ID Q7PVV8_ANOGA Unreviewed; 732 AA.
AC Q7PVV8;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 4.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
DE Flags: Fragment;
GN ORFNames=AgaP_AGAP009172 {ECO:0000313|EMBL:EAA14977.4};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA14977.4};
RN [1] {ECO:0000313|EMBL:EAA14977.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA14977.4};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA14977.4}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA14977.4};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA14977.4}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA14977.4};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA14977.4}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA14977.4};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA14977.4}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA14977.4};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAA14977.4}.
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DR EMBL; AAAB01008984; EAA14977.4; -; Genomic_DNA.
DR RefSeq; XP_319935.4; XM_319935.4.
DR AlphaFoldDB; Q7PVV8; -.
DR STRING; 7165.Q7PVV8; -.
DR ESTHER; anoga-q7pvv8; S9N_PPCE_Peptidase_S9.
DR MEROPS; S09.A73; -.
DR PaxDb; 7165-AGAP009172-PA; -.
DR GeneID; 1280128; -.
DR KEGG; aga:AgaP_AGAP009172; -.
DR VEuPathDB; VectorBase:AGAP009172; -.
DR eggNOG; KOG2237; Eukaryota.
DR HOGENOM; CLU_011290_1_1_1; -.
DR InParanoid; Q7PVV8; -.
DR PhylomeDB; Q7PVV8; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070012; F:oligopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 25..431
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 505..727
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EAA14977.4"
SQ SEQUENCE 732 AA; 83318 MW; 365E2A008C6AC1DB CRC64;
TQFGRLAMPE AAAAAAAEAR QFVYPAARRD ESVVEEFHGV KIADPYRWLE DPDAEETQAY
VEKQNEISKP FLDTCPEWKK LNEKLRKRWN YPKYSCPFKH GNKYFFFMNT GLQNQDVLYV
QDKLDGEPKV FLDPNTLSAD GTIALVGSRF SDDGKLYAYG LSQSGSDWTK LKIRNVETGE
DFPETIEHTK FVTASWTKDN KGFFYARYPV VAGKADGSET AANENQKLYY HRVGESQDKD
VLIAEFPEEP SWRLMPEVSD CGKYLMLFIM KGCKDMLLYF SNLEKAGTLE SKLDFVKVVT
EFDSDYDYVT NEDNIFSFRT NKVAPNYRIV NIDFEQPEME HWKTLVPEHP KNVLDWTTCV
NKDRIVLGYI DDVKSLLVVH SLADGSFVSK FPLEIGTVAG FSGKKKYSEI FYHFVSFLTP
GIIYHYDFEG KTEAAGGGAM EPTVFREVKI EDFDNSRYAV EQIFYHSKDG EKVPMFIVQR
KQEKKEHKPC LLYGYGGFNI CVQPSFSITG LVFIDSFDGI LAYPNIRGGG EYGERWHNAG
RLLKKQNVFD DFQHAAQYLV EHGYTTHDKI AIQGGSNGGL LVGACINQRP DLFGAAIAQV
GVMDMLRFHK FTIGRAWVSD YGDMNEKEHF ENLLRYSPLH NVRTPTSEKD QYPATLVLTA
DHDDRVSPLH SLKFVAALHD AIKDSEHQKN PLLLRVYSKA GHGMGKPTAK KIEEATDILT
FMYKTLGLKL SF
//