ID A0A0N5BIP6_STREA Unreviewed; 1453 AA.
AC A0A0N5BIP6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
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_0000582600.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000582600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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DR STRING; 174720.A0A0N5BIP6; -.
DR WBParaSite; SPAL_0000582600.1; SPAL_0000582600.1; SPAL_0000582600.
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:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProt.
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; cd00303; retropepsin_like; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 3.30.70.270; -; 2.
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; IPR041373; RT_RNaseH.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR33064; POL PROTEIN; 1.
DR PANTHER; PTHR33064:SF35; RIBONUCLEASE H; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 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 305..319
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 522..776
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1143..1305
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 1364..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1453 AA; 168348 MW; F6A8200899D3BCA6 CRC64;
MPSKEEKLKS VLSAANELGL NISNEVVPGK KLSVINLLLR GYSDKPEELV ENIRLIVADI
KRLLKTTTVL VKKPKAEEKT EKMARYDLSL YKTLPVFEGE SSFVNFYEQF KDAMEFAVDD
EDEEELHPVP EKKQLVLLKG KLGEKVQERL RTIDKDSNLT QITEFLKECY AKYEVSKDKL
RIHINRMSRD DFKNYEEYLK ELFKLCEKYH MKEEKEVRDK LIIADIICKH DAQTQRAVEN
CGIKNPDDLV EFLKLREKRD GKFDNVRNKK GFSSKSFNQS KTEVKGTKFK MHQETPVNKK
DNIICYACQS KGHYASECKT KGDSLEKVSR IETERKVNVV KKDKMKKFDR CPRSVSERCN
NDLIINVKLG KKSKEVERIC MVKGLIDTGS TVTIISEKEA RYLGYDDNVC KDEGTSFVLA
NGAKWKAEGT MMLEICIEDV KIYNQVSIVK EEEICTNGKY NMIIGNDTLM AEGANINYAT
KEITFLGRLV NANCDSNVKA EGLMNRVSTV RREGTPCVFE LKEKMKSAFP EVISDSKVDI
GCCKLSAPKL QVLKQFPKAY RYKHSVKDKE IIKETIEQWL QIGAIKKCYN PSVIINLTVA
VRFDTTEVVM KNDKLEDEVQ IQVKRDTRNL KDEYGRLCKG RYFSKIDLRQ FFLQIPLNEE
DKTLLGIQCP VTNELYSWQR LPFGLNVSSS IAQSIINEVI ENCEFKDENG AVIDENLYGV
MAYIDDILIY TMEDSMQFHK TILFCMLKGL CNYGLKINAG KMELMRTEIC YLNVILSHMK
IRPNPMYIKG LLKMKKPSNV SELRRYLGAV NYCRDFIFGI TELEKPLLTL LQKDQSYLWT
DECERSYNEI QTMLKEVGFL KLPDQSREFI LFVDASKYSE SGLLMQMAKV NEIEKLWIEK
ESKRYPDKYK GIVEDLKENQ SSINEDEERL LPVGYYSKKL GMGESASATL LEVRGLCRTL
DHFKEVTKTS KVIAYTDHKP ILQMLKGGKP ESGRYIRYIN RIFQYDGLRI RYLEGAKNIA
ADYMSRAYCR ATRRKLIRVK EKGNEILVKD GNNPAEEGGG CTESQLNDEI QGKEEMEEKK
LLLFKEIHDQ QGHPYAEASI DMLEKRWPYE NIKREYRNYV NNCKICIERN GIHKTMMKMG
EFTADRPLQM VQMDCLGPLP TSERGYKHLL VWIDVNTRFV GGWPIPDLSH EKIVEAVEES
LIYRYGMVEN VKADNSKYFD KALEVLKERY KIGVERGVPY KHTSQSLVER VIQTLQNVIS
KTGMELLINL EAQWDKVVQR GFYAINNMKH ATLRESPYFL MFGRRPLLSW DLEEMEDMDA
TEREGRISYL VDQQTEFEHQ LCNRYSALLM KAVRSKMNQM IMENKKKEKS AVEKSHYTPE
QTPRDRLNIK VGDPVAVFFP KKNKFEACWK TGYIVVNITN DEGESLKIYC KKKNKTKGRP
LVRSINDVKL LNL
//