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Database: UniProt
Entry: K7XSK3_9CALI
LinkDB: K7XSK3_9CALI
Original site: K7XSK3_9CALI 
ID   K7XSK3_9CALI            Unreviewed;      1699 AA.
AC   K7XSK3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   08-NOV-2023, entry version 52.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
GN   Name=POL {ECO:0000313|EMBL:AFX81144.1};
OS   Norovirus Hu/Norwalk/10110/2009/VNM.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX   NCBI_TaxID=1261203 {ECO:0000313|EMBL:AFX81144.1, ECO:0000313|Proteomes:UP000131891};
RN   [1] {ECO:0000313|EMBL:AFX81144.1, ECO:0000313|Proteomes:UP000131891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hu/Norwalk/10110/2009/VNM {ECO:0000313|EMBL:AFX81144.1};
RA   Madupu R., Halpin R.A., Ransier A., Fedorova N., Tsitrin T., McLellan M.,
RA   Stockwell T., Amedeo P., Appalla L., Bishop B., Edworthy P., Gupta N.,
RA   Hoover J., Katzel D., Li K., Schobel S., Shrivastava S., Thovarai V.,
RA   Wang S., My P.V., Campbell J., Farrar J., Vinh H., Hoang N.V.,
RA   Wentworth D.E., Baker S.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp is
CC       first released by autocleavage, then all other proteins are cleaved.
CC       May cleave polyadenylate-binding protein thereby inhibiting cellular
CC       translation. {ECO:0000256|PROSITE-ProRule:PRU00870}.
CC   -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC       similarities with helicases, does not seem to display any helicase
CC       activity. {ECO:0000256|ARBA:ARBA00025124}.
CC   -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC       end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC       RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC       to viral RNA thereby promoting viral proteins translation.
CC       {ECO:0000256|ARBA:ARBA00025359}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase with a preference for cleavage when the P1
CC         position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC         Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001491};
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro
CC       is first autocatalytically cleaved, then processes the whole
CC       polyprotein. {ECO:0000256|PROSITE-ProRule:PRU00870}.
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DR   EMBL; KC175350; AFX81144.1; -; Genomic_RNA.
DR   Proteomes; UP000131891; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23192; Caliciviridae_RdRp; 1.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 6.10.20.70; -; 1.
DR   Gene3D; 6.10.250.3230; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR001665; Norovirus_pept_C37.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR013614; Viral_PP_Calicivir_N.
DR   Pfam; PF08405; Calici_PP_N; 1.
DR   Pfam; PF05416; Peptidase_C37; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   PRINTS; PR00917; SRSVCYSPTASE.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51537; NV_3CL_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00870}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00870};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00870}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT   DOMAIN          465..632
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51218"
FT   DOMAIN          1009..1189
FT                   /note="Peptidase C37"
FT                   /evidence="ECO:0000259|PROSITE:PS51537"
FT   DOMAIN          1425..1546
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..76
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1038
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
FT   ACT_SITE        1062
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
FT   ACT_SITE        1147
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
SQ   SEQUENCE   1699 AA;  189108 MW;  9EA7985BA8FDE6FA CRC64;
     MKMASNDASA AAVANSNNDT AKSSSDKMFS NMAVTFKRAL GARPKQPPPR EIPQRPPRPP
     TPELVKKIPP PPPNGEDEAV VSYSAKDGVS GLPELSTVRQ PEETNTAFSV PPLNQRENRD
     AKEPLTGTIL EMWDGEIYHY GLYVERGLVL GVHKPPAAIS LAKVELTPLS LFWRPVYTPQ
     YLISPDTLKK LHGETFPYTA FDNNCYAFCC WVLDLNDSWL SRRMIQRTTG FFRPYQDWNR
     KPLPTMDDSK LKKVANIFLC ALSSLFTRPI KDIIGKLRPL NIINILASCD WTFAGIVESL
     ILLAELFGVF WTPPDVSAMI APLLGDFELQ GPEDLVVELV PVVMGGIGLV LGFTKEKIGK
     MLSSAASTLR ACKDLGAYGL EILKLVMKWF FPKKEEANEL AMVRSIEDAV LDLEAIENNH
     MTTLLKDKDS LATYMRTLDL EEEKARKLST KSASPDIVGT INALLARIAA ARSLVHRAKE
     ELSSRPRPVV LMISGRPGIG KTHLAREVAK RIAASLTGDQ RVGLIPRNGV DHWDAYKGER
     VVLWDDYGMS NPIHDALRLQ ELADTCPLTL NCDRIENKGK VFDSDVIIIT TNLANPAPLD
     YVNFEACSRR IDFLVYAEAP EVEKAKRDFP GQPDMWKNVF SSDFSHIKLA LAPQGGFDKN
     GNTPHGKGVM KTLTTGSLIA RASGLLHERL DEFELQGPAL TTFNFDRNKV LAFRQLAAEN
     KYGLIDTMKV GRQLKDVKTM PELKQALKNI SIKKCQIVYS GCTYTLESDG KGNVKVDRIQ
     STSVQTNNEL AGALHHLRCA RIRYYVKCVQ EALYSIIQIA GAAFVTTRII KRVNIQDLWS
     KPQVENTEEA TNKDGCPKPK DDEEFVISSD DIKTEGKKGK NKTGRGKKHT AFSSKGLSDE
     EYDEYKRIRE ERNGRYSIEE YLQDRDKYYE EVAIARATEE DFCEEEEAKI RQRIFRPTRK
     QRKEERASLG LVTGSEIRKR NPDDFKPKGK LWADDDRSVD YNEKLSFEAP PSIWSRIVNF
     GSGWGFWVSP SLFITSTHVI PQGAKEFFGV PIKQIQVHKS GEFCRLRFPK PIRTDVTGMI
     LEEGAPEGTV VTLLIKRSTG ELMPLAARMG THATMKIQGR TVGGQMGMLL TGSNAKSMDL
     GTTPGDCGCP YIYKRGNDYV VIGVHTAAAR GGNTVICATQ GGEGEATLEG GDSKGTYCGA
     PILGPGSAPK LSTKTKFWRS STAPLPPGTY EPAYLGGKDP RVKGGPSLQQ VMRDQLKPFT
     EPRGKPPKPS VLEAAKKTII NVLEQTIDPP EKWSFAQACA SLDKTTSSGH PHHMRKNDCW
     NGESFTGKLA DQASKANLMF EEGKNMTPVY TGALKDELVK TDKIYGKIKK RLLWGSDLAT
     MIRCARAFGG LMDELKAHCV TLPIRVGMNM NEDGPIIFEK HSRYRYHYDA DYSRWDSTQQ
     RAVLAAALEI MVKFSSEPHL AQVVAEDLLS PSVVDVGDFT ISINEGLPSG VPCTSQWNSI
     AHWLLTLCAL SEVTNLSPDI IQANSLFSFY GDDEIVSTDI KLDPEKLTAK LKEYGLKPTR
     PDKTEGPLVI SEDLDGLTFL RRTVTRDPAG WFGKLEQSSI LRQMYWTRGP NHEDPSESMI
     PHSQRPIQLM SLLGEAALHG PTFYSKISKL VIAELKEGGM DFYVPRQEPM FRWMRFSDLS
     TWEGDRNLAP SFVNEDGVE
//
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