ID B4KSW9_DROMO Unreviewed; 1358 AA.
AC B4KSW9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Tripeptidyl-peptidase 2 {ECO:0000256|ARBA:ARBA00020244};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
DE AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232};
GN Name=Dmoj\GI19561 {ECO:0000313|EMBL:EDW08466.2};
GN ORFNames=Dmoj_GI19561 {ECO:0000313|EMBL:EDW08466.2};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW08466.2, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:EDW08466.2, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CH933808; EDW08466.2; -; Genomic_DNA.
DR RefSeq; XP_002004531.2; XM_002004495.2.
DR MEROPS; S08.090; -.
DR EnsemblMetazoa; FBtr0433085; FBpp0390224; FBgn0142298.
DR GeneID; 6578623; -.
DR KEGG; dmo:Dmoj_GI19561; -.
DR eggNOG; KOG1114; Eukaryota.
DR HOGENOM; CLU_003084_1_0_1; -.
DR InParanoid; B4KSW9; -.
DR OrthoDB; 2441948at2759; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0032991; C:protein-containing complex; IEA:EnsemblMetazoa.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.710; -; 1.
DR Gene3D; 2.60.40.3170; -; 1.
DR Gene3D; 6.10.250.3080; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR022232; TPPII_C_art.
DR InterPro; IPR046939; TPPII_C_sf.
DR InterPro; IPR048384; TPPII_GBD.
DR InterPro; IPR048383; TPPII_Ig-like-1.
DR InterPro; IPR022229; TPPII_Ig-like-2.
DR InterPro; IPR046940; TPPII_Ig-like_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF12583; TPPII_C; 1.
DR Pfam; PF21316; TPPII_GBD; 1.
DR Pfam; PF21223; TPPII_Ig-like-1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 38..513
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 538..654
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 681..772
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 808..992
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 1097..1164
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
FT REGION 1052..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 465
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1358 AA; 149686 MW; 9D9657D5F93FF01C CRC64;
MASDLSGIVE SSFPTAALVP KAETGVLNFL QKYPEYDGRD VTIAIFDSGV DPRATGLETL
CDGKTVKVIE RFDCSGCGDV DMSKKLIPNE NGIVKGLSGR SLKFTPQLLA LNTDKERAVR
VGLKSFNDLV PAKVRDNIVA QAKFKSWDKP HKTATANANR KIVEFESQNP GEASKLPWDK
KIIKENLDYE LEMLNSFEKM YSDVRVSYDC VLMPTENGWL TIIDTTEEGD LTKALHIGEY
SRTHETKNVD DFLSISVNVH DDGNVLEVVG MCSPHGTHVA SIASGNHNSR DIDGVAPNAK
IVSLTIGDGR LGSMETGTAL VRGIMKVMEL CREGRRIDVI NMSYGEHSNW SNSGRIGELM
NEVVNKYGVV WVASAGNHGP ALSTVGTPPD ISQPSLIGVG AYVSPQMMEA EYAMREKLPG
NVYTWTSRDP CIDGGQGVTV CAPGGAITSV PQFTMSKSQL MNGTSMAAPH VAGAVALLIS
GLKQQQIEYS PYSIKRAISV TANKLCYVDP YAQGHGLLNV EKAFEHLVEH RQSKDNMLRF
SVRVGNNNAK GIHLRDGVQR KFIDFNVNIE PVYFNDKEVD PKEKFNFNVR LSLVPSQSWV
QCGAFLDLSY GVRSIVVRID PTGLQPGVHS AVVRAYDTAN VQKGPLFEIP VTVVQPHVLE
DTQSTPIFEP FSNRADKSVE FQPNTIQRDF IQVPDKSTWA VLRMRLTDPN RGNDVGKFFL
HTNQLLPNQS CRKLETMKII GVSSEFDATA TFRVKANKIL ELCIAKYWSN HGQSHLKYSL
EFHGVTALNP NAYVMHAGRG IHKLELDALV SEEVQPSLQL KTAAVVLKPS EAKISPLSAT
RDVIPEGRQI YQNMLVYNLN VNKAADVALY APLFNDLLYE AEFESQMWML FDVNKTLLAT
GDAHSHTFFT KLEKGEYTVR LQVRHEKREL LEKISEANLI AVYKLANMIS LDFYDSYNQG
IVGGRKISST KVRDTSKVIY VAPISQEKLN KANLPSPCAW LSGNLILPKD EGGRRVDLHS
FTYILNPAEK KSSSNGAANG AAASNANPAA AAASTNGVKP KPASTIQEEA SAANSAGGDG
VTSQTDGPAN GCSGTPSSPQ KGKAGADDYA ESLRDFQCSH IAKCDLEKAE KIYNDVIAAH
PKHLPAHLQL IQNIESSELK SLLPFAFVAA QQNRSKEGDN ANADKPKEDL QKQRSALERI
VKLADIVINE TDADALLSYY GIKNDTRSDA AKIKTNMDKQ KNNLIEALVK KGIALAKVYV
LDDNVKDHLA ELNDVYTEII KFIDANDSKA IQFSIWHAFA HNHYGRMYKY VTKMIEDKRV
RELYDEMAAI NFAMGYEHTK PLIDRMAISY FPGSFRLF
//
