ID F0YA63_AURAN Unreviewed; 910 AA.
AC F0YA63;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AURANDRAFT_64441 {ECO:0000313|EMBL:EGB07876.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB07876.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; GL833129; EGB07876.1; -; Genomic_DNA.
DR RefSeq; XP_009037253.1; XM_009039005.1.
DR AlphaFoldDB; F0YA63; -.
DR EnsemblProtists; EGB07876; EGB07876; AURANDRAFT_64441.
DR GeneID; 20224831; -.
DR KEGG; aaf:AURANDRAFT_64441; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; F0YA63; -.
DR OMA; YLMSAST; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000002729; 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 Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000002729};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..910
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012181016"
FT TRANSMEM 803..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..466
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 487..572
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 153..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 910 AA; 92272 MW; 077B7084A971B811 CRC64;
MALLLGALLA AVATAANLRA PPPSLLDTLK SYTRVDVAHA DGAALGADES FRDAVRLRIS
GAGIDVVLDL ERDSSAFHAN YKELALDGAG GVVVARAGRR GCAYRGAAAG VVGGAPASGR
ATACLGAAFD GVLALGDRVL DVRAAPGGHV AYDAHADRKG EPGTCGVDGR HYAPGAGGHD
HGEGREGDDH GEGREGHDHG EAHDHDDHDD RGEAHDHGDR DEAHDRRGDR ARRLAAGECD
DGATKYLGVV VFNDESRYAT RGVDVEAHSA AVLDVVHSIY GDEAPFGLYD GATVKCRVVP
VVVGQMTWRD GDPAEVDYAA GDACDACGDA CGAGEVSASC LLSSFAAYAD DQRDAIEATL
GASMDVGLLL TSRDLDGSTV GLGYVSGMCH GGFSAAIASV GSGELGYAAA VVAHELGHNF
GMEHDAVGDD GAPAYLMSAS TPQAPSGTNL QFSAASRSSA AAYFEDTYGV GPVDACLDDA
EEPSWDAAIC GDGIVDAGEA CDVGLFIEDA CCRDDCSLEP GCECAAADAC CDGGLFAAAG
TVCRAAVDDA CDDEETCTGA SGDCPTDLYR SAGTACDDVV QEAHFDGGRA VAGQCYAGDC
VSLEDSCVDL EMDDEPAVYP CVELSDCARV LCSNKESGAR QCINRGLAVR DGTPCGDGGA
CFAVGYEAGF ALTVDDGAGD GDGDGGGADD LCVDPSTLAT YHWDTGADGC AAPSCRTEEG
AAAGDERCDD DPPGSPARCS HPPTGTPAPT GTPAPSPGPS PPPTPAPSAS LAPTASPHGA
ADDDDGGPPY LEAWNDLDFP MKMGAILAAV AALALLCLGA GRCCGAGRGR PRARGHPGRR
QFELADVATP ASPAAPIPPL APPSRRQPQI DVRRSTRQPR APPPAAPPST IGATIDAYDR
NARGPDFGPR
//
