ID A0A2G5VLV1_9PELO Unreviewed; 1009 AA.
AC A0A2G5VLV1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN Name=Cnig_chr_I.g2660 {ECO:0000313|EMBL:PIC52641.1};
GN ORFNames=B9Z55_002660 {ECO:0000313|EMBL:PIC52641.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC52641.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC52641.1}.
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DR EMBL; PDUG01000001; PIC52641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VLV1; -.
DR OrthoDB; 5862337at2759; -.
DR Proteomes; UP000230233; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
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-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR FunFam; 1.10.340.70:FF:000003; Protein CBG25708; 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 Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR055510; DUF7083.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR050951; Retrovirus_Pol_polyprotein.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR PANTHER; PTHR37984:SF5; PROTEIN NYNRIN-LIKE; 1.
DR Pfam; PF13650; Asp_protease_2; 1.
DR Pfam; PF23309; DUF7083; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF00665; rve; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 4: Predicted;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
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:UP000230233};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 291..304
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 311..326
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 625..729
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 266..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..886
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 113736 MW; 6A4C231A16404455 CRC64;
MPPKVSKEVS EDLNVKLVEM MALLQQSMQV QQESMQAQAE RHDKAIEVLT QRLAAGESAE
SSDNSSKLMS ELGGRIAQFV FDLEEEKTFS KWYARYGTAF TVEGASLKDG QKVSLLISKL
SDQVYDQYTK RICPKEFKEV EFKDTVDILK EMFDIKKSLF SHRFACINIT RENETPVEYT
NKVNALCEAA MLKDIDPEGW KVFFWLRGLD PNRDQKQLAY FLKYVEQKLE QQQKVNINDL
CAEWQKFLRQ SSVLLEMSES DKVVKAVQSK NLDNRQNQKP SNREESRGEH CLNCGRAGHK
TPECLKPQRT CFNCQKQGHI AKFCKSARFS ESKNTQNVLM VGGTVSEDVQ VNSIRQFVSA
KVEGKTMDFQ LDTGSDITLI GRKDWERIGK PKLERIKSTV KSASGNELKL LGRTLVSFVL
KGSVGSEYVY VREQGNLLGL DWIERSSEMS YHLERMVNAG SQTKSGSIQS KLNKGKKKFP
KVFKEHPRRC TEEKAVLSVK QTASPVCMAE VQKETKNDTL MKKVIKWVSK GTWPRKVDKR
LKQWFSIKDS LSVTQECLMF GDRVVVPKSL QRAVLKQLHE GHPGMVRMKQ MARAFVYWPR
MAEDVEEAVA QCKACQIHEK TPKKVSLVPW KTPERVWQSV HIGYVGPGNG QYYLVAVDAK
SKWAEVKIVK TINATTTVRK LKEIFSQNGF PETIVSVNGP QFESKEFAMM CQENGILHIR
SPAFHPESNV NTLKMGLKQL KGEGSVGNET LAKFLLHYRS KPSTALSGLS PAEVYLNRRL
RTNMIIPQLN KKSGGSDSCT MKKKFKHQSV NAKAKAYKKC DGIYTKVFEK KVDGRERNGT
NAQRFQGTTN AVTANRSQSV VHRGTRQGAS QGSRGASQGA SQGTSQVVSE SASQGRGQMR
GQRSATVSAP VCQSTSIRRQ AARLDPCWLI PFRHFNIPGS RFILPSLDPT MPALNTAFST
QGRARDEWDT MFKIPNQWNP GDEVGFKMNS KTKRFIGGNG AFDMPALGL
//
