ID E2BV82_HARSA Unreviewed; 1032 AA.
AC E2BV82;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Putative cysteine proteinase CG12163 {ECO:0000313|EMBL:EFN80374.1};
GN ORFNames=EAI_14720 {ECO:0000313|EMBL:EFN80374.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN80374.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN80374.1,
RC ECO:0000313|Proteomes:UP000008237};
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 C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; GL450824; EFN80374.1; -; Genomic_DNA.
DR AlphaFoldDB; E2BV82; -.
DR STRING; 610380.E2BV82; -.
DR InParanoid; E2BV82; -.
DR OMA; PGCPYEL; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 2.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.10.450.10; -; 3.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
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; IPR018073; Prot_inh_cystat_CS.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF959; CATHEPSIN F; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00031; Cystatin; 2.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00043; CY; 2.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54403; Cystatin/monellin; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00287; CYSTATIN; 2.
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:UP000008237};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1032
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003158303"
FT DOMAIN 456..562
FT /note="Cystatin"
FT /evidence="ECO:0000259|SMART:SM00043"
FT DOMAIN 587..693
FT /note="Cystatin"
FT /evidence="ECO:0000259|SMART:SM00043"
FT DOMAIN 727..784
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 813..1030
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT REGION 128..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 115712 MW; B6ABC5929489F85F CRC64;
MGFLVYVYLG YLLLARVQSN PVNIPVNQVP LTLWERAWSA LNEHSPTHHL YAQGNLINAQ
ELVEPPYKIY KFTYNLSPIC GAESPVSGSP CPKEACTIDL KQDENGEIET LNDSIQCMYF
YPADAQNEVS QEQQGDQSTS YQEQEDSQVT ESLAEQVNNN RSVELYHEVQ ETGDENVRPF
IAMRASNPSY CPGCPYELNP QLMGLLPFSK QALKSMDEQS TGDYKHKLIK IVKVTRSVPV
SSNVIQYQLL LLIGESECLK NALEQDECPL QVDVPAKLCL ITFEQQPWQQ TGLKITKNNC
TSPENVSSSN NLSQQPDSES LSQMTVKYDE GQPLKDAYEG LKDILDNYTH APTSPEISSE
SKETSSKRAV TEPTIVKILL NRSQDDEKNE GFFDKTKEFG EFLEDFDVPV KVEHVTPESM
KEGEFKRKKV RAENFMVEKA IDRNVVNRQK RSPQVQLVGA PSPISVNDSD VQMYVEKALR
MVSHDSDEPN EPSIVEIVKA TVQVVAGSLH KITVKMGTSH CAKGTKNNCQ LQAGSEVKDC
QISVLSQSWL DKGEPSITVE CPPPPEMVEK ATDRNVVNRQ KRSPQVQLLG APSPISVNDS
GVQMYVEKAL RKVSHESNEP NEPIVVEIVK ATVQTVAGRL HKITVRMGTS NCPKGPTHNW
QLQAGSEMKD CQISVLSQPW LDSGEPSITV ECPPPEKSHR KERSLRGTNY NEKMLRIAED
MRSERLFENF VNTYNRTYAT EEERNLRLSI FRENLGIIRL LRKNEQGTGQ YGVNQFADVS
TEEFHAFYLG LRPDLRTENN IPLRQAEIPD IELPNSFDWR QKGAVTPVKN QGMCGSCWAF
SVTGNVEGQY AIKHNKLLSL SEQELVDCDD LDEGCNGGLP DNAYRAIEKL GGLELESDYP
YEAENERCHF KKNMAKVQVG SAVNITSNET QIAQWLVANG PISIGINANA MQFYMGGVSH
PFKFLCNPKN LDHGVLIVGY GTSNYPLFHK KLPYWIVKNS WGDRWGEQGY YRVYRGDGTC
GLNTMASSAV VV
//
