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Database: UniProt
Entry: A7LM24_9GAMR
LinkDB: A7LM24_9GAMR
Original site: A7LM24_9GAMR 
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
//
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