ID A0A182K530_9DIPT Unreviewed; 1801 AA.
AC A0A182K530;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR005865-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., 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 christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR005865-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR005865-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 STRING; 43041.A0A182K530; -.
DR EnsemblMetazoa; ACHR005865-RA; ACHR005865-PA; ACHR005865.
DR VEuPathDB; VectorBase:ACHR005865; -.
DR OrthoDB; 3431105at2759; -.
DR Proteomes; UP000075881; 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; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 6.
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; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24260; -; 1.
DR PANTHER; PTHR24260:SF131; CLIP DOMAIN-CONTAINING SERINE PROTEASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 6.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 6.
DR PROSITE; PS50240; TRYPSIN_DOM; 6.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 28..274
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 328..570
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 672..898
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 974..1188
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 1236..1472
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 1588..1801
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT COILED 643..670
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1801 AA; 202633 MW; 1B784572B38C2E39 CRC64;
MVRVCFIVLF SLVKDCHLRH YRHGERGLVG PAFAKPAFLT EFAHIGAIGW TQPDGKITWG
CGGSLIWDNI IITAAHCTAN DELSNVVRFG DLNIYSDEDD TYAQQLKIVN IFRHPKYSFS
ARYYDIALME LEHNITVHET VAPACLWLDQ EVRFKELESA GWGQTGFGET ATPILLKITL
KPMSNDNCTE HYTSNTVRGL QRGLDLHHIC AGDAKMDTCL GDSGGPLNVR LLHNYKVTPF
LVGLTSFGRP CGQSHPGVYT RIAPFRSWIV ETLQKNGLSD LKDSDFNPAD CALRHVAFRQ
GAFSNVVANA SGVFESFDVQ REYITQEFVG EIVQLKWPDT VAPAKNNCMG SIIDHNTVVT
LGDCTSHKGL QPTHVIHGER PDKFYLDTSA RDEKLYNVIE IHLHPNYTNG SYYNNIAVLK
IAGSFNILPA CIWNAPDLPD RLMEIATVGR VDLNVYQYKG QTIHDARFKP LTPRVYAYEN
NNCLLASQYQ ERLDQGLQHQ HLCFGNDPFL VPQVCDLTGG GPLQRSVVRL KRYFKHVYGI
SLFGRDCGYG EPAVAVRLHA HMDWLESVLL PSKSSRQNPN SLDAVQFINP DLEQFDRCDF
YDGSVGLCVP VERCRGVRQR FERNEGMIFC GNGTIVCCLP KDVLDDEQLL NDEDQQLEDC
ENRYESFRRR NFLGSTEQPD PKPHIVEVVW IDKNSKDMFS LCLGYLITTG TVITSAACTE
IKNRKPNFLR LGSIYSRYED FTIHAPIKTI IRHPKYDYAT GANNLALIKL INPIEPTAAL
FPGCLWRNKT HTPLVATMQT LVQSQLRQSD VHPVYDSDCK QHVKAPLQDG EFCMHSDVSE
SQKCPNTAGL IVWRGKGTKN APVEYLIGVY SHSSCEADEP LINSRICEYV PWIIDNLNTS
CKLFPIKPKL PEDEVPMMLA NDKITLDDCH TRNWKDGFEG LVAPAYGNPA LLREFAHIAA
IGWTGADGKV IWGCGGSLIW ENFILTAAHC AANDEDIAPD VARMGDLNIY SDEDDEFPQQ
LRIVKVIRHQ QHRFSAKYYD VALIQLEKNI TVHETVAPAC LWLDDEVRFP KLYAAGWGKT
GFGEDKTNIL LKVDLTPMNN TECARFYTSS ERGLRNGLHA HHLCAGDEKM DTCPGDSGGP
LHVKLLHNAK MTPFLVGVTS FGKPCGQANP GVYARVSSFV EWIIETLQKE GELATVQKFQ
PWSCALRYVH VREYEDDVVV SRSNNYETYD SDKAHLSGGD SNQRVDIFWE QSIVPVRDNC
SGVLIERDAV ATLADCTSHM GATPSRVRLS NGNFINVSET IVHPKYSPAA GPYYNNIAIL
KLPFPVSIIP ACVWYNDIIP DPQFEVIGKG RADLYGYNRD EPVTTFDPRI IAISPRATLS
SNNECRLADQ YWTMLGKGLQ QEHICFQNKP FLVPATCDQQ LGGPIEREMW RFSRYFNYAY
GMNLFGRDCG FGEPAVAVRF NAHRPWIESV LLPEVANQRK STSTGSKDEV IFINPDLHLN
DRCRYSGGME GVCVLHDNCP SVRERITNGE TVILCSNGSV VCCPRDGIKS PPSEIEREFN
DCEQRYAHLR KQRQQRWNGF QPLNLRLPHF AEVGWEEGSE LRFQCIGYLI STRAVVTAAS
CLAKKQFEPS VVRLGSVRSG QFSTDIAIIP ISSVVFHPEF NQSSYENNIA ILKLTSPVQL
TVNTFPGCLW LNTTHTPVES VVYAGSDGFN LIHPMYVRDC NKRFAKQFTD PRITCMNPGV
FGTGEHCYPS GSPIIFRKYE DTNLFTEYLV NIYSHGRCNS SSLRIVHRVA MYIDWFTEVL
K
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