ID A0A401SRI2_CHIPU Unreviewed; 621 AA.
AC A0A401SRI2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=chiPu_0011476 {ECO:0000313|EMBL:GCC33010.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC33010.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC33010.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCC33010.1}.
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DR EMBL; BEZZ01000479; GCC33010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401SRI2; -.
DR STRING; 137246.A0A401SRI2; -.
DR OMA; NGYWYIT; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 66..423
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 486..578
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 621 AA; 71364 MW; 3DAD7824D7AB3CDD CRC64;
MHRVVGTLQK VRLGIHRCWH ITAAPGGLFR SRSGTLSGSR SFTNLPRNFK NLEMEKNKSC
REFIGEEHLN AELKYYKSKS HKYSKLQDWF KRKLEEVCNQ YVSNSYSSVI QMKDFEYFEE
DGCIYRRHQN GDQIPEVVLS LDQLQFLQTA EAQFQQIRVS PNQKYLASSI SSSSDKSICI
VVKLGPKPEV VHVLPRAFNF EWGTDNSLFY TNLEKLQSHQ VLKLLLEDAG ATSEMVYKEN
DPRFFVELAS TKDGRFITIN SNSKNSSEVW LFDRMYPQNN PRIVQERVSG VIYLVEHQRN
QLYILTNYGA TEEYRLMKAP ISSPGMKSWQ TVYEVKERTK LLDMELFKDH CIMILKYSDH
LYLHVFSLDE PSTVKCIQLP SWACVIESED NLKYESNKFS FRLSSPVQPP VRLLYSIEDN
ELHIQENGFK TTNIRDYKVT YLKAPSMDGT LVPITVFHKT PFNKMNKKPL LAHVYGAYGI
DLNVDFKPEQ MVLLEDGWIL AYCHVRGGGE LGLSWHKASR LDKKQVGIYD LEACLHHLHS
TGYSNPRRTA LTANSAGGVL AGSLCNVSPD SVRAVVLRVS ELPNIILDIQ PGGDHFGPSK
WEESIHEVAR HYAFLYEELE L
//
