ID D3JLG8_HASV3 Unreviewed; 928 AA.
AC D3JLG8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative serine protease {ECO:0000313|EMBL:ADC53713.1};
OS Human astrovirus-3 (HAstV-3).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Mamastrovirus; Mamastrovirus 1.
OX NCBI_TaxID=35740 {ECO:0000313|EMBL:ADC53713.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADC53713.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rus-Nsc03-H191 {ECO:0000313|EMBL:ADC53713.1};
RX PubMed=22326537; DOI=10.1016/j.meegid.2012.01.019;
RA Babkin I.V., Tikunov A.Y., Zhirakovskaia E.V., Netesov S.V., Tikunova N.V.;
RT "High evolutionary rate of human astrovirus.";
RL Infect. Genet. Evol. 12:435-442(2012).
CC -!- FUNCTION: Protein covalently attached to the 5' extremity of the
CC genomic and subgenomic RNAs. {ECO:0000256|ARBA:ARBA00029406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC Evidence={ECO:0000256|ARBA:ARBA00024586};
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|ARBA:ARBA00004301};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}.
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DR EMBL; GU223905; ADC53713.1; -; Genomic_RNA.
DR MEROPS; S01.109; -.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR045835; Astro_1A.
DR InterPro; IPR045833; Astro_p19.
DR InterPro; IPR045836; Astro_VPg.
DR InterPro; IPR022068; Mamastrovirus_p20.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF19415; Astro_1A; 1.
DR Pfam; PF19414; Astro_p19; 1.
DR Pfam; PF19416; Astro_VPg; 1.
DR Pfam; PF12285; Astrovir_pp_1; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ADC53713.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 753..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 104561 MW; CAD0BEBD84B3ED68 CRC64;
MAHGEPYYSS KPDKDFNFGS TMARRQMTPT MVTKLPKFIR NSPQAYDWIV RGLIFPTTGK
TYFQRVVVIT GGLEDGTYGS FVFDGREWVE IYPIEHLNLM SSLKLIHKAN ALQERLRLSQ
EEKATLALDV QFLQHENVRL KELIPKPEPR KIQMKWIIVG AVLTFLSLIP GGYAQRQTNN
TIFTDMMAAC KYSTETLTEN LDLRIKLALA NITISDKLDA VRQILNFAFV PRAHWLRTVF
YYIHYYEMWN IFMFVLAIGT VMRSARPGTD LITLATSHLS GFRMAVLPTI PFHTTMTLWV
MNTLMVCYYF DNLLAITMAI LAPILGIIFL CFMEDSNYVS QIRGLIATAV LIAGGHACLT
LTGTTTSLFV VILTCRFIRM ATVFIGTRFE IRDANGKVVA TVPTRIKNVA FDFFQKLKQS
GVRVGVNEFV VIKPGALCVI DTPEGKGTGF FSGNDIVTAA HVVGNNTFVN VCYEGLMYEA
KVRYMPEKDI AFITCPGDLH PTARLKLSKN PDYSCVTVMA YVNEDLVVST AAAMVHGNTL
SYAVRTQDGM SGAPVCDKYG RVLAVHQTNT GYTGGAVIID PADFHPVKAP SQVELLKEEI
ERLKAQLNST VENPATVVTQ QPIVTLEQKS VSDSDVIDLV RTAMEREMKV LRDEINGILA
PFLQKKKGKT KHGRGRVRRN LRKGVKLLTE EEYRELLEKG LDRETFLDLI DRIIGERSGY
PDYDDEDYYD EDDDGWGMVG DDVEFDYTEV INFDQAKPTP APRTTKPQQV DTSQKKPRPE
LEAEVQPLDL SQKKAKQPEH EQQVAKPTKS QKNEPQPYTQ TYGKAPIWES YDFDWDEDDA
KFILPAPHRL TKADEIVLGS KIVKLRTIIE TAIKTQNYSA LPEAVFELDK AAYEAGLEGF
LQRVKSKNKA PKNYKGPQKT RGPKTTTH
//
