ID   F4WE17_ACREC            Unreviewed;       763 AA.
AC   F4WE17;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 14 {ECO:0000313|EMBL:EGI67455.1};
GN   ORFNames=G5I_03848 {ECO:0000313|EMBL:EGI67455.1};
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:EGI67455.1}
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   -!- 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; GL888102; EGI67455.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WE17; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   InParanoid; F4WE17; -.
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   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR041645; ADAMTS_CR_2.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   PANTHER; PTHR13723:SF275; STALL, ISOFORM C; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF13574; Reprolysin_2; 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:EGI67455.1};
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   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..763
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003320373"
FT   DOMAIN          186..419
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   REGION          505..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   763 AA;  86392 MW;  E085E7FCEB06F461 CRC64;
     MSSVLMRLIL IILLNQVYAR NIPRDTEVIL LPLWNSKGAS EIPLTFKVFG QLIQLNLRRN
     DNIVSPQFQV WKHNAKSITE ELSQLNAPDP CYYLHKSHEG SAAISFCQEH GLHGLVFLEN
     VTLEITPLRN DLASLPLLID DHYIKEEASL PLGDPHVVKR SSSRSPFIDP DFETKRRLIR
     DTKENLTLEL AVFFDEAAYR LFSPFLDEDD EKIRDMLLAY VNGIQALYHH PSLGVSIDIS
     LIRLDIIQRQ PIDLPHFGGE RGSLLDSFCY YANARNPPED SHFHHWDMGL YVTGLDLYAI
     ENGRKNGATM GLATVGGLCI PYYSCVIAEL GVTDQLGKPY PSAGFTSVYI AAHEIGHNRM
     ICLFKSLGMP HDSSGNACPK DGYIMSPSRG VRGETVWSDC SREVAEMLSQ TKHCLLDQPE
     PRNFSDALAH NHSRYRDLPG KEWTAKRQCE LLLRDKDADV VTLYQACQSL QCKTPHRSGY
     YFAGPALDGT RCASGRECRG GECLPVPEPA PESSDSQKDS WSEWKEGSCS SGCLQRSKGA
     RVRRRFCENR NRLRMARDCK GMYYDVILCK DEKLCKKKRR TIDEFATLKC GLFSERLPKL
     DGTAKGLQAA HEADMPWMAC AIFCRRKDIA AYYAPRVELN DLGLDPYFPD GTWCHAEEGQ
     DYFCRQHHCL PENFRFGKKL PKIYRYEDDN EELGPQNAQN RLGFADRSSV IKYLTSGPDG
     IPLLTSVSRS IASPFDEDEW IDKDYIELPP SISESPYPII NSY
//