ID A0A1R1YFE9_9FUNG Unreviewed; 1208 AA.
AC A0A1R1YFE9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE SubName: Full=Retrovirus-related Pol polyprotein from transposon {ECO:0000313|EMBL:OMJ25632.1};
GN ORFNames=AYI70_g771 {ECO:0000313|EMBL:OMJ25632.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ25632.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ25632.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ25632.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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:OMJ25632.1}.
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DR EMBL; LSSN01000140; OMJ25632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1YFE9; -.
DR STRING; 133412.A0A1R1YFE9; -.
DR OrthoDB; 5599418at2759; -.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR CDD; cd01647; RT_LTR; 1.
DR FunFam; 3.30.70.270:FF:000020; Transposon Tf2-6 polyprotein-like Protein; 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 InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR005162; Retrotrans_gag_dom.
DR InterPro; IPR050951; Retrovirus_Pol_polyprotein.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR PANTHER; PTHR37984:SF5; PROTEIN NYNRIN-LIKE; 1.
DR Pfam; PF13650; Asp_protease_2; 1.
DR Pfam; PF03732; Retrotrans_gag; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022750};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 638..818
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 314..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..102
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 344..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 135609 MW; 55DB175379C8496E CRC64;
MSNTMQVSAG QLQVAEMSYS NRVAENALLK TQLAAAESQY DQLAAENETQ KDQNEKLASE
NAELKSQRVA EFKFKTEKFM QYQQEKLEIV IIEKQLAQKE ADFYRHQVVI ASRPVHATSA
SSPKMPKIPE FRGSTIGFTR WISWVSDLFE NYPELTDFNR RMMVVESLKD EARSWYDAEP
DSSTTSWEAL KDALLRQYGG TNSIANAFQT INSMTLTSRS DFNIFIQKIR PAIQLVAKTD
STLSIAMLSQ QVDSDIRRFL PEILNESFAS FEQRLKLQFQ ELQIKSASRS NTVYRPADLS
TSMDLDSISA PIRRINNYSR PNSPPGLRPR SPINFRNRNM KPHTPSNSTM SPAQFEQSNS
MQIISKPPKP PDKSFKTVSF SYPPTTDIKY ISASDSPDAL FASRLPFYDL PTGKLTSTPL
TTMTLHLNES ICFKLTATIN GRSVSVLIDT GSQITSMTES ICSILRLPTT SCEPLNLRLG
DNSAGSTSDK LAIADICFGA TKFKTTFRLM TTQPYDIILG ANFIVASKSA YDPTTMTISF
AQGDKIDTFK MMPSGLVATE WAPLVLAASA VDCLPKADPD ISAILRDVAT LFDPTPSIIN
TDFPHQLRLT TDQPAHARMR RYSPEEARVL REHVKELYEA GYARPSTSPY SANPLIVPKA
DGTPRVVINF RPLNKITIRD EYPLPRIDVI QNQLFGCCFY SKLDVLKALY RIPLHSDSIE
ASAFSIPDGH HELLVMPQGM SNSPATFQRN IDRALRECID GGYCAAFADD ILVFSKTREE
HLFHLRSVLK KLSDKGFKLN PKKCIFAVPK VDILGFTVSK DGQEIAEDKI AAVKKFPRPV
NVPTLRRFLG MTSFCRAFID NFTDTAAPLY KLLKNDISYD WNSECETAFQ RLKMAMTSAP
VLAHPDTSMP YIMYTDASNV GIGASLHQCQ SDGTFRPIAY ANRKLLPAEV NYCASDKEAL
AVVYGFNKFH HYVHGSCTEL HTDHRALITA LKHEDPRGRI ARWNSALQAY DFTAKHVKGL
DNTLTDALSH DFEDTDTDIC KMHLPITRSR NIGPKTRRIW GQLDELIEDD SPLNTADSAQ
TDYYDATDPD YNSSIDPIIR TTTAAENDTD QTFQEYNLTE YLPSKTHFTK MQQIDPKINE
ILTTLSNVDS ASTHLAKQAE SYCIKNSMLY NASNSDCSRL YIPSALDNAV NYYHHDTPMM
TRLDIVAL
//
