ID   A0A0N5BR36_STREA        Unreviewed;      1266 AA.
AC   A0A0N5BR36;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Endonuclease {ECO:0000313|WBParaSite:SPAL_0000834000.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000834000.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000834000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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DR   AlphaFoldDB; A0A0N5BR36; -.
DR   STRING; 174720.A0A0N5BR36; -.
DR   WBParaSite; SPAL_0000834000.1; SPAL_0000834000.1; SPAL_0000834000.
DR   Proteomes; UP000046392; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
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:UniProt.
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; cd01647; RT_LTR; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041577; RT_RNaseH_2.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF17919; RT_RNaseH_2; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 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; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
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          209..224
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          444..638
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          989..1150
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
SQ   SEQUENCE   1266 AA;  145761 MW;  7425EDC1F6190A83 CRC64;
     MDPTTGTMNI ELPKYTDMSK DIGLFLRRMT ILLDSQNLDD ARKQAMLKIQ LPDACLDFLE
     GKEFANYNAL VNSLKEKYNG QISKTTAQSR LLSFQFEFKD VEKEILKFAE LVKCASSVTD
     EDELFNWQLD RLTIQLGEKN RIARERLMNC RKDYKSIQEA AADIACSINM HHNSAKNDHK
     KQRSESNSCS YCKKKGHSYD DCRKRLNLCL KCGEKGHKVN ECKKNVTMVT LKEKKVEDKS
     DFFIVKAMIN GYCFNGLIDS GSDSTIVPKC IAKEFVNVDE LPAVEIVTAG KRTLMKRFSG
     SACIELEGFQ TAIDELLISD EKYQQFDGII GLNVLKNLNI VIDLENKELL PKDKSKFKHV
     FHCQVKNTEL SEMERNFKIH LKEELPDLNP KSDFDCGKGI DVAPEQMMIN VKPLGIKYYS
     APTSKDIQAN IDEMLKYNII SRSQVVEVSP FYPIIKFDKE SNAPKKFYDE NGSEFTRMRV
     LLDAREVNNR TVKISYQPNT AFRIIQHLRE FSYASVLDLH QAFFQVKLHP NNYNMFSFTY
     NRQTYSYNRL PQGAVNSPII FQRTMELVLE EFCKNCDDKN MQVEVYQDDI ILLTSLEKDH
     HLKILKMLLC KLNECNVKLS IDKSKFLQTS VNYLSWTFER NIVRPSDVSI LKLTKRKFPE
     KKFQLYQFLQ SLCYFKITIK DWDLMTRDLY ISCKGDKNDK IIWSDANKMK FDELIKALLG
     KPYLHLRKDD LPLIMVVDAS SIAVGGYIYQ QQDSERLILG HFCCILGKCL KARSPTYLEL
     KAISVGVETF KDLVCGKTLY AHSDHRPLES LLNSKSITQP KHMELLCTIK QYVTEIIYIP
     GSQNCIADYI SRCTSANEGG SNKILKEINF IHESCNGKDE LTEMIKNDQI NLETYDVKLN
     DIKYVTVKKD NDLQEERLVI PIVGDKLAWH IIKSVHDKYG HIVGRKLIEV VERKYKIKGL
     KVKVEKFINQ CLTCQKTMEK NLFRPELETI QYPENVWEIV ATDICVVAQH GKIIQFIDTL
     SRYWVPIVIE NLSSEETCNI AIREIFSRYG NPQKIICDQG TNYKGFEFQT LCESMGIELH
     FCTADHKTGN AICERSFKTM RTILMKLKII ADENATFNFK DAVSYASLIY NSTECTTTKQ
     TPFLLMFGRH PNVSDLVNIG YQNSSTIDKL KELRKVAQVT SQCIREHQNE MINMTRESHD
     IKIGDQVLVK SNTSTKIDCP FDGPYQVKDI KGNKLSLVKP GKSRRGRSLI RNVAQCKPYS
     VSNGEE
//