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Database: UniProt
Entry: A0A016WWK9_9BILA
LinkDB: A0A016WWK9_9BILA
Original site: A0A016WWK9_9BILA 
ID   A0A016WWK9_9BILA        Unreviewed;      2227 AA.
AC   A0A016WWK9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   Name=Acey_s0468.g2007 {ECO:0000313|EMBL:EYC44209.1};
GN   ORFNames=Y032_0468g2007 {ECO:0000313|EMBL:EYC44209.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC44209.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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:EYC44209.1}.
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DR   EMBL; JARK01000068; EYC44209.1; -; Genomic_DNA.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd01647; RT_LTR; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 3.10.20.370; -; 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; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
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; 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; PF17917; RT_RNaseH; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   TRANSMEM        2072..2096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2108..2125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2131..2157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2205..2226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          493..510
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          876..1055
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1433..1591
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          1630..1654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2227 AA;  251839 MW;  8CE27CC9BE989BED CRC64;
     MADKKPDKSP AGAQTEVRQE FALSTLNEEL DIIMQDLKNL PQDLTAAPNV KLGKAQRPMV
     EDAIRERVQQ VCDQLERLTQ STSGYRVFGK ELFALLHGEG IENIEDLRDF INTTGKDGEI
     LEDICADLNT DVTQVRKAVR DLKKQTGRQQ QEVEMETDEG IDTNTCENTI QDYEQRFQLQ
     DRVQAGEAHA RLDQPMTSAN SVPCSMPCTT HSAQEPNSRE AGQNGFSEWL DFLQANTCPT
     PGVFYGKRNE NYREFMRRFR RKYRKVVQSD KDLIEILGDD HLGGRAKSIL LALPAAIVQQ
     GFEAVAEELG KLVAADSTAG RLRALTELRS LRMRPNQSVA EFCVLLENLA RQANPDCTLE
     DRSMEYAQIL LDNLAKWPEH VQLIAALHRV TPDRAYSEVK QLAITMEQSK MMFTTQEQRK
     QFRQGNNWRS RATNYRDTNS GIILPEHSNR VNDCSRRMEP QRRDIAANNG RQNFNQPQPQ
     PFQRVNGRNA ETRRCFKCSE VGHIGRHCPQ QQQANMARNQ RQLQTPHRMD HRVSQMIARG
     HSMGITVREP RSSFEGLIGN QLWVTLEVLG ENLPAMIDSG SMISILPVGV LARAKKSGFD
     VDTLEAIEVE GTLPVYDASN NRMKFLGGVR VDVQLVGGQR SMVSFFVADQ PGNEILLGTN
     ALEGLGVYII VDSKHDKESA CTEFIHDEEG EQIKSVRSLR RVYMPPYTCC LIQAQCETEA
     DEVVMWSSRR GVPTGVFKIS DKGLTLPIVN DGEDPLIIEN GEELGKWSTD KWSEGWENMD
     LAVTGAATEN LSTEDRRALL SEQITSNLAS KVIQQDLAGV LDEFEDVFAV SDRELTRTNL
     VEMNIDTGES SPIRLKARPV PLAVRQKLKD MLEDLQRRNI IERSKSDWAF PIVLVEKKDG
     SLRLCVDYRE LNKRIKQDSY PLPTVEAVLQ SLAGKKFFST LDMCSGYWQI PLSKEAKEKS
     AFTTPEGLFQ FTVTPFGLST SPPVFQRMMD MVLYDLTGSE VFCYIDDIII CTHTRERHLE
     LLREICQRMR DAGLKLKAQK CVLLQTQVSF LGHLIDANGL HMDPRKVEVI KNYPTPTNIK
     QLRTFLGMAS FYRKFCLGFS KQTSCLFALT SAKVKWSWDE EHNRAFEKVK KMISSGPVLS
     QPDIEKARSG ERPFKIFTDA STYGLGAVLS QDGDDGQLHP LFFASKALTK AERRYHVTDL
     EALAVVFAVR RFHMFIYGLP VVVMTDHQPL TALFKRKNVS ARVLRWSLEL QRYNLEVRYV
     KGKANAVADA LSRGVAHLEE EEPLEGLGEA VVNEIRAEES SKWLKELEAD DQFAEIIKLL
     RKNDLDGTVR LKGSNTPVRI SDFILDNGDL KMYQDDGTLV YVVPKEKRRE VFLESHEGTF
     AGHFGPQRLL KKLRKQVFWP GMAKDIMKWS QECQKCFVSN PRQAIVPPLK PISTARPYEL
     IGVDVLELGP TRNGNRYAVT VIDHFSKWAA AYPVADKSAE TIAKVLFQRW VAEGCRYPKA
     IISDKGGEFE NKVMDELTTV MKIDHKFTKG YNPRENGITE RLNGTIVAML RRSTVVPVEW
     DERLPFCMMA YNMTPHRATG ESPYFILHGM DPEFPSSIIP NGGITWYSMD KSMDEYKTAI
     LQSMAEVHDR VKEHNERTRA RMKRDYDAKN EVDPSRHPKV GDRVYVVAPA EKSKCAHPKL
     VSEWMGPFRV LQISENSALV ARMGQNSEPL RVQFDMLRIV PKCISDEQLV TVTSRGKRGR
     KPRVAHVKLI TSPCFSGVKI DNVRMAGHVQ FICKDNCLAK AKLGDLKGVH FPGAFAKEPV
     ITVWNAWKAA SLFIRTDIDM AEKVKHHTNG VISPDAKALV AVLRLAYDRC RDWTAFICST
     AGVNKHVNVD GYDVTPLLDH AVKVVRMEML EGEKQNRPEK TGGTGYASPV YGRILEKDGR
     RGSLETQIVT TFRHVRDVLD GWQHMRNWVI VWPVELNVTG ELVKEIIDRC KKHFEEGGVI
     VTAWTPVMRS NVEMWKNTMG LWLTIDGILA KLARASQFYT TSRTRMENGR LFTEVSNDLL
     SGPITFEEAS AGDCLGNFTV GMYSCIDVTV TFSASAFGII GTLLVPSILL VIASWLHFWV
     HGSWSVPRTI SAALPFFLFA VLFLFRRDVV AAAPGLCCWF IFCLVITFLS LLEYFVVICC
     GIRRSIRYTA NGHPEENPIG AAKETLEVAY DTRCANFRNN NGIDIIARVL FPLIFIIFLV
     VFFLFFI
//
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