ID A0A0E3URB9_9ABAC Unreviewed; 384 AA.
AC A0A0E3URB9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Viral cathepsin {ECO:0000256|ARBA:ARBA00018042};
DE EC=3.4.22.50 {ECO:0000256|ARBA:ARBA00012484};
DE AltName: Full=Cysteine proteinase {ECO:0000256|ARBA:ARBA00031337};
OS Lambdina fiscellaria nucleopolyhedrovirus.
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC Alphabaculovirus lafiscellariae.
OX NCBI_TaxID=1642929 {ECO:0000313|EMBL:AKC91705.1, ECO:0000313|Proteomes:UP000201190};
RN [1] {ECO:0000313|EMBL:AKC91705.1, ECO:0000313|Proteomes:UP000201190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GR15 {ECO:0000313|EMBL:AKC91705.1};
RX PubMed=26021909;
RA Rohrmann G.F., Erlandson M.A., Theilmann D.A.;
RT "Genome Sequence of an Alphabaculovirus Isolated from the Oak Looper,
RT Lambdina fiscellaria, Contains a Putative 2-Kilobase-Pair Transposable
RT Element Encoding a Transposase and a FLYWCH Domain-Containing Protein.";
RL Genome Announc. 3:e00186-e00115(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity, hydrolyzing substrates of
CC both cathepsin L and cathepsin B.; EC=3.4.22.50;
CC Evidence={ECO:0000256|ARBA:ARBA00000656};
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; KP752043; AKC91705.1; -; Genomic_DNA.
DR RefSeq; YP_009133288.1; NC_026922.1.
DR GeneID; 24170909; -.
DR KEGG; vg:24170909; -.
DR OrthoDB; 4752at10239; -.
DR Proteomes; UP000201190; Genome.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF947; CATHEPSIN O; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 82..138
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 168..382
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 384 AA; 43170 MW; 01691C57AC47A646 CRC64;
MSASALIILI AQSALFLSFR AQIAFVGTMR THTHTCNKFK LLIVYIMNKC ALTATVILSV
LAHAPSSTTV SAYNLQKAPD YFDVFVANYN KMYRDDAEKH YRFAIFKQNL EEINNKNKES
DSAVYKINKF SDLSKSEIIA KYTGLNVPSP QTTNFCKTIF LDQPPDKGPL AFDWRHLNKV
TSVKNQKDCG ACWAFATLGS VESQYAIKHH RHIDLSEQQM IDCDHVDMGC NGGLLHTSFE
QMIAMGGVVN EHEYPYAAEN RQCGIDFDAL SPERLAVRVL GCYRYVTVHE EKLKDLLRAV
GPIPIAIDAS GIVDYYRGII NICENYGLNH AVLLVGYGVE NNVPFWTFKN TWGEDWGENG
YFRLRQNVNA CGMLNELASS AVIE
//
