ID F4X7S9_ACREC Unreviewed; 766 AA.
AC F4X7S9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 16 {ECO:0000313|EMBL:EGI57485.1};
GN ORFNames=G5I_14463 {ECO:0000313|EMBL:EGI57485.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI57485.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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; GL888891; EGI57485.1; -; Genomic_DNA.
DR AlphaFoldDB; F4X7S9; -.
DR STRING; 103372.F4X7S9; -.
DR MEROPS; M12.A51; -.
DR EnsemblMetazoa; XM_011068806.1; XP_011067108.1; LOC105153768.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; F4X7S9; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04272; ZnMc_salivary_gland_MPs; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034030; ZnMc_salivary_gland_MPs.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF243; SOL NARAE, ISOFORM C; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF13582; Reprolysin_3; 1.
DR SMART; SM00608; ACR; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:EGI57485.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 239..471
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 766 AA; 86136 MW; 46456F950A2B2432 CRC64;
MDLFMSRSIK RTEITNGRDL DYIHEHMTRE EMLSVFYTGH ESVPPYEVVP VLHTMHKRSL
DAKPQIHLKA FGKDISLSLK PTEGLLTANS LPMWIVTRNS SQPDGLHYER VKDIGMNIGD
IYQDAENMAS ILLHRDTNGK VRVDGTIGSE LIIRPLPERV LQEVMSKAST LYEPELLPNI
TSSEDLEHTS HHIVFKKVDR PISDEYSDFS LMEPDHLAKR YRIKRSINSR SRREAPYIIY
PEILCIVDYD GYRLHGGDNV QIKRYFVSFW NGVDLRYKLL KGPKIRISIA GIIISRGRDA
TPYLERNRVG RDAIDSAAAL TDMGKYLFRE RRLPVYDIAV AVTKLDMCRR QYANDVCNRG
TAGFAYVGGA CVVNKRLEKV NSVAIIEDTG GFSGIIVAAH EVGHLLGAVH DGSPPPSYLG
GPGAEKCRWE DGYIMSDLRH TEKGFKWSHC SVSSFHHFLN GDTATCLYNA PHEDEALPRV
LPGKLLSLDA QCRKDRGTSA CFKDDRVCAQ LFCFDAGSGY CVAYRPAAEG SPCGDGQYCL
NGKCVAEHEN IIPDYTQNIP TYVRRDSIFN SAIHTRPIFA HYNNTDYRYP WEATQSIPLS
STPSTPTTTT IRTSTYPYKH VTNLFATTVS KYTRTIINNL YTDQYKTRYN NNNSNNSNSS
TGGGFSTTTR RSNFFNSYYT VSTTPKITYG PKVSPFKYKN TVISFSTTTK GYQNGLRNDG
RGTEAGECTD VGSDCAELID RLRTWLCHLQ SVKSRCCASL KTICAD
//
