ID U4UBA4_DENPD Unreviewed; 587 AA.
AC U4UBA4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=D910_05249 {ECO:0000313|EMBL:ERL87861.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL87861.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL87861.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- SIMILARITY: Belongs to the ATG8 family.
CC {ECO:0000256|ARBA:ARBA00007293}.
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DR EMBL; KB632003; ERL87861.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UBA4; -.
DR STRING; 77166.U4UBA4; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR CDD; cd17232; Ubl_ATG8_GABARAP; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF153; GH19262P-RELATED; 1.
DR Pfam; PF02991; ATG8; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lipoprotein {ECO:0000256|PIRSR:PIRSR604241-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742}.
FT DOMAIN 213..474
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 118..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 584
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604241-50"
SQ SEQUENCE 587 AA; 65231 MW; 8AB08A3EA9827C21 CRC64;
MQLPSAVSAT ISTLARVAAG VRGLHHPPGQ SLLSHFLLQN LPLNWFGEVE IKDHNKGFLV
KNPDYRLKAG TPLTIKFFVR FDPNRPPPKL VSLRLNAVVK CPEDGVVTEA PWAAGHLFTN
QPDLSDPSSP DFGNSPSINI RPPGRRPGSS DDEDFYHSDF GALSLPDSGR PQAKPSLLAK
ATCGTVVVNP SKAPMAFKHL QTLMFQKSPR PLITHGQAIG DGDFPWHAAL YHAQGIDLTY
TCGASLISLQ HLLTVAHCVT RKKSTNSINA GNLLVYLGKF YLRIWKTPGI QDKRVDSITV
HPKYNPHTFG NDVAVVKLAE PAELTNYVRP ICLWEGNSKL DLLVDQLGTV VGWGFDESGK
ITEQLTKANM PIVSQETCIY SFPDFYSRFT SNTTFCAGFK NGTSACNGDS GGGMVFPRPG
SDKTNPVWQI RGLVSISVAL QNGFKCDSSH YTVFTDETSG ISLNFGENMR FMYKEEFPFE
KRKVEGEKIR RKYPDRVPVI VERAPQAKIG DVDKKKYLVP SDLTVGQFYF LIRKRIHLRP
EDALFFFVNN AIPPTSATMG SLYQEHHEED FFLYIAYSDE NVYGTKQ
//
