ID A0A1Y9H2R1_9DIPT Unreviewed; 441 AA.
AC A0A1Y9H2R1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR015767-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR015767-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR015767-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR AlphaFoldDB; A0A1Y9H2R1; -.
DR STRING; 7168.A0A1Y9H2R1; -.
DR EnsemblMetazoa; ADIR015767-RA; ADIR015767-PA; ADIR015767.
DR VEuPathDB; VectorBase:ADIR015767; -.
DR OrthoDB; 3445752at2759; -.
DR Proteomes; UP000075884; 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 Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF154; GH18608P-RELATED; 1.
DR Pfam; PF00089; Trypsin; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}.
FT DOMAIN 1..140
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 192..440
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 143..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 49390 MW; 9C6DD4B86914CAD4 CRC64;
MNDYVQPVCL WPTATDHERV VGRTGHVVGF GLHNQTHMSD DLLEAEVPVV DLINCLESNR
GVFGTTLTSQ MLCAGALNGV GPCNGDSGGG FYLEINNVWY IRAIVSFAPN LYGESVCDPE
QYTIYTDVHK YMEWLSGNHY EHIPPIGQPN QPDTTSPSSA SSPNALLPEF ATENFTYSKC
GQRNPDGVVQ HMVQKKFRAE YGEFPWTVAL FKRAEKLTFC CNGALIGERA VLTTGHCVIL
CGNSTSEIVV RVGEWNISTP MPIPWEEIVV KDIQTHLLYK HMPQAYNIAL LKLELPVQYR
ATVQPVCLPT AAHTLATDKK MIASGWSNAP KKQHSTTHQV QKQFNLLHIE LQTCKDNFQS
FVNQIYATLL SSVMCVTSNS FDHKRISDKE EGSPVVVKVS DEFQLRGLVS WGFKFKEAAV
RCTVLTDVEY FLSWIERMMD E
//
