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POLX_TOBAC
ID   POLX_TOBAC              Reviewed;        1328 AA.
AC   P10978;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Retrovirus-related Pol polyprotein from transposon TNT 1-94;
DE   Includes:
DE     RecName: Full=Protease;
DE              EC=3.4.23.-;
DE   Includes:
DE     RecName: Full=Reverse transcriptase;
DE              EC=2.7.7.49;
DE   Includes:
DE     RecName: Full=Endonuclease;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2536143; DOI=10.1038/337376a0;
RA   Grandbastien M.-A., Spielmann A., Caboche M.;
RT   "Tnt1, a mobile retroviral-like transposable element of tobacco isolated by
RT   plant cell genetics.";
RL   Nature 337:376-380(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.49;
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DR   EMBL; X13777; CAA32025.1; -; Genomic_DNA.
DR   PIR; S04273; S04273.
DR   AlphaFoldDB; P10978; -.
DR   MEROPS; A11.002; -.
DR   Proteomes; UP000084051; Unplaced.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR025724; GAG-pre-integrase_dom.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR013103; RVT_2.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF13976; gag_pre-integrs; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF07727; RVT_2; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Nucleotidyltransferase; Protease; Reference proteome;
KW   RNA-directed DNA polymerase; Transferase; Transposable element; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1328
FT                   /note="Retrovirus-related Pol polyprotein from transposon
FT                   TNT 1-94"
FT                   /id="PRO_0000199561"
FT   DOMAIN          473..642
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         230..247
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          189..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..800
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        297
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1328 AA;  151077 MW;  F27E76C504B19B1B CRC64;
     MSGVKYEVAK FNGDNGFSTW QRRMRDLLIQ QGLHKVLDVD SKKPDTMKAE DWADLDERAA
     SAIRLHLSDD VVNNIIDEDT ARGIWTRLES LYMSKTLTNK LYLKKQLYAL HMSEGTNFLS
     HLNVFNGLIT QLANLGVKIE EEDKAILLLN SLPSSYDNLA TTILHGKTTI ELKDVTSALL
     LNEKMRKKPE NQGQALITEG RGRSYQRSSN NYGRSGARGK SKNRSKSRVR NCYNCNQPGH
     FKRDCPNPRK GKGETSGQKN DDNTAAMVQN NDNVVLFINE EEECMHLSGP ESEWVVDTAA
     SHHATPVRDL FCRYVAGDFG TVKMGNTSYS KIAGIGDICI KTNVGCTLVL KDVRHVPDLR
     MNLISGIALD RDGYESYFAN QKWRLTKGSL VIAKGVARGT LYRTNAEICQ GELNAAQDEI
     SVDLWHKRMG HMSEKGLQIL AKKSLISYAK GTTVKPCDYC LFGKQHRVSF QTSSERKLNI
     LDLVYSDVCG PMEIESMGGN KYFVTFIDDA SRKLWVYILK TKDQVFQVFQ KFHALVERET
     GRKLKRLRSD NGGEYTSREF EEYCSSHGIR HEKTVPGTPQ HNGVAERMNR TIVEKVRSML
     RMAKLPKSFW GEAVQTACYL INRSPSVPLA FEIPERVWTN KEVSYSHLKV FGCRAFAHVP
     KEQRTKLDDK SIPCIFIGYG DEEFGYRLWD PVKKKVIRSR DVVFRESEVR TAADMSEKVK
     NGIIPNFVTI PSTSNNPTSA ESTTDEVSEQ GEQPGEVIEQ GEQLDEGVEE VEHPTQGEEQ
     HQPLRRSERP RVESRRYPST EYVLISDDRE PESLKEVLSH PEKNQLMKAM QEEMESLQKN
     GTYKLVELPK GKRPLKCKWV FKLKKDGDCK LVRYKARLVV KGFEQKKGID FDEIFSPVVK
     MTSIRTILSL AASLDLEVEQ LDVKTAFLHG DLEEEIYMEQ PEGFEVAGKK HMVCKLNKSL
     YGLKQAPRQW YMKFDSFMKS QTYLKTYSDP CVYFKRFSEN NFIILLLYVD DMLIVGKDKG
     LIAKLKGDLS KSFDMKDLGP AQQILGMKIV RERTSRKLWL SQEKYIERVL ERFNMKNAKP
     VSTPLAGHLK LSKKMCPTTV EEKGNMAKVP YSSAVGSLMY AMVCTRPDIA HAVGVVSRFL
     ENPGKEHWEA VKWILRYLRG TTGDCLCFGG SDPILKGYTD ADMAGDIDNR KSSTGYLFTF
     SGGAISWQSK LQKCVALSTT EAEYIAATET GKEMIWLKRF LQELGLHQKE YVVYCDSQSA
     IDLSKNSMYH ARTKHIDVRY HWIREMVDDE SLKVLKISTN ENPADMLTKV VPRNKFELCK
     ELVGMHSN
 
 
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