ID B3VQ65_PIG Unreviewed; 1313 AA.
AC B3VQ65;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative gag-pol polyprotein {ECO:0000313|EMBL:ACF20333.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ACF20333.1};
RN [1] {ECO:0000313|EMBL:ACF20333.1}
RP NUCLEOTIDE SEQUENCE.
RA Buzdin A., Hejnar J., Matouskova M.;
RT "Porcine endogenous retrovirus PERV-A including open reading frames for
RT gag, pol and env proteins.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms the spherical core of the virion that encapsulates the
CC genomic RNA-nucleocapsid complex. {ECO:0000256|ARBA:ARBA00002845}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the beta type-B retroviral polymerase family.
CC HERV class-II K(HML-2) pol subfamily. {ECO:0000256|ARBA:ARBA00010879}.
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DR EMBL; EU789636; ACF20333.1; -; Genomic_DNA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR CDD; cd06095; RP_RTVL_H_like; 1.
DR CDD; cd03715; RT_ZFREV_like; 1.
DR Gene3D; 3.10.20.370; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 1.10.150.180; Gamma-retroviral matrix domain; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
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; IPR041577; RT_RNaseH_2.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR33166:SF1; CORE SHELL PROTEIN GAG P30 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW DNA integration {ECO:0000256|ARBA:ARBA00023195};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW ERV {ECO:0000256|ARBA:ARBA00022783};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}; Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022932};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW Transferase {ECO:0000256|ARBA:ARBA00022932};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
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:PRU00047}.
FT DOMAIN 493..508
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 547..617
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 725..916
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1129..1303
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 97..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1313 AA; 147695 MW; 2B3FD09BAD5D9E34 CRC64;
MGQTVTTPLS LTLDHWTEVK SRAHNLSVQV KKGPWQTFCV SEWPTFDVGW PSEGTFNSEI
ILAVKAIIFQ TGPGSHPDQE PYILTWQDLA EDPPPWVKPW LNKPRKPGPR ILALGEKNKH
SAKKVKPSPH IYPEIEEPPA WPEPQSVPPP PYPAQGAARG PSAPPGAPAV EGPAAGTRSR
RGATPERTDE IATLPLRTYG PPIPGGQLQP LQYWPFSSAD LYNWKTNHPP FSEDPQRLTG
LVESLMFSHQ PTWDDCQQLL QTLFTTEERE RILLEARKNV PGADGRPTQL QNEIDMGFPL
TRPGWDYNTA EGRESLKIYR QALVAGLRGA SRRPTNLAKV REVMQGPNEP PSVFLERLME
AFRRFTPFDP TSEAQKASMA LAFIGQSALD IRKKLQRLEG LQEAELRDLV KEAKKVYYKR
ETEEEREQRK EREREEREER RNKRQEKNLT KILAAVVEGK SNRERERDFR KIRSGPRQSG
NLGNRTPLDK DQCAYCKEKG HWARDCPKKG NKGLKVLALE EDKDQGRRGS DPLPEPRVTL
KVEGQPVEFL VDTGAKHSVL LQPLGKLKDK KSWVMGATGQ QQYPWTTRRT VDLGVGRVTH
SFLVIPECPA PLLGRDLLTK MGAQISFEQG KPEVSANNKP ITVLTLQLDD EYRLYSPLVK
PDQNIQFWLE QFPQAWAETA GMGLAKQVPP QVIQLKASAA PVSVRQYPLS KEAREEIRPH
VQRLIQQGIL VPVQSPWNTP LLPVKKPGTN DYRPVQDLRE VNKRVQDIHP TVPNPYNLLC
ALPPQRSWYT VLDLKDAFFC LRLHPTSQPL FAFEWRDPGA GRTGQLTWTR LPQGFKNSPT
IFDEALHRDL ANFRIQHPQV TLLQYVDDLL LAGATKQDCL EGTKALLLEL SDLGYRASAK
KAQICRREIT YLGYSLRGGQ RWLTEARKRT VVQIPAPTTA KQVREFLGTA GFCRLWIPGF
ATLAAALYPL TKEKGEFSWA PEHQKAFDAI KKALLSAPAL ALPDVTKPFT LYVDERKGVA
RGVLTQTLRP WRRPVAYLSK KLDPVASGWP ICLKAIAALA ILVKDADKLT LGQNITVIAP
HALENIVRQP PDRWMTNARM THYQSLLLTE RVTFAPPAAL NPATLLPEET DEPVTHDCHQ
LLIEETGVRK DLTDIPLTGE VLTWFTDGSS YVVEDTFSGW VEAYPTKKET STVVAKKILE
EIFPRFGIPK VIGSDNGPAF VAQVSQGLAK ILGIDWKLHC AYRPQSSGQV KRMNRTIKET
LTKLTTETGI NDWIALLPFV LFRVRNTPGQ FGLTPYKLLY GGPPPVGRNC LCT
//
