ID A0A0V1CEV7_TRIBR Unreviewed; 1394 AA.
AC A0A0V1CEV7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 02-APR-2025, entry version 35.
DE RecName: Full=Integrase catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=T03_15691 {ECO:0000313|EMBL:KRY47805.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY47805.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY47805.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY47805.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRY47805.1}.
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DR EMBL; JYDI01000228; KRY47805.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CEV7; -.
DR OMA; MMPMVRD; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProtKB-ARBA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 1.10.340.70; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR005312; DUF1759.
DR InterPro; IPR040676; DUF5641.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR008042; Retrotrans_Pao.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR47331:SF1; GAG-LIKE PROTEIN; 1.
DR PANTHER; PTHR47331; PHD-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13650; Asp_protease_2; 1.
DR Pfam; PF03564; DUF1759; 1.
DR Pfam; PF18701; DUF5641; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF05380; Peptidase_A17; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 365..380
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1057..1245
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 288..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..307
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 157522 MW; 57757C2D5D8938F9 CRC64;
MSKTVEASDL WIVNTMASAT KVRSKKLAAN KDHLYQLLAE LEELCLESAD VREIKEQIAL
MKKIYHESDA LQGELVLDLD GEERQSAIED WSKTAVRAEN DRLPEMELPQ FSGKVLEFTT
FWAQFEASIH NRSDMDAATK FTYLISSTEG RARSSIEGIL LTAANYTQAV SIFKARFGRP
RMVVREHLTA LWKLPACSDM SMRGIQSLVD ELTKHLRCLV ALNKDPFAGP LPLSESMMPM
VRDKFPLELL KAWDTKLGPD AGEDEDNLQK FLEFAQWQAN LLTKPLEEDG ERSVGRSEHR
RSPRKLSRST WKNADRVTSS AAALAVAALG NCPFCEGKHK GAVCEKFTRA DLPRRMVMAR
SKGVCFKCLE AGHLAKNCRE NRTCAVDGCE QTHHELLHSS TPRESANRTE PSSVQRGMLA
KGNGKGALLQ IVRARAYGPD GTHAVVNCLL DTGAQVSFIR KDIAEALGLT GFYEKVRLET
VGGSLAPQRR LRRVEFSLGA NSVADQPALR RRVEALAIPR ICGKIPHSMS CSLSNKDKDA
ARTEVGQQSK PQRPLTIDVL IGVDHYYDFV TGRMKRNATG SIALETLLGW IICGKPHSSP
SEEARVLLTK VEEPTDAALR KFWEIEAMGI TPEDVVAPED TRMMEQFEKS LSFNGERYQR
QMLSTASSIF DPMGFLAPFM WKQELEELPL INVPRALVPV ALVETKLVEL HAFCDASELA
YGAVICLRVE TSAPLAFWTL SLPRLELMGA LVAARLVHYT QRAHSLPIHS ITCWCDSEVA
LSWIQQLVEP ASWRHCSGKG NLADWLSRGV TVTKLAEGNV SWHGPTWLAR PQQTWPRRQE
NHKRNPLIPP GEERTTKHAT CASMTVQTTE EPLHPGRYGN IEKLFRISAY CRRFAMNCRS
LVSARHGGNL TTWELHKAEE MWVRRTQEEE VQAEIQALVR HGRVAEHSRI SQLDHYLDER
GVLRAGGRLV NSDLPAPMQH PAVLPGNHEL TRGLIRRCHQ RQLHAGVEQT LASLRQHYWV
LKGRSQVKRV TRECLVCRRA TARPTQPRMA TLPRDRVVEA PAFSQVGMDF AGPLYVRVGR
KTTSPRYVCL ITCMVTRAVH LELVPQMTTA RVLQALRRFM ARRGRPKIIQ SDNFRSFKRA
AAEFCQLWQS IDMDRVQREL VGHRIHWKFI PDRSPWMSGY WERLVRSVKE SLRKVLGQAL
LDDCELQTIL CEVEACLNAR PLTFVNDGPG DPQPLSPFQL LTGRQYVDLP AVESQDPEWR
PTDHVNPKWE NRWRYRQQLM ARWWRRWRST YLASLLPRNK RRNNGVGPRI NDLVLILEDS
RPRTRCPLEV VIQLFPGQDG VSRAARIRTS TSESSTTTRP VAKLVMLEPA PIIDGEGNSP
SPGEDVTDVT ARFR
//
