ID A0A177EMH8_9MICR Unreviewed; 1302 AA.
AC A0A177EMH8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, 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 ORFNames=NEIG_01785 {ECO:0000313|EMBL:OAG32906.1}, NEIG_02291
GN {ECO:0000313|EMBL:OAG33108.1};
OS Nematocida sp. ERTm5.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX NCBI_TaxID=1805481 {ECO:0000313|EMBL:OAG33108.1, ECO:0000313|Proteomes:UP000077089};
RN [1] {ECO:0000313|EMBL:OAG33108.1, ECO:0000313|Proteomes:UP000077089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERTm5 {ECO:0000313|EMBL:OAG33108.1,
RC ECO:0000313|Proteomes:UP000077089};
RA Reinke A.W., Balla K.M., Bennett E.J., Troemel E.R.;
RT "Identification of microsporidia host-exposed proteins reveals a repertoire
RT of large paralogous families and rapidly evolving proteins.";
RL Submitted (FEB-2016) 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:OAG33108.1}.
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DR EMBL; LTDK01000102; OAG32906.1; -; Genomic_DNA.
DR EMBL; LTDK01000090; OAG33108.1; -; Genomic_DNA.
DR VEuPathDB; MicrosporidiaDB:NEIG_01785; -.
DR VEuPathDB; MicrosporidiaDB:NEIG_02291; -.
DR OrthoDB; 1364977at2759; -.
DR Proteomes; UP000077089; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 CDD; cd00303; retropepsin_like; 1.
DR CDD; cd09274; RNase_HI_RT_Ty3; 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 InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
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 PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 260..275
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 535..715
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1049..1196
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 228..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 150343 MW; D3B96DE8EE9E14C2 CRC64;
MTNKSSHLRG RGKNQLEADT NTASYSQIEH QEENGGGSNA GKILQGFTEL DFRNGREELE
SQMQVTTYLF CQSWKNINPR YKIAILRNEL TRRSGSIEAT MVRELRSLIA TVSPSSPEEW
TEELWNQIWE RILQIAEQAR PSPVADLPCF KEFLRMTEKG SYLDWCAMMI GQTMAPAIRP
IADIALEFAI RKAIYPANFS EIWRMGGENR DEANRCLWEE CARLDQQRER NRSEMANRKE
RKERRHVSTN HQGHGSSFSC HRCGLAGHRA RDCRRDISSD RRKDFKGKEQ NSRRNWNNPA
PDQSKDGVKV VSTTGPHSGN PEGASSYTTA QIQGVHLPAL CDTGAEINLM SWEDFNLLRG
KGVVLTPRPT QKVISTAGPQ DLICENYVLA DIVVGNSNQI PAKVYIGKDF HGTMILGNPT
LEELRIFLVQ LPQSQDRAGV FYTATRMKPS ENVVRNIEEI LENENPEQIE GISRESLMTK
EDYKSLEAAI ARIQPTQQVE VAEINTPPGK FASEYRFMPN HNLEKAKKLV LDFIKEGFME
ETQASKWLIP IRLARKPNGT WRFCLDYRRL NELVEQDNYP LPDVQSIFDG LYGKRIFSVL
DIANGFFRVP LREIDRQKTT CKIGNRFFRM KVLPMGYKNS PAIFQRIMDK MLKEELETGN
VKVYIDDILI ATESYEEHVE ILRRVLGILK AHGMEVNWEK VRLAYKEIRF LGHTMWMNKI
KPMDDRITEV MKIPVPQTPK QVRSFLGKVN YMGRHIYNLS ELKAPLNEFT SKGRKFVWND
KHQEAFENLK VAVSKIIAAT MPDPRKKFTL ETDASSTGVG AVLRQEDSTI GFFSMRLTPT
QQRYTITERE LYAIVWAMGR CKQYLLGVEF DVVTDHKAIE AFFTKKDQEF GNERIARWMQ
ALESFQFTPK YRRGEDMVIP DGLSRMYEGT SRDLGNPSEV NGKKVLDPSD GNASRVAATL
DVLPRHCNEG SEEMRRDALG RQGWQDAGGA WEEDILSWHE EFGHRKMIRD DLKEKGVLVS
ARELVRILRK CRVCLERDNQ FMKHNEYIDT QDPGELVGID LMEYQRRYIF VAVDYYSRMA
FTFELKNKEA KNIVACLESV YGTFPFQKLL CDNGKEFANA QVKLWLRKHG VEVGYRPPYF
HEGTGRVERL IRTLRDSLNR TKGTVRQKLK RVTRAYNQKV HRAIGTSPEL ASKPENRGMV
TQAIERYKRE FGKTTEPRLA EGTQVLIRKD IRQKDDKHFE RVGQIVGQAG PHSYEVMPEK
GKILVRNRNQ LKVLKIREEE FITRNEIGIP LQEWQDHHEE RY
//
