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Database: UniProt
Entry: D8LK99_ECTSI
LinkDB: D8LK99_ECTSI
Original site: D8LK99_ECTSI 
ID   D8LK99_ECTSI            Unreviewed;       454 AA.
AC   D8LK99;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   28-FEB-2018, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBN79633.1};
GN   ORFNames=Esi_0283_0033 {ECO:0000313|EMBL:CBN79633.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales;
OC   Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN79633.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBN79633.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C.,
RA   Brownlee C., Carrano C.J., Charrier B., Cho G.Y., Coelho S.M.,
RA   Collen J., Corre E., Da Silva C., Delage L., Delaroque N.,
RA   Dittami S.M., Doulbeau S., Elias M., Farnham G., Gachon C.M.,
RA   Gschloessl B., Heesch S., Jabbari K., Jubin C., Kawai H., Kimura K.,
RA   Kloareg B., Kupper F.C., Lang D., Le Bail A., Leblanc C., Lerouge P.,
RA   Lohr M., Lopez P.J., Martens C., Maumus F., Michel G.,
RA   Miranda-Saavedra D., Morales J., Moreau H., Motomura T., Nagasato C.,
RA   Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F., Pommier C.,
RA   Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C.,
RA   Segurens B., Strittmatter M., Tonon T., Tregear J.W., Valentin K.,
RA   von Dassow P., Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of
RT   multicellularity in brown algae.";
RL   Nature 465:617-621(2010).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; FN648468; CBN79633.1; -; Genomic_DNA.
DR   ProteinModelPortal; D8LK99; -.
DR   InParanoid; D8LK99; -.
DR   Proteomes; UP000002630; Unplaced LGUn.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.30.250.10; -; 2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002630};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   454 AA;  48785 MW;  6EA8DF000CA95D7F CRC64;
     MASKNNNPDN AAATASLLED FVDFLNEAWT AYHATAEARR RLLAAGFEEL DESQATHDVK
     PVSKASKAGF LQLATQPYGG GLWHTWFDRD LGVAGRAIVK RGEGKYSHDL VKINRPVLRI
     PTLAIHLTKA DERKSFSPNL QSNFFPVLAT EVKAKLTAGG ASSKAAAGEG ESPGKEGGGD
     ERHHALLVEM VAEELGCQPE DVKDFELQFW DTQPSCLGGA CSEFVFSGRL DNFCSSWQSI
     RALIDGCEGD GLASCKGVRS VFLFDHEEVG STSCHGAAGT LLPDCMKRIA KGLAASPSDF
     VMEAVVRKSF LVSADMAHAL HPNYQDRHDP ALGPKIHSGM VLKHNANQRY ATNAVTAFFF
     RELGARAGLP TQEFAVKSDS ACGSTIGPTL SALSGIRTVD VGSPQLSMHS IREMMGADDA
     VFGYRHIKGV FVGCFSCFFF ASGAREEGCC LGRL
//
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