ID A0A132AL70_SARSC Unreviewed; 563 AA.
AC A0A132AL70;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Counting factor associated protein D {ECO:0008006|Google:ProtNLM};
GN ORFNames=QR98_0102840 {ECO:0000313|EMBL:KPM11711.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM11711.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM11711.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM11711.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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:KPM11711.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXLN01017759; KPM11711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AL70; -.
DR VEuPathDB; VectorBase:SSCA002272; -.
DR OMA; KAFHHFK; -.
DR OrthoDB; 5472948at2759; -.
DR Proteomes; UP000616769; 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; 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.
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 Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 271..327
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 357..563
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 563 AA; 64798 MW; 60FA6E1D307B90BC CRC64;
MEEMKTIFFS HSIAKLVTKE EQTYGMARII VSVCFLNLLI ISFASAERPV FSDVYDIKGR
ILLPYAELDE PFNAYFDAKA NKSRIDYYGE LQLTIQRPDT NQFFKIAYMV NKHGHTEQVC
FSMDGSLLAP VNIQSVLPDL SSFQFSKRDL CQNFFSRLTA EAQCESWTYS YQFGSRVNKY
LFLLRYNSDG IAIPVYYMMM GFDTLLGSHF DKYEIVYESY STKPINETIF DVADKFECRD
FPGETGKQGL ALMNPIREFV HNVYDHVDEH FDKFTAKHDR NYTDESEEML RRKVFLHNYR
FIMSQNRKNT HYQLAINHLA DRTDEEISKI RGRLIRTNSD FNGGLLFNKL DYDIEQIPDQ
WDWRLIGAVT PVKDQAICGS CWSFGATGTM EGIYFVKTGK LLKLSQQQLV DCSWPEDNNG
CDGGLDFQTY KYIMKSGGLA TEEDYGHYLG VDGICHDSSV KKAVKIKGFY NVTVGDPEAM
KAAIYYHGPV SIGVDASQKT FSFYSHGVYY DPKCDPKNLD HQVLAVGYGV LYGQKYWLVK
NSWSTYWGND GYILINQKHN DCA
//
