ID A0A165H4P9_EXIGL Unreviewed; 515 AA.
AC A0A165H4P9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Integrase catalytic domain-containing protein {ECO:0000259|PROSITE:PS50994};
DE Flags: Fragment;
GN ORFNames=EXIGLDRAFT_588446 {ECO:0000313|EMBL:KZV91451.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV91451.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV91451.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV91451.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49;
CC Evidence={ECO:0000256|ARBA:ARBA00024557};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632};
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DR EMBL; KV426027; KZV91451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165H4P9; -.
DR STRING; 1314781.A0A165H4P9; -.
DR InParanoid; A0A165H4P9; -.
DR OrthoDB; 1664232at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR013103; RVT_2.
DR PANTHER; PTHR42648; TRANSPOSASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR42648:SF11; TRANSPOSON TY4-P GAG-POL POLYPROTEIN; 1.
DR Pfam; PF07727; RVT_2; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW Transposition {ECO:0000256|ARBA:ARBA00022578}.
FT DOMAIN 1..137
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 225..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZV91451.1"
FT NON_TER 515
FT /evidence="ECO:0000313|EMBL:KZV91451.1"
SQ SEQUENCE 515 AA; 57365 MW; 5BFA63519B07F539 CRC64;
LDDHSSFASG YWLRKKSDTH ASIVEHTDWA EKRAGKPMLV SHNDEGGEFI GKRTLEFFKS
RGIDVRHTET ASPWQNGRVE RLNRAMAEGV TTMLNHAHLP RSWWKLAGAA WLWVRNRTIS
SSLPEGKTPL ELFCREKPDV SRFRVFGCYA HALVPPERRP AFTTHGRDCI FVGYSKEKVG
CWIFYDINTR KIFESSNAVF DENSFPGTAA PDPRSIFDGD LTELEGLEDP LPEGRSRDQT
PPPLAHDTPP PRTAQLEEDA TPRPPPPPQA GTPPQPEDRT PRPRAPIRSA PTEPDTPIPP
RRTSTRPGRP APGSLAEPDL RRSTLYPVAL EPGPSSLREY REPTPQIQLS DTEDEGVMPN
SSASESSDGV IPSDDGEDSL LSDAHVVEPR TFKEAMSRPP DEAMKWLAAA HEELDNLVRK
GTFVMVKLPP GRKAIGSQWV FKLKRNSEGV IERYKARLVA RGDSQRPGVD FTETFAPTVR
WGTLRTIFAL VALEGYVCVS ADVTAAYLNG DLEEE
//
