ID A0A0L0CMU7_LUCCU Unreviewed; 628 AA.
AC A0A0L0CMU7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNC33673.1};
GN ORFNames=FF38_08754 {ECO:0000313|EMBL:KNC33673.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC33673.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC33673.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC33673.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC33673.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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:KNC33673.1}.
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DR EMBL; JRES01000171; KNC33673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0CMU7; -.
DR STRING; 7375.A0A0L0CMU7; -.
DR EnsemblMetazoa; KNC33673; KNC33673; FF38_08754.
DR OMA; YEQCNHQ; -.
DR Proteomes; UP000037069; 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; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24258:SF134; AGAP011908-PA; 1.
DR PANTHER; PTHR24258; SERINE PROTEASE-RELATED; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..628
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005536317"
FT DOMAIN 27..108
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 380..621
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 141..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 70006 MW; 224415821FC4812F CRC64;
MFLSYWKNVA VILCFSLNQV LCLFDQCNHK VEMKAGEKLY LNSPYYPGEY PVGSSCRYVL
KAPQDYELKF TCNIKLNTPQ SATRCVNEVF YFNREGSEVL TGSEYFCGTG KMERKSFLNQ
AVLSYISTPY YKRILPNVVK ESEEEIQRNK TSTTETKKQQ QKRKMTTTTA KPTTTTSRPL
NVNQVTTSSS SIALPANLLT TSFTQAPLTE STTTYFLTSS DEDEEENIKE TMQQEQQKDE
DKNVTNSFAY VVALLSSKID IKAFATKITT ATQTTTKSPV TIATTSSKPT SVLNFYDFLP
VDTWRNSSIA THKISTKRVS KVIIGQDYTS SKHTAFPPTP THTPLFSHTT RNSQGGGSFS
CLVEVLETQC ECGWSSSLKI AGASGVAGIN EFPSMAGVMT IKNQKIFCGA TIIHHRYLLS
AAHCYITPET SRPEYLTAVV GEHDLSTVLD SFYTRQYDLI KIILHEQFHA TSTKVHNDIA
ILKTRYPIEW NRSVGPVCLP FYTLKEGSGT IPYAGQRVET AGWGTTSFGG QQSSVLLKTT
LDVISRNECQ NIVRNLPFGA FCTYTPGRDT CQYDSGGALY ARGERLYAVG IVSYGFACAT
NQPSVNTRIS SHLKWIRNKT PEAKYCTK
//
