ID A0A093V8N9_TALMA Unreviewed; 802 AA.
AC A0A093V8N9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein B {ECO:0000313|EMBL:KFX48500.1};
GN ORFNames=GQ26_0122060 {ECO:0000313|EMBL:KFX48500.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX48500.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX48500.1}.
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DR EMBL; JPOX01000012; KFX48500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V8N9; -.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_012383_1_0_1; -.
DR Proteomes; UP000029285; 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:KFX48500.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..802
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001892714"
FT TRANSMEM 701..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..483
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 508..597
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 741..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 802 AA; 86260 MW; 2559A5587A41C6DC CRC64;
MKFGVSWLCA TLSATAIFLQ RGDARSQAPP PIQHVSELEN VVIHTPSHRI HSQSNFDITF
TIHNHAEPIK LKLEPNHDVL AEDAEVQYLN ADGTIRHTES IDRRDHRVFK GSAFTEIEPD
HWTYAGWARV YVKRDGPNPL FEGAFSLMHD YHNIKLRSSY MRSRSDFDVI PAEKDEDYMV
IFKNSDMYWD EEHTELKRSL PDPSCEADKL DFNTDPNHPV FRPPQQSPNL ASMSFDQLLG
LSKRQSDTGN VAGNAGGINL ASTIGDTTGC PNSRLVALVG VATDCNFLNA FGNNESAARA
DVISMFNSAS SVYERTFNIS LGLKNLTMSP AECPDVPSKA APWNLPCTSG NVSSRLSDFT
AWRGEQSDEN AYWTLMTNCP TNSEVGVSWL GQLCVHGSTN ASVAGANVVV KTATEWQVFA
HETGHTFGAV HDCDPSACQQ GLQTTSQCCP LTSSTCNANG QYLMNPSTAS NLENFSQCTV
GNICSAIGRN SVRSNCLVNN KDVVTYTGSQ CGNGIVESGE DCDCGGTAGC GDNACCDPTT
CKFKNSAVCD DSNEPCCSGC QFKAANTTCR ASTGPCDIAE VCSGTSGSCP ADKFVDDGKS
CTRGNATGLT CASGQCTSRN QQCRTILGAV LGSNDTYACD DSSCTLWCAS SILPSNQCVS
MQQNFLDGTP CNGDGHCDNG QCMGSSVGGE IKSWIDRHKP LVIGLAATIG GLLVLILLSY
ITSACRRQRY RKVVPAPLPD GRRYQGYRGP PAPPPGAGWW SGPMPPATQQ QRSPVYGAPP
AYAPPGYDHN GAPWPGVQPR YA
//
