ID N1R9A0_FUSC4 Unreviewed; 773 AA.
AC N1R9A0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein B {ECO:0000313|EMBL:EMT61681.1};
GN ORFNames=FOC4_g10014748 {ECO:0000313|EMBL:EMT61681.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT61681.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB726996; EMT61681.1; -; Genomic_DNA.
DR AlphaFoldDB; N1R9A0; -.
DR STRING; 1229665.N1R9A0; -.
DR HOGENOM; CLU_012383_1_0_1; -.
DR Proteomes; UP000016929; 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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR Gene3D; 3.40.1620.60; -; 1.
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 InterPro; IPR034028; ZnMc_ADAM_fungal.
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; PF13688; Reprolysin_5; 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 Integrin {ECO:0000313|EMBL:EMT61681.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..773
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004111150"
FT TRANSMEM 694..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..484
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 508..598
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 773 AA; 83660 MW; 1F761AC71BCE9DAE CRC64;
MVSLWSIATA IAGVALFFET SLASSVKRNA VSYISFIDEP VINTPSHRIR ADSHFDLLFS
LHNGQQKIRL KLEPNHDILH ENFAITHIGA DGAVRSVETV NREDEKVFKG HVFIQRVGRE
GWTNAGWARI TMHRDGKEPV FEGTLRIDGN HHHIHTGTNY QQVRHEDDPI LSASEARDDV
MVVWRDSDIM SFNPTELKRR GASAALCDSD TLSFNSKFHE LQDFDTFGAA NTKSLFGRQS
IDTGTGNDGS SVDLESTIGS VNGCPTSRRV ALLGIATDCG YTSTFNSTEA LRKNVIRMVN
DASEVYEKSF NITLGIQNLT ISDGSCPGSP SDTAPWNQKC SNSVDLSDRL NLFSAWRGQN
EDSNAYWTLL STCNTDSAVG LAWLGQLCRP GASANSNTGG RNETVAGANV VVKTSAEWQV
FAHETGHTFG AVHDCTSQTC PVSSDAQSCC PLSKSSCDAQ GDFIMNPSSR EGISEFSPCT
IGNICSGFRR NVNTECLTDN RNVKTISGQQ CGNGIVEEGE DCDCGGEASC GDNPCCDAKT
CKFKGQAECD NSNEECCTDK CKFASSGTVC RSSTGPCDPE EKCTGSSATC PKDKHSDDGT
DCGDSLQCAS GQCTSRDEQC RANYQNTTSS SVKACTNSCL LSCQASGDGF CTQRNQNFLD
GTPCGGGGRC QNGSCEGAST WKEIENWFKN NKNIAIPVGC VLAALLLLSI SCCCFSCIKR
RIARRRAAKQ PAMGAWPGYP RGPVPNQQGP YMYAPIDNNN GWQQQRTRSM RYA
//
