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Database: UniProt
Entry: A0A0B1TBN1_OESDE
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ID   A0A0B1TBN1_OESDE        Unreviewed;      2345 AA.
AC   A0A0B1TBN1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Integrase core domain protein {ECO:0000313|EMBL:KHJ92750.1};
GN   ORFNames=OESDEN_07357 {ECO:0000313|EMBL:KHJ92750.1};
OS   Oesophagostomum dentatum (Nodular worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX   NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ92750.1, ECO:0000313|Proteomes:UP000053660};
RN   [1] {ECO:0000313|EMBL:KHJ92750.1, ECO:0000313|Proteomes:UP000053660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ92750.1,
RC   ECO:0000313|Proteomes:UP000053660};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Oesophagostomum dentatum.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN551154; KHJ92750.1; -; Genomic_DNA.
DR   Proteomes; UP000053660; Unassembled WGS sequence.
DR   GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 2.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF00665; rve; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053660};
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          190..204
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          976..1147
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          237..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1179..1308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1344..1364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1191..1239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1289..1308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2345 AA;  262214 MW;  C02868AFC2893CDC CRC64;
     MPLPDGESLP VVFSGLTLGQ LAPKNIGTFS GLANQDFESW LRKFEDVVRM VNPPLPEQLK
     TNTLVGFLEG EARDLVEEMQ DADKNSYDRL KPALRFHVKA ANPANFDEAV VKAITYESLL
     ADVANSLSIL PGVQPAVPAV NVISSAQNPT RYEGRNDQQR DNFRNRQVRN YSNNFNRRVW
     ERAPNSNVVC YRCGKSGHIQ TFCRFSLPPA NLRPPRQQFP VRNNFRSGRI NQNSQQQFGY
     GRSVAQQPTV PQQRNDGRNP SRVLALEQTS ATEDPNPEEL SIIQQKDAHI AALIDRNNAL
     ADIAFATRNP KPQNDGEESS SYQSTQINCT KILPNWSATA QPLKIKVFRP NTIRYKSVAN
     VCRIITQTII YSVNFFGARS QKILSQEQTV STGVCRHMAT VYAYHGSSTI ESSIGPLEGC
     QYKDGACTTK SGSAIIWEPE TQESCRYVLV SPMKGVLIDK FAHNDSVIKF YPVTGVYEII
     PSSKVTVIQH STNRPQAIVK PALTLFHNLV ITNISEFVPG QQFTELWSAI EALIDTGSSI
     TLAAQDLCAA LGIFQLDHPQ TSSAMGMAGI LVPMAGSKEV IMQIGNIELH PTIHFTKGPC
     VPNMNSDYEV IIGHDILAQL PPMTIDYKAQ KVCFGAMVLH LGTLSNSNNS GEPPPYPVRV
     KDTTVLQPNA ECFVSCTVPI APPKDLVLVS QCSKIANKDL IVAPALISSN SPVVLVSNPT
     SQPVTLYAGM RLADASEVVQ EGETLAESGD TFSPPAISCV SELTSNDPTY KINLTNSDLT
     ESERKQLVQL LDSFADVFSR HQYDIGSCTA GKVHIYTTND PPSRIRPYRV PMKYREELQK
     HVNMLLKCGV MKESHTPWVH NLVVVRKKDN SLRVCLDMPS EMANKTIIRP NGCLYYHFER
     NGTKDLLLLV PDSLRQLLFD AYHSSALSGG HMGWKKTLAK ILRKYYWPTI YGDIHRWCES
     CLTCQMRRKP KPEFRERLIP VHSEAVFAKV GLDLCGPLRP TERGNKYILN IVCWFTRYVI
     SMPLPDARAN TIAHALFTEC VLKYGTMSEL ISDQASSFTS HFYQEFCNLL HIQQKFATPY
     HSMGNGATER TFSTFQMMLS KFINTKQEDW DLFIPCVTFC YNTTINEATD LMSQSDSAAL
     SILNQGVAST EEPSEKQPDQ PVETDLEVSS GVVEVKMDEE TDEHAAEVAP TATSDSPTPQ
     VPANTPETTT DQVQPVTFPK GPARQTSLNV CGSSSEGEEP QSDRSSRSGS KAHSGKGALE
     KPTTSRGSVR RKITRSFYEQ TRSYSRSPSD SESDMEAEVP VKKAKPSDEV ETALASLVEQ
     ATLIQSVPPQ KVPPSKAILY KPQDEEWKQK EKKSSHREME SFKTHPYRRD LRSKRAPVIS
     PYYNTNLDAA EFEEMPTSGY AGIIEGIFPE PNEGVPKSLR SKITILDAVG PHAIEDFRAR
     HSYDYMFDKN GRKTRLRTMA LADPATDEEK NTYMHGLEFD QGIAPVLYRV KTLFGTGAKL
     EAVHFEVFLP DRYDLAIITI DQYAINVKTE KRGLDITKII VGDLVWVYSL AVTTKFATTE
     HRKPTTIAAA YRLREATVWR VERFALIYRE LRPTLGFVTR IVSQQDGTFE LYMQGHRGLV
     TVNRNRLEDP NSFELIKPNS FIVAPFRPRQ LNYVVFACSV RDQMSMLATL IDIQMPYIPG
     PSPAPFNIRV NSVEHQQLVN SKLTRFDLFS TSPTEVLAFL EPLYSTSCGV IAASVRAATD
     SAAHATAWRS PNINSFPILV TFTIPIQRKT GWAVGSTIRG SYESDFMDGQ IVNVKREKYE
     SYLEVTAKLE TDSGVRFRSC ILNARYDNIL VRTFLYTIEE RANPVLTMLE KCVISDILHP
     NSLGWMSARA LLAGDIQLEG IDNPDQESIT VSVDGTDVTL NQHQVNAVNQ FNKEYPILIV
     DSAYGAGKSL CTAVMAMEAV RKDETILVAA VQNTALDVIG LKIAQLQNKD IRPIRYVNDT
     IGADPDITSP FALQTLMETF HETHGHLLTK YWYAKFRKFS ESRREMREFY FTGTQRHVVT
     REHRRLLLLE QDASEDVKVL VARFLKFYNP NVYLCTISAS LNLTSKKGLW RRLGNKWKRV
     LVDEASMVPE SAIIAMLARF QNAKFTLVGD SKQLPPYVGV NHVPLAVEIS STSILDVAQK
     HGRVPVCMVS TVYRPHEEMM KLNSELFYDG QLICGTPREM RMGLLSRLRM PNSSLPVALV
     DVCGHSIQSV TGSHSNEVEA RAVLVLTTNV TVGTVDSAQG SERSVVILCT TRTHVERTSK
     PTFFSDPRRL NVALSRAKDG MFILGLKSYL QKVETWSAIV EWCEQHGAAT TLDYFDALMR
     PRFHY
//
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