ID A0A4C1WEI9_EUMVA Unreviewed; 628 AA.
AC A0A4C1WEI9;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Counting factor associated protein D {ECO:0000313|EMBL:GBP49768.1};
GN Name=cfaD {ECO:0000313|EMBL:GBP49768.1};
GN ORFNames=EVAR_81387_1 {ECO:0000313|EMBL:GBP49768.1};
OS Eumeta variegata (Bagworm moth) (Eumeta japonica).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC Psychidae; Oiketicinae; Eumeta.
OX NCBI_TaxID=151549 {ECO:0000313|EMBL:GBP49768.1, ECO:0000313|Proteomes:UP000299102};
RN [1] {ECO:0000313|EMBL:GBP49768.1, ECO:0000313|Proteomes:UP000299102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31044173; DOI=.1038/s42003-019-0412-8;
RA Kono N., Nakamura H., Ohtoshi R., Tomita M., Numata K., Arakawa K.;
RT "The bagworm genome reveals a unique fibroin gene that provides high
RT tensile strength.";
RL Commun. Biol. 2:148-148(2019).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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:GBP49768.1}.
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DR EMBL; BGZK01000552; GBP49768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4C1WEI9; -.
DR STRING; 151549.A0A4C1WEI9; -.
DR Proteomes; UP000299102; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF975; 26-29KD-PROTEINASE; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000299102};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 200..256
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 288..505
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 628 AA; 70991 MW; E57892D37394769A CRC64;
MNFRYDKGNA KSRIDYYGGM VKTYQLTPKV FPEYGSSIKI APITTEKVLN QMTCLQVNGT
EDHKVEIQSV LPDMTDFKFV GKEDMMDSET SKWRMTQTIG DKINKYTMWV KYRQDLSGQN
VPIPVRYEMK GYNSLLGSHY DHYYLDYMDY NVDPIDPSVF EVDAGLKCTS FPGPGAHYAT
FNPMKEFVHP KRDFHVDDEF TRFKVKHSKQ YFNDIEHSKR LNIFRQNLRY VYSKNRAHLG
YSLAINHLAD RTDDELKALR GRRYSVDDNG GLPFPYGELD IAEMSVKLPP EFDWRLFGAV
TPVKDQSVCG SCWSFGTTGA VEGALFLHNG GHLVRLSQQA LVDCSWGFGN NGCDGGEDFR
AYKWIMQHGL PTEEDYGGYL GQDGYCHIDN VTAVTSIKGW VNVTANNENA LRLAIFKHGP
ISVGIDASHK SFSFYSHGVY FEPKCANKVD ELDHAVLAVG YGALNGQKYW LIKNSWSNLW
GNDGYVLMSS KENNCGVETA PTGVFSKKAY SFLKGRPRIR SYSPLRTSMG GGDYLHSNGP
RARLSLINPT NLGVFGLAKN VVLLTLEQLT PRYCATVRME PRTSYNLETH EGRIEAILRH
LPVLLHPAAS DCLRAGQEER KPTCEGFL
//
