRAGIHDIVC
EALGVSQGHN LSNKQGVAPA EASFRQDIVV EAELVAFSEA TDRIDEFWRI RSLIASTAVG
VRHKTPPAPP STAEGMDSQC SMLSNGSDGG TRHLALVFFD ILLLDGTSLL SFPYSERRAT
LEGVVRVIPG YSMLAERVCI DMKRAEASDT LRKAFATLIA DYQEGAVLKA DGAQYGERRW
PWLKRDYIKG YGDTVDLVLL GAAWEKDRAR ELRVLPTAYT TFYFGLLANA DERKSNPSCR
PHFEVVFTSA YGLSRQELEE VNFMIKNSDM VPYCEQAIEG LPYRFKLCPN LRPPAVLLQQ
PLLAELFGAG FSKAQSSMFY DLRFPRMTKV HRPSERPWSD GLTLQEYQQI ARAAVGRDRP
GKAEDDCVKA MFHPHQPASP GVRCPKKRKQ MEMLWIEKLE VADGKKRGGA SPSKRARLNT
VGPRRKTVDV GNAENIAEAG VPIDENTPEA GTEGLRARLG MARLTSVTNV TAAAASSPVR
HPLGSGPGSS RVSEPSPVSI RDLPPTDRTP SRAEPPRASP PVATPPGMPL PQTPPPTMAK
PAPSLQGPQP TLILKREDDD CSRILDVRTN SASPTTLHHF LQDSVVWLAR PPRTARPSWR
APSCAVIPKG NQVSTLDAVT IACGWGSTPA CKWSNRGVVF VDVSEILFLQ DTLHELASRR
AALLGHKDIA RCKPILILDM KMLAYDTLDE TLTADEVESR AICRFG
//
