ID A0A0F7ZKM3_9HYPO Unreviewed; 1339 AA.
AC A0A0F7ZKM3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Integrase catalytic domain-containing protein {ECO:0000259|PROSITE:PS50994};
GN ORFNames=HIM_09970 {ECO:0000313|EMBL:KJZ70650.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ70650.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ70650.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ70650.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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; KQ030614; KJZ70650.1; -; Genomic_DNA.
DR OrthoDB; 2546268at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR025724; GAG-pre-integrase_dom.
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; PF13976; gag_pre-integrs; 1.
DR Pfam; PF07727; RVT_2; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
PE 4: Predicted;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW Transposition {ECO:0000256|ARBA:ARBA00022578}.
FT DOMAIN 586..750
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 151890 MW; C3358CA3F3F71AC6 CRC64;
MAGEIAPEQR SSPAAESSNS TVGSSAQHQS TVSPPLSCAT PALVRLLQPK KRRLRTPDTW
KHFRLPQGDE ETHQNSQRLW YCQHCQNPSW RTVSTTSAKR HMRKDHGIII EDSERPAKRA
LQQSLEVAFT RAEEKTREQE SRGDQSVLRN TIQLDAFYEA QIQLITRRRL PLNCVSWPEY
QALLCAVNPL AEEILIHSGT TVLTHIERSY EIHRQNVKAY LQASRSQIHF SIDLWSSPHR
KAFLGICAQW VDERYEPREA LLGLPNIQYS HSGETMSRLL LDTIPLDVRE QPLSHETHIY
VATCSMALQQ DPQASQAAIP TVNSFEETLF VRLDHCQREQ PVDSTVRPSF EPEPERGPEF
VPFHVPEREP QVRQLPPTPL LLFQLFVPTF LVETWVKYTN ASPQPGPEGP KKENSREYSW
RETSLGECGT EVTGPQGPSI LRLYNAAFCE NFACNLVSYR KLKKQGIWFD DHPDRPTSLR
GPDHAILALI TEKCGQLVLE DIPDDFSRGS FFTRRNKFNS YTKRRPQKAT AELWHLRLGH
PGPRALEHLV NASQGVRIKG IPTHKCDNCA MAKIKRQIRR TPRETDSFNP GERLAVDFHD
FERDGEGYNS LLLVSDRNTG FCWDYYLTDR TTETVIATLA KCFAYIELHH GFKPRIIECD
NELISQKPGV EDYLRGRSFK IEPSAPYTQD QNGGAERSGG VIKDKARAMR GKLPTDLWVE
ITKAATYLNN RTPKYRIRWK TPYERLYGHK PAQEHLRAYG CKVFAMTSCN LRRLARNRGS
RRRGVHRVVA LVHDTPFFNF DDDTDEASNT QTASQEEEAP KYVEARFELL PTPPPTPPAA
LLAASIQTSQ LPGGALRRSQ RNDVASQLPG GDEADHLIRS QRNDAGPGGQ EATASSDSQG
TTSSRLCSQE ATAFSDSKET QSSFSTLFPT PKSLLYRPQE AARERLASIL KDPKQRIHRS
SLPPAPSRHH QLNDHLLGDQ FKEAEEDHLK SHRDMGSWRE VKTSDAPKRL KILDCMWVYI
YKFDKHGFFK KCKARLVVRG DQQARTSSQD TYAATLAGRS FRTLMAISAR FDLELIQYDA
VNAFVNANLD EEVYMKMPPG HRRQGTLLRL VKALYGLRKS PLLWHRELTA TLRRIGFKSV
PHEPCCLTLK GIIVFFYVDD IVFAYHRKDG AKARDLETQL QTHYKLTGGK DLQWFLGIEI
LRDREQQLIW LSQSSYIDKI GKLASSRPPS TTPMSAIELL PYEGTARDAE IHIYQVKVGS
LLYAAVITRP DIGFAVSRLA RFNTNPGPVH HRAADRVLLY LQSTRALALQ LGGGDDFEVA
SDASFADNSM DRKSSQAGN
//