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Database: UniProt
Entry: A0A3N4LVM7_9PEZI
LinkDB: A0A3N4LVM7_9PEZI
Original site: A0A3N4LVM7_9PEZI 
ID   A0A3N4LVM7_9PEZI        Unreviewed;      1072 AA.
AC   A0A3N4LVM7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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=L211DRAFT_834636 {ECO:0000313|EMBL:RPB26964.1};
OS   Terfezia boudieri ATCC MYA-4762.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pezizaceae; Terfezia.
OX   NCBI_TaxID=1051890 {ECO:0000313|EMBL:RPB26964.1, ECO:0000313|Proteomes:UP000267821};
RN   [1] {ECO:0000313|EMBL:RPB26964.1, ECO:0000313|Proteomes:UP000267821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4762 {ECO:0000313|EMBL:RPB26964.1,
RC   ECO:0000313|Proteomes:UP000267821};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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DR   EMBL; ML121532; RPB26964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4LVM7; -.
DR   STRING; 1051890.A0A3N4LVM7; -.
DR   InParanoid; A0A3N4LVM7; -.
DR   Proteomes; UP000267821; 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   PRINTS; PR01217; PRICHEXTENSN.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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:UP000267821}.
FT   DOMAIN          390..525
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          664..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..818
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  119413 MW;  AC025B342CB26F4F CRC64;
     MPFPYMHVVS LLNPLSDIAT RKPPPKPAVL KARYSALITS WFDYHRPLFT ATKLEPIALF
     SLLFPELRTD RVYNLREDGL VRVIARCLCL GVTRQQQLSN WRRDADGDLG KMVGRVMRAA
     ENSPPCPGEE VTVEEIEKAL EELASRSIFS SQSKRTPAGA ATKGAHEILT PLFRRMSSSE
     GMWLTRAILK SYLPAVIPEK ATMYAYHFLL PSLWGVQGDL RKCLEVLGGS VFRNFPPAPE
     KKDIRELLKG AGRLVRPEVG VRVGRVEFLK ARSCKNVVAL ADGQRMSMER KYDGEYCQIH
     IDLSKGKDWI KIFSKSGRDS TQDRARIHGT VREALRILKP EERGFKQNCI LEGEMVVYCE
     KEKRILEFYH LRSHISRSGV FIGTSADERP DFQNQHLMLI LFDILLLDSQ PYLSYSYDRR
     ITALSTLIQP RPGYIELASR FEINFSNPIA LDILREQFAH GITQRWEGFV LKPCEGPYLD
     LVGERRSAWI KLKKDYIRGM GDTADFAVVG AGFEAQRGRE RAIGGWGFTT FFVGVLRNKE
     GVVRFGSRPA YHAVFHISYC ISKPDLEHLK NLAYFRAKEY KKGTHLEEYD LEVAPNLPPI
     DVYFTTPLVF EVMGGGFDRP SNCDYYILRW PRVVKIHWDR DWRDAVGFDE LQELAEEAIR
     MPKGRSTAVL EEEEERRWVK RLEQGDQGGK RKQRDEGASG TTPGRQASHA ASPMEDVGGG
     KRRFMRRVVS DGEDSQQQSQ SQDSEMETPP RSQQRESSWS PASSPSQQPR EQSREQQPQR
     LLSSPQPLPQ APRNTQQAGK PLPSPPTSSA PVTAPPAQVP GPSIMTTLSP LPLPTPFLSS
     TARAPLHPLP TPSVINALPP PPAPHPPCPS PLHNATIFLI PSVHAQSRLS PLLALHKPKA
     VYFWTHLPSI YAATQAGLSS SPEASQLASI TPSISPPGNG ATAMTPPIES NVIAAGGDVV
     DGNGTGAGMG KIILLIDFRT PGTSKKFIAK ILEKAGLEPG AAGIDCYDWR VVGHSDWKGE
     RRLDLLDKDK EGENVDASGD GNGNIVAEKG GSRSGSGRRR KVDWDLFYMV SV
//
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