ID A7LM24_9GAMR Unreviewed; 1618 AA.
AC A7LM24;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=Gag-Pol polyprotein {ECO:0000256|ARBA:ARBA00018735};
DE Flags: Fragment;
OS Xenotropic murine leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11837 {ECO:0000313|EMBL:ABS85542.1};
RN [1] {ECO:0000313|EMBL:ABS85542.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZB-9-1 {ECO:0000313|EMBL:ABS85542.1};
RA Kozak C.A., Yan Y.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Constituent of the pre-integration complex (PIC) which
CC tethers the latter to mitotic chromosomes. This allows the integration
CC of the viral genome into the host DNA. {ECO:0000256|ARBA:ARBA00002042}.
CC -!- FUNCTION: Forms the spherical core of the virion that encapsulates the
CC genomic RNA-nucleocapsid complex. {ECO:0000256|ARBA:ARBA00002845}.
CC -!- FUNCTION: Targets Gag and gag-pol polyproteins to the plasma membrane
CC via a multipartite membrane binding signal, that includes its
CC myristoylated N-terminus. Also mediates nuclear localization of the
CC pre-integration complex. {ECO:0000256|ARBA:ARBA00002390}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004455}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004455}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004425}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004425}. Host endosome, host multivesicular
CC body {ECO:0000256|ARBA:ARBA00004560}. Host late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004566}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004566}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004534}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004534}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; EU035300; ABS85542.1; -; Genomic_RNA.
DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase 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:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
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: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; cd09273; RNase_HI_RT_Bel; 1.
DR CDD; cd06095; RP_RTVL_H_like; 1.
DR CDD; cd03715; RT_ZFREV_like; 1.
DR Gene3D; 1.10.340.70; -; 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; 2.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR039464; Gag-pol_Znf-H3C2.
DR InterPro; IPR002079; Gag_p12.
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; IPR002156; RNaseH_domain.
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; PTHR33064; POL PROTEIN; 1.
DR PANTHER; PTHR33064:SF28; REVERSE TRANSCRIPTASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF01141; Gag_p12; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR Pfam; PF00075; RNase_H; 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 Pfam; PF16721; zf-H3C2; 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; 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; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host endosome {ECO:0000256|ARBA:ARBA00023046};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
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 503..518
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 560..630
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 740..931
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1173..1319
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 1443..1601
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 107..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1618
FT /evidence="ECO:0000313|EMBL:ABS85542.1"
SQ SEQUENCE 1618 AA; 181046 MW; B049BC15D2BE70A4 CRC64;
MGQTVTTPLS LTLEHWGDVQ RIATNQSVDV KKRRWVTFCS AEWPTFDVGW PQDGTFNLDI
ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF VSPKLSPSPT APILPSGPST
QPPPRSALYP ALTPSIKPRP SKPQVLSDNG GPLIDLLTED PPPYGDQGPS SSDGDGDREE
ATSTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN
NPSFSEDPGK LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP
TQLPNEVNAA FPLERPDWDY TTPEGRNHLV LYRQLLLAGL QNAGRSPTNL AKVKGITQGP
NESPSAFLER LKEAYRRYTP YDPEDPGQET NVSMSFIWQS APDIGRKLER LEDLKSKTLG
DLVREAEKIF NKRETPEERE ERFRRETEEK EERRRAEDEQ RERERDRRRQ REMSKLLATV
VTGQRQDRQG GERRRPQLDK DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDDQGG
QGQEPPPEPR ITLTVGGQPV TFLVDTGAQH SVLTQNPGPL SDRSAWVQGA TGGKRYRWTT
DRKVHLATGK VTHSFLHVPD CPYPLLGRDL LTKLKAQIHF EGSGAQIVGP MGQPLQVLTL
NIEDEYRLHE TSTEPDVSLG STWLSDFPQA WAETGGMGLA VRQAPLIIPL KATSTPVSIK
QYPMSQEARL GIKPHIQRLL DQGILVPCQS PWNTPLLPVK KPGTNDYRPV QDLREVNKRV
EDIHPTVPNP YNLLSGLPPS HQWYTVLDLK DAFFCLRLHP TSQPLFAFEW RDPGMGISGQ
LTWTRLPQGF KNSPTLFDEA LHRDLADFRI QHPDLILLQY VDDILLAATS ELDCQQGTRA
LLLTLGNLGY RASAKKAQLC QKQVKYLGYL LKEGQRWLTE ARKETVMGQP TPKTPRQLRE
FLGTAGFCRL WIPGFAEMAA PLYPLTKTGT LFNWGPDQQK AYQEIKQALL TAPALGLPDL
TKPFELFVDE KQGYAKGVLT QKLGPWRRPV AYLSKKLDPV AAGWPPCLRM VAAIAVLTKD
AGKLTMGQPL VILAPHAVES LVKQPPDRWL SNARMTHYQA MLLDTDRVQF GPVVALNPAT
LLPIPEKEAP HDCLEILAET HGTRPDLTDQ PIPDADHTWY TDGSSFLQEG QRRAGAAVTT
ETEVIWARAL PAGTSAQRAE LIALTQALKM AEGKKLNVYT DSRYAFATAH VHGEIYRRRG
LLTSEGREIK NKGEILALLK ALFLPKRLSI IHCPGHQKGN SVEARGNRMA DQAAREAAIG
TVLEASTLLI ETSTPYTPTY FNYTETDVKR LQELGATYDK TKGYWVLQGK PVMPDQFVFE
LLDSLHRLTH LSLQKMKALL DREEGPYYML NRDRTLQHVT ESCTACAQVN ASKAKIGARV
RVRGHRPGTH WEIDFTEVKP GLYGYKYLLV FVDTFSGWVE AFPTKRETAK VVTKKLLEEI
FPRFGMPQVL GTDNGPAFIS QVSQSVADLL GIDWKLHCAY RPQSSGQVER MNRTIKETLT
KLTLAAGTRD WVLLLPLALY RARNTPGPHG LTPYEILYGA PPPLVNFHDP EMSKLTNS
//