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Database: UniProt
Entry: T2CKN0_SIV
LinkDB: T2CKN0_SIV
Original site: T2CKN0_SIV 
ID   T2CKN0_SIV              Unreviewed;       875 AA.
AC   T2CKN0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:AGV33906.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AGV33906.1};
OS   Simian immunodeficiency virus (SIV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11723 {ECO:0000313|EMBL:AGV33906.1};
OH   NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1] {ECO:0000313|EMBL:AGV33906.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RT-SHIV {ECO:0000313|EMBL:AGV33906.1};
RA   Hsu M., Keele B.F., Robbiani M.;
RT   "Exposure to MIV-150 from a high-dose intravaginal ring results in limited
RT   selection of drug resistance mutations in SHIV-RT infected rhesus
RT   macaques.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC         cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC         immunodeficiency virus type 1 and Moloney murine leukemia virus
CC         enzymes prefer to cleave the RNA strand one nucleotide away from the
CC         RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC         from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC         away from the primer terminus.; EC=3.1.26.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00023415};
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000256|RuleBase:RU004064}.
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DR   EMBL; KF598164; AGV33906.1; -; Genomic_RNA.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   CDD; cd05482; HIV_retropepsin_like; 1.
DR   CDD; cd01645; RT_Rtv; 1.
DR   Gene3D; 1.10.10.200; -; 1.
DR   Gene3D; 3.30.70.270; -; 3.
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; 2.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR017856; Integrase-like_N.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR034170; Retropepsin-like_cat_dom.
DR   InterPro; IPR018061; Retropepsins.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR010659; RVT_connect.
DR   InterPro; IPR010661; RVT_thumb.
DR   PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR   PANTHER; PTHR41694:SF3; INTEGRASE-RELATED; 1.
DR   Pfam; PF02022; Integrase_Zn; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF06815; RVT_connect; 1.
DR   Pfam; PF06817; RVT_thumb; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50876; ZF_INTEGRASE; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU004064};
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004064};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004064};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00450}.
FT   DOMAIN          44..113
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          167..357
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          557..680
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   DOMAIN          686..727
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50876"
FT   DOMAIN          736..875
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGV33906.1"
FT   NON_TER         875
FT                   /evidence="ECO:0000313|EMBL:AGV33906.1"
SQ   SEQUENCE   875 AA;  99430 MW;  400E1E741DD53474 CRC64;
     QAAERKAERK QRDALQGGDR GLAAPQFSLW RRPVVTAHIE GQPVEVLLDT GADDSIVTGI
     ELGPHYTPKI VGGIGGFINT KEYKNVEIKV LGKRIKGTIM TGDTPINIFG RNLLTALGMS
     LNFPISPIET VPVKLKSGMD GPKVKQWPLT EEKIKALVEI CTEMEKEGKI SKIGPENPYN
     TPVFAIKKKD STKWRKLLDF RELNKRTQDF WEVQLGIPHP AGLKKKKSVT VLDVGDAYFS
     VPLDEDFRKY TAFTIPSINN ETPGIRYQYN VLPQGWKGSP AIFQSSMTKI LEPFREQNPD
     IVIYQYMDDL YVGSDLEIGQ HRTKVEELRQ HLLRWGFTTP DKKHQKEPPF LWMGYELHPD
     KWTVQPIVLP EKDSWTVNDI QKLVGKLNWA SQIYPGIKVR QLCKLLRGTK ALTEVIPLTE
     EAELELAENR EILKEPVHGV YYDPSKDLIA EIQKQGQGQW TYQIYQEPFK NLKTGKYARR
     RGAHTNDIKQ LTEAVQKITT ESIVVWGKTP KFKLPIQKET WETWWTEYWQ ATWIPEWEFV
     NTPPLVKLWY QLEKEPIVGA ETFYVDGAAN RETKLGKAGY VTDRGKQKVV TLTDTTNQKT
     ELQAIYLALQ DSGLEVNIVT DSQYALGIIQ AQPDQSESEL VNQIIEQLIK KEKVYLAWVP
     AHKGIGGNEQ VDKLVSAGIR RVLFLEKIEP AQEEHDKYHS NVKELVFKFG LPRIVARQIV
     DTCDKCHQKG EAIHGQVNSD LGTWQMDCTH LEGKIIIVAV HVASGFIEAE VIPQETGRQT
     ALFLLKLAGR WPVTHLHTDN GANFASQEVK MVAWWAGIEH TFGVPYNPQS QGVVEAMNHH
     LKNQIDRIRE QANSVETIVL MAVHCMNFKR RGGIG
//
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