ID A0A267DUG8_9PLAT Unreviewed; 892 AA.
AC A0A267DUG8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BOX15_Mlig004074g3 {ECO:0000313|EMBL:PAA52928.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA52928.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA52928.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA52928.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA52928.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 -!- 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:PAA52928.1}.
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DR EMBL; NIVC01003162; PAA52928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267DUG8; -.
DR STRING; 282301.A0A267DUG8; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..892
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012854213"
FT TRANSMEM 793..817
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..397
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 408..497
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 468..488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 892 AA; 94388 MW; C312AD93DAAE0856 CRC64;
MKALVLLLLV LQQLQSALCV EVDHGSAQSG EPPVLYFHQL NHSACDGEML AVVNIEGQEG
RRVSLKLTES SREFLAADAP ADSQFVLDGL GSRPCFYQGQ LVEGGTPVVA KLSRDGLFSA
TFDYNGTVYE VRPQSKRLAV FLGNRLPKLG GTERRCPLAA KSAVTAAAER PIRSRQSALL
MDTRSGVAQP AQKFIQLVLV SDEAYFIGMG RDSARTQDRL WEIGNYINSL YKQLGVNVVI
VRAIVLTTDP FTLANKTSAV SSSEMLDKFM AYRMQNLSHI QHSAAHLVSG LRMTGSDVGL
AHLGKLCQFA YGGGVNSDLD IAGSAINVAV TVAHELGHNL GMNHDEDDVP CSCPDPQGCI
MKAVGGEINP LRFSTCSVNR YLEFTVDAGL GYCMSRPPEP TVKLSTDGPK CGNRILEAGE
DCDCGLAAWC NNSCCNPTTC KFNPGASCAS GQCCNITTCS LISRGTECRA ARGVCDLPEF
CNGSSEWCPE FDDYVLDGTA CAVNPAAPSE ALAYCYSGAC TTRDSRCHAM FNGTNYRSAP
DSFSNLTADP SNTENGYCNY RATAYNPVGY AHESCSFENR RCGTLYCIGI MSEPFPMPRW
KSMAPADARL VMVTSGGGGL DAAFARLDLR PTGYRDPGMT PDGAECGAGM MCVNSRCTSL
ASIRSNITGS VGLPNCNGRG NWTQSLQCFC SSGFRPPDCL LPGAGGSVTN QPAFADTSSS
PVTTLATATA TTTATTAAAA TAVSDVSGQT TISNPVDFST SLSVRINSTL QSSSTTAATM
MSSPAAGGTD SGLYIGIGVA AAIVFLLLVV GVSYLLWRRC RAEGRTGKDQ TDSPADSGGG
LFVAAAGPPA HLSNFYDSIR DLGKRRDSSL SRRKYWPAPP PEVQADVNGL AV
//
