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Database: UniProt
Entry: D7G2Q1_ECTSI
LinkDB: D7G2Q1_ECTSI
Original site: D7G2Q1_ECTSI 
ID   D7G2Q1_ECTSI            Unreviewed;       492 AA.
AC   D7G2Q1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Cell division protein {ECO:0000313|EMBL:CBJ26876.1};
GN   ORFNames=Esi_0048_0099 {ECO:0000313|EMBL:CBJ26876.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ26876.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBJ26876.1, 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., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; FN648685; CBJ26876.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7G2Q1; -.
DR   STRING; 2880.D7G2Q1; -.
DR   EnsemblProtists; CBJ26876; CBJ26876; Esi_0048_0099.
DR   eggNOG; KOG0731; Eukaryota.
DR   InParanoid; D7G2Q1; -.
DR   OrthoDB; 179729at2759; -.
DR   Proteomes; UP000002630; Chromosome LG23.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR   PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Cell cycle {ECO:0000313|EMBL:CBJ26876.1};
KW   Cell division {ECO:0000313|EMBL:CBJ26876.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          241..403
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          29..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  52843 MW;  11BD1A8649E8E77B CRC64;
     MVRTIVFVVL RIRAVAAGLG AMLGLGRWTK KSSSSNQSLF SSAGGKKKAA AGKSRGRRAT
     AFSRLFRKRT ATLLVVMLFV LAMGFRSAGT PAVTEVPMST FMQLMEGKRG ADVVESVRVS
     KTGTMFFKMN GKECYTLPLR VSKEVFKALC NSGIPFRASK SPPGLSFIFP VVYLLAVYYF
     IVKRGQGSMV GSTGKLASST ELDTSLTFGD VAGVDQAKSQ VQELVSMIKN PAPFIAAGAR
     LPSGLLMVGP PGTGKTLMAR VMAAEAGVPL PPPRRFRGVG GYLLIGRLPK FYYCSGSDFV
     EMYVGRGAAR VRKLFVKAGK TAPCIIFLDE LDALGKERSG TGGRQTNDEA EQTLNQLLAC
     MDGLDTNNNG VMVIAATNRY DVLDNALTRP GRFDRIVRVD VPDAAGREAI LKVHTRKMKL
     EDVDVLRAVA ELTPGLAGAE LATIANEAAI SAARRGSQQL LETDFLESVT NFYVSRKKGV
     AGLQNMFKGM LT
//
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