ID A0A0V1CM33_TRIBR Unreviewed; 1346 AA.
AC A0A0V1CM33;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Retrovirus-related Pol polyprotein from transposon 17.6 {ECO:0000313|EMBL:KRY50278.1};
GN Name=pol {ECO:0000313|EMBL:KRY50278.1};
GN ORFNames=T03_17994 {ECO:0000313|EMBL:KRY50278.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50278.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY50278.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY50278.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRY50278.1}.
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DR EMBL; JYDI01000154; KRY50278.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CM33; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 3.10.20.370; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR005162; Retrotrans_gag_dom.
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; PF03732; Retrotrans_gag; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 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; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 175..190
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 402..581
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 929..1090
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 924..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1346 AA; 153064 MW; 7AC505FE6454DC99 CRC64;
MRKKNKATIS RPVLEDQEGV RARMLPTKRE LGKRGGRAEF RKRLLDAYGP EESTGQLIER
FHTLHQREGQ TIEQYAQEVA EVGRRAGVTE RDLVARFAGG ITSKEAYLAI RLREPATLTE
ARRLRRQRRT GNPKPEKTEA TQLMEDLIRE VRMISLKLEK QESTAARPAR RATECFRCGE
QGHFLRDCPQ RRVAARVTPA MTSTRPMERT MATINPQTGN VLAVPGMIEN LEISLLVDSG
AVVSVISKQV WDKATSCRKL REVQYNWETD GRWRPSAGGS FSCTWGDGRG RSRLWWWRSW
WSRASWAQIS WTPWCGACTS GLAICIGCMG TGVPQKGTGP VTTGKPAKAA GSGSTHLLTQ
QRRTSLVTHR IETGEARPIK QPPRRLPVAQ RSVMERLVGQ MLESGVIEPA SGPWSSPVVV
VRKKDGSPRF CVDYRRLNAV TRVDAQPLPR IDDTLDALAG SQWFSTLDLA SGYWQVEVAE
PDREKTAFST PMGLFQFRVM PFGLCNAPAT FQRLMENALR GLTIKGCLVY LDYIIVYGRT
EEEHMERLAK VLHRLQSVGL KIRPDKCQLM RRSVRYLGHV VTQHGIGTDP EKTAAVQEWP
RPRCVKEVQQ FMGLASHYRR FVRNFSSIAG PLHKLTRKGQ RWSWGPEQEV ALTKLKSVLS
SPPILSHPQF DQPFLLDVDV SEDALGAVFS QTNHQGLPLV VAYASRSLSQ PERKYCATRR
EMLALAWATR HFRPYLYGRM FTARTDHNAL RWLRNLREPE GQVARWLERL AEYEFEVVHR
PGQQHRNADA LSRRVCKQCG AMNPTADAEV AAMTLGPTGR IQEWQYAEPE LRKIQEWVDK
RDWPQEPPAG SHMFRSLWSQ RDRLTLRDGI LCRAWEAPDR EEEKKSCEPS TTIRRAVTWE
WRRHWAGTPT VLLATAAGRR RGLVSGVPDL RRPGGTDQKA AGTDADPPET RRGNRYILVV
CDYFSKWPEV FPLPDAEADT VATALVNGIF CRYAAPETLH SDQGRNFEAG VIAEVCRLLG
IAKTRTTAYH PQSDGLVERM NRTLIDMLAK VSIDQPEDWD VHLDRVLLAY RSSVHHITGA
TPCRIIFGRE LRLPVDVVYG LPQGMQAETT GVYVQRLRQE LEQVFDTVRA KAKLEQRRQK
LWRDKKARGH AYEPGDQVWF QVPVKTKLGA HWEGPYLVQK KLDWNTYRLR KIRAGKEPVV
VHFYRLKAYH DRQQTAETWE VGRKRRTMRR PAWMRDFIYT RDDQEGVRWN VTIISSGEAI
VGFLRYTVLV VVVIANKYCI LVLARMLPTK RELGKRGGRA GSNRTDDTDA EMNPQVNTGA
SSFDDDCGSN PVEATNEPAR QSGSLH
//
