ID E2AUB3_CAMFO Unreviewed; 686 AA.
AC E2AUB3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Proclotting enzyme {ECO:0000313|EMBL:EFN62970.1};
GN ORFNames=EAG_02951 {ECO:0000313|EMBL:EFN62970.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN62970.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR EMBL; GL442815; EFN62970.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AUB3; -.
DR InParanoid; E2AUB3; -.
DR Proteomes; UP000000311; 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; 3.30.1640.30; -; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR022700; CLIP.
DR InterPro; IPR038565; CLIP_sf.
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; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF12032; CLIP; 2.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 2.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS51888; CLIP; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 21..74
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 125..326
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 353..406
FT /note="Clip"
FT /evidence="ECO:0000259|PROSITE:PS51888"
FT DOMAIN 451..686
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 686 AA; 75207 MW; 62BF01ECAB970AAA CRC64;
MTFVECPFLK PEYTLRTLFG QCQNPQGRPG ICINIKNCAP LLNLLQTNSQ NPEIANFLRS
SLCGFEGRDP QVCCPTDING GNTGGTENTG NNFEGEQGRG EITNTVYGPL YPPDCGFSNI
SLRRVVGGSP AALGSWPWLT VLGFRNPRNP NVPRWLCGGA LISTRHVLTA AHCVHGRDDL
YKVRIGDLDL NSDSDGATPF EDFIEWKAVH PGYNPTSHTN DVAVLKTTRE VPFSCGPTSS
RLLQTQLPVR PQQECVRAFQ NFKGNVIDDR VLCAGFAQGG KDSCQGDSGG PLMSPNPRDN
KFYYVIGVVS YGFRCAEPGF PGVYTKERFK MWSSVVLISS LCILISPTQS QGQCQNPQGR
PGICINIKKC TLLLNLLQTN SQNPEVAKFL RSSLCGFEGR DPQVCCPTDN GGNTGGTENE
GEQGRGEITN TVYGPLYPPD CGFSDVPLRR VVGGSPASLG SWPWLTVLGF RNPRNPNVPR
WLCGGALIST RHVLTAAHCV RDDLYKVRIG DLDLNSDSDG ATPFEDFIEW KAVHPGYNPT
SHTNDVAVLK TTREVPFSPT LHPICLPVDD FNRNRNVENT YPFIAGWGSV YFRGPTSSRL
LQTQLPVRPQ QECVRAFQNF KGNVIDDRVL CAGFAQGGKD SCQSLLWSLE GDDDEAFLVI
EISHSHYIYG TGTGRNLRSY FTGSVL
//
