ID T0Q5K0_SAPDV Unreviewed; 1518 AA.
AC T0Q5K0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=SDRG_12420 {ECO:0000313|EMBL:EQC29876.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC29876.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC29876.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC29876.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601577-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601577-2};
CC -!- SIMILARITY: Belongs to the peptidase M8 family.
CC {ECO:0000256|ARBA:ARBA00005860}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; JH767180; EQC29876.1; -; Genomic_DNA.
DR RefSeq; XP_008616715.1; XM_008618493.1.
DR STRING; 1156394.T0Q5K0; -.
DR EnsemblProtists; EQC29876; EQC29876; SDRG_12420.
DR GeneID; 19953147; -.
DR VEuPathDB; FungiDB:SDRG_12420; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2556; Eukaryota.
DR InParanoid; T0Q5K0; -.
DR OMA; DTYADYC; -.
DR OrthoDB; 49135at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00055; EGF_Lam; 2.
DR Gene3D; 3.10.170.20; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR Gene3D; 2.10.55.10; Leishmanolysin domain 3; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR001577; Peptidase_M8.
DR InterPro; IPR003842; Vacuolating_cytotoxin.
DR PANTHER; PTHR10942; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR PANTHER; PTHR10942:SF0; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF01457; Peptidase_M8; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR PRINTS; PR01656; VACCYTOTOXIN.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|PIRSR:PIRSR601577-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1518
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004569317"
FT TRANSMEM 1426..1447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 560..597
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 610..639
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 810..845
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1225..1265
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1471..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT DISULFID 587..596
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 629..638
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 835..844
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1255..1264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1518 AA; 160231 MW; B1C646A24F6D5094 CRC64;
MKMLLGIVLV LIRSAVGGHD CGHDELMERF LADVDTSTLR SPQNLVSSKS RRLDADGVAS
SLFNPIRISF DTSKLFSDPG YLCSNVGDVV SRDGSSYTCA PNDVLTSDKR SFITNVLLPA
ITSYFSKVLS VQSVSGNLVV PGIGCSANGQ WACCTNSMPP YLASTGIAKT DFLIHVTARP
TSGAVLAWAL PCNLDQYGRP ISGQANFGPN RLDASSAARS QQVGTALHEL THALGFSSSR
FPDFRQPLNG APWGAGNVVF NTLERGVAVS KIITPKVVAA VKQQFNCYNW VNAGGELENG
AQGTAATTTS HWEKRIFQNE YMTATASATP VFSALTLALF EDSGWYTANY SMAEALAWGY
LEGCTFATAK CSEWSSDYFC RAKGDHCTPT RDAKGYCNLA TYTSSIPAGF QYFGNAALGG
QDTYADYCPL NSGYSNGGCA NLGTYVTPGM GEILSSSSQC FQSTLSTSGT RYNDRVTSTP
VCYSVDRCTK TAMLVTVGTT QVSCPMAGGA VSVPGYSGSL SCPPANTICQ RLQNECSGAG
VLQTDGSCVC HPGFNGADCS LLNCPAANGA TCAGHGTCDG STGQCTCQSG YTGLACSLLV
CPGIDDPKYN AVECSNHGTC NAVTGACTCN AGYSGNACEC VPGCPGCGAN GSCDCKTGSC
ICAAGYYGTS CQTSQMPTVT TLELANATAY MGSVAAKSYQ FFRVQLDSSS SDVTVRVVTT
VGDADVYASF VTQTPTVGSL RASTFVSDAN RTDGVDAITL CGSLGVFPRG INDTFHFCRQ
PNTQFVQGAP GYLYIGVFGF AASRFAINVK LNKCSSESCS NHGTCGKYYA GVCACDRYWT
GDACNLPQCR PDCIDFDNCP VPGSSTPVGV VSRGLRNTSD CFGNGVCTVL PNADGVDQPT
CVCDPAYHYD RPNDAQSLCK VPIPSISFVE HYNSSFVVYA QSLDEQVEIG KWALYTINVQ
PSWSYVYVQL DDVSVTSDAL VLVRKNTLPS LDVTHPYPIQ AADGAAWATQ AGTQRILLTR
AASTLSDGLL YVGVYNSLYA RSSLAFSLNV QANSSCVNAS RICPEATSTC SPALDGLCAC
ATGYGGAFCD RGPIAHRRVW HNASAAINIS VQLRPGQWTY LTLDVPDPDV TFIKVQLSNI
DDAMPLLLVR GPLETGLPAL DLGAAFDFDA MAASAMSQTV VVPVSTACSG PTCYKVAVYN
KRFAADILLA QLSVQPVTAV SEVYPSYTCG GNGDVTICGG RGTCLDSKDG PSCSCKNGWH
GLTCASPNPI DMGTLWYASE NASLLCSVCT ATFSLPNDGG ALFTLPQSMQ PNTGIQLRVT
NLDGVSPTVY VAEVPPRSIY DFSRVSFSEG TEEVVQLLNE PLSGQFWVLV YSEAPITMST
SNASVSSRFQ IAASLVARNG SSSATASITD TGFLPSVMQW LTTSSAGITV FTILLIFLTL
VVGFFVYRIF RSPDNQDGAI RSIAHDIPVS NRPVMPSPAT EAPDSPLRNA GRSESASDNG
RRRSIDIELA EHPHVMQL
//
