ID A0A151X363_9HYME Unreviewed; 1222 AA.
AC A0A151X363;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=ALC60_06423 {ECO:0000313|EMBL:KYQ54700.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ54700.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ54700.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ54700.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ54700.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KQ982568; KYQ54700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151X363; -.
DR STRING; 64791.A0A151X363; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034036; ZnMP_TLD/BMP1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00059};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001199-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 22..1222
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5007359162"
FT DOMAIN 336..537
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 539..655
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 656..769
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 769..809
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 812..929
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 929..969
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 973..1085
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1086..1202
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 400..422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 402..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 656..683
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 1222 AA; 139510 MW; 876E21A5F2EDD0EB CRC64;
MRTFLVLAIV YLLAKIVDCR AVENDTDKNE RGKRRHKFSV EELFNTKFPH IITGDLDTDI
CKAGGFLGDI ALPNIKYDTE WREQKLNKSY LEELKKYREE ILKEGLQVEE EEILQFKSEH
DANKQMFHEH DEMVVQEKPE PIMINRNQYS TGDKPDDFSF STRNDDIINP AVKDEGLKFR
LESSTQVLKK RHSGRQAHRQ LSRRTWISKS MKARQSNDDM PLEFSTTTTL TLGDNKYVGH
IHTDSVKEIF SSLSETSTQN VSSNRRRRRH HRKRILRRCS HSHCNRRMHG LIIDASDEIV
SIHDRRLRSI EFYDIEHKPK YLTNKSGAYL SRIRRAATAR KERVWDHGVI PYEIDGNFSG
AHKALFKQAM RHWENFTCVK FVERVPREHP NYILFTERPC GCCSFVGKRG NGPQAISIGK
NCDKFGIVVH ELGHVVGFWH EHTRPDRDRH VQIIRDNIMS GQEYNFNKLT EEEVNSLGLP
YDYDSIMHYA KNTFSKGTYL DTILPMEIHG KKRPEIGQRI RLSEGDIAQT NLLYKCHKCG
RTFQENSGSF GSPNHPNNSP SGDGERCEWR ITATHGERIV LNITSLDIFK SDYCRSDYLE
IRDGYWYKSR VLGRYCGSGK MHEPIVSSGS RMLVTYVTSS RQSGHRGFTA SYEAVCGGDV
ELDGVGHLES PNYPEEYQSS KECVWKLSVP QDYQVALKFQ SFEIENHDNC VYDYVEVRDG
HNNDSPLIGV YCGYKIPPDI KSTGNKLLVK FVSDGSVQKA GFSATFMKEF DECVLTDHGC
EHDCINTLGG YECSCKIGFE LHSDGKHCED ACGGFFDDSN GTITSPSFPE TYPGNKNCVW
EIIAPPQYRI TLNFTHFDLE GNNVYQEECE YDSVEVASKL GDDVLRKHGI FCGARLPPLI
TSEGNFMRIT FTSDNSVQKS GFAAVFFTDM DECANNNGGC QHECKNTIGS YQCSCHNGFT
LHENGHDCKE GGCKYEITTP MGTITSPNYP DYYPGRKDCV WHFTTKPGHR IKLVFKVFEM
EPHQECAYDH IAIYDGDSPE SITLGRFCGN KEPHPILATS NQMYMVFKSD ASVQRKGFLA
THSTACGGHL MATDRVKHLY SHAKYGYYQY DHRTDCDWII EAPLGKNVHL SFLSFQLEYE
AECGYDFVEV FSGLDASSPP YGRFCGNSNT TDFISMNEAL LVRFKTDDTI SNKGFVAIFV
AIDRQDSEEN LGGEDNEDQE NI
//
