ID A0A163JDA0_ABSGL Unreviewed; 1521 AA.
AC A0A163JDA0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN Name=ABSGL_04063.1 scaffold 4834 {ECO:0000313|EMBL:SAL98522.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL98522.1};
RN [1] {ECO:0000313|EMBL:SAL98522.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98522.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT552138; SAL98522.1; -; Genomic_DNA.
DR STRING; 4829.A0A163JDA0; -.
DR InParanoid; A0A163JDA0; -.
DR OMA; NGATAMI; -.
DR OrthoDB; 1707090at2759; -.
DR Proteomes; UP000078561; 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:0015074; P:DNA integration; IEA:InterPro.
DR CDD; cd00024; CD_CSD; 1.
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; 2.40.50.40; -; 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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
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 PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR Pfam; PF00385; Chromo; 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 SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT DOMAIN 1167..1325
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1453..1511
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 267..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1521 AA; 173761 MW; FDB177C87E8307D5 CRC64;
MPSVDIIETT AQATRLAQEK LQESVQELTQ LMIANAKGKV PMKAFKDNEA KQNLWKTTLL
NLNGLGPMLK KEIKVPTNLP VLQLVSDKEI NDKHPAFEMI DNFLEMFTII MHQHHLDLNQ
HWETCIISSL QHSTTKCSWF KENLMAKGLS WQQAQETIKH QFGGAQTQSY YLEKLNSMES
DRHENPVHFV ERFSTCLHRA QVEDSVAYGS MLIRGLTKHH RSLVKQIKAT HAATDPTYNL
SINVAYVARV VPLLYIEDFD NDRNNRATRR ATRFNNGSDT NRHDYPNSNY SNTNYANNRG
RGRNNYRGRA RHYQNGRGYV SNNRNNSSNS NSNTTPTFEE CKAKGICFHC RSKWTVGHKC
QQYMEKFGGK TDYTPFKQRL ARLEHQIKTQ EAVLAMRDID LNKDGNMDTE EECKRKKSRM
AKIENELNPD SFVVPIQIES HRTFALLDSG ANFSSLDRTF ILNKQISFSS INGNIQLADN
HYSTKRIGKT NALNVTYNSK AHKISFEVMD LPKNESYTCV IGTDYFQKLG IFLVGLATSY
DDTAPLQFDD ERKDIPKPDE SPAGTALEQK LFYQAIKNSV TNNQKVDKRS FCTVPESIVT
LDTPAGKTCY KRQYPIANNL MPLIDEAVTK WLNEGTIVRA GVNTEWNSPL TLAPKKDADG
NKSRKRPCLD PRHINLLLPN DRFPLPLIKD IFETLKGATV FTTLDLQNAF HRFQIAPADQ
HKTTFTHRGT QYMFQGCPFG LKPLSSKFQR VTNMILEDMP FATSFIDDIV VYSANINDHA
KHVQQVINKL TSVNLILNPD KCHFAQQSVY LLGFCVSVKG LSLDTRKVTN VQKWPTPKTG
NDIERFLGVI NYFRDHIPKV STLTAPLDRL RKEKKLGNKW TPVCDTVFIK LKYVLTCTTV
LKHPNLQLPF NVATDASNTG IGAVLFQVVN KKVQHIGFFA RSLSKSERNY STTKRELLAI
IFALNKFHKY LWGNHFTLYT DHRALIYIHT QRIANPMMIQ WLDTILQYNF TVAHVPGMSN
ILPDALSRLF PIENKLVGDI DTLPARKIAY KEAKMEKLVN QHNDDLIIPD KDDRDKLIQH
YHRSAHIQQP EEEQLRTVNG DEERKTIMEK QHALGHNGAT AMIKAIQADG MTWPNLKADA
VQHVSKCNAC MQYNVARKGY NPLSSITSRL PGDHWAVDLA GPLEETHKGN VYILVMIDIC
TKFVIIKAIP DKTSLTIAES LIDVFSTFGY PKIIQSDNGT EFVNKIIKKI TEVACIDHRL
ISAYHPRANG AAERTVQTVK GAIQKHMEGQ SKDWDHYIPT AQLAINARIV RLTNSAPFSL
MFARKLNAFV DHTKTTITED NKAVMDRIED MKNIVMPAII QRTTELRELT QNKFNSKHKM
IEFKIGTLVN IKKPTYTKQL EPKYKGPFKV VRKNKGGAYT LQHLDGELLD RNYPPSALKS
VSDDLITNEE DRWEVDTIVD HRGIPGKYEY LVRWKGYTKE SDTWEPPSMF DDIQTIKNYW
SKRQGALMES SQLHKKRKTN L
//
