ADMB_ASPFU
ID ADMB_ASPFU Reviewed; 785 AA.
AC Q4WQ08; Q58I95;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein B;
DE Short=ADAM B;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADM-B; ORFNames=AFUA_4G11150;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15936900; DOI=10.1016/j.femsle.2005.05.017;
RA Lavens S.E., Rovira-Graells N., Birch M., Tuckwell D.;
RT "ADAMs are present in fungi: identification of two novel ADAM genes in
RT Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 248:23-30(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Probable zinc protease. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL89676.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY944632; AAX47072.1; -; Genomic_DNA.
DR EMBL; AAHF01000005; EAL89676.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_751714.1; XM_746621.1.
DR AlphaFoldDB; Q4WQ08; -.
DR SMR; Q4WQ08; -.
DR STRING; 330879.Q4WQ08; -.
DR GeneID; 3509039; -.
DR KEGG; afm:AFUA_4G11150; -.
DR VEuPathDB; FungiDB:Afu4g11150; -.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_012383_1_0_1; -.
DR InParanoid; Q4WQ08; -.
DR OrthoDB; 1593931at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0016021; C:integral component of 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:0008237; F:metallopeptidase activity; IDA:AspGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR041645; ADAMTS_CR_2.
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; IPR034028; ZnMc_ADAM_fungal.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..785
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein B"
FT /id="PRO_0000390772"
FT TOPO_DOM 27..703
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 279..507
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 516..605
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 737..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..755
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 398..492
FT /evidence="ECO:0000250"
FT DISULFID 446..464
FT /evidence="ECO:0000250"
FT DISULFID 577..597
FT /evidence="ECO:0000250"
SQ SEQUENCE 785 AA; 85082 MW; 1AAADA820F19104A CRC64;
MRFLKSALPF VASALSLLSV QAAARSQEPS AIQHVSILEH AVINTPSHEV DHLTDFDVTF
ELPDKHQTIK LELEPNHDIL ADDAYVQYLD AEGNVHREEP IQRHEHKVFK GRSLLRRDNG
LWRPVGWARV YVQRDGSKPL FEGVFSIDND NHHVELKSTY LQKKRVEDAS IPDRKDEYMV
VYRDSDMIRQ VRSELKRSLI SSSSCQAEKL GFNSDPQHPI FRSEFQDMDL GMSSYGSMSL
NSLFGLSKRQ SDIGGVSGNA GGVNLAQTIG STSGCPKTKQ VALVGIAADC SFRASFDNDD
AAKQWIINMV NSASDVYEKS FNISIGLRNL TMTDKTCPET APASTQWNMP CDQSNITQRL
NLFSQWRGQQ SDDNAYWTLM SNCPTGSEVG LAWLGQLCNT EVTGDGSNSV SGTNVVVRVS
GGGWQVFAHE SGHTFGAVHD CDSMTCAQNL EASSQCCPYN RGTCDANGKY IMNPSTGADI
TAFSPCTIGN ICSALGRNSV KSSCLSDNRN VVTYTGSQCG NGIVEAGEDC DCGGESSCGD
NPCCDAKTCK FKSGAVCDDA NDSCCSQCQF SPAGTVCRAS LGECDLQETC TGNSSTCPAD
SFKKDGEKCG DTSGLTCASG QCTSRDYQCR TVMGSLIHDN NTYACPQFDS SCELICTSPS
LGSCFSINQN FLDGTPCGSG GYCHNGRCDG SNFGSWVEQH KNLVIGVACG VGGLLVLSIL
WCMINRCRRA RTVVKRPPMR PWPGPMPPPP PQMGQWAGPN RGYQGLRAEP PPPYPGPYQS
ATRYA
