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Database: UniProt
Entry: I7MKN2_TETTS
LinkDB: I7MKN2_TETTS
Original site: I7MKN2_TETTS 
ID   I7MKN2_TETTS            Unreviewed;       755 AA.
AC   I7MKN2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Protein SEY1 homolog {ECO:0000256|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_03109};
GN   ORFNames=TTHERM_00139640 {ECO:0000313|EMBL:EAR99602.2};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR99602.2, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
CC   -!- FUNCTION: Probable GTP-binding protein involved in generating and
CC       maintaining the structure of the tubular endoplasmic reticulum network.
CC       {ECO:0000256|ARBA:ARBA00029381}.
CC   -!- FUNCTION: Probable GTP-binding protein that may be involved in cell
CC       development. {ECO:0000256|HAMAP-Rule:MF_03109}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03109}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03109}.
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DR   EMBL; GG662639; EAR99602.2; -; Genomic_DNA.
DR   RefSeq; XP_001019847.2; XM_001019847.3.
DR   AlphaFoldDB; I7MKN2; -.
DR   STRING; 312017.I7MKN2; -.
DR   GeneID; 7823447; -.
DR   KEGG; tet:TTHERM_00139640; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   InParanoid; I7MKN2; -.
DR   OrthoDB; 1606at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_03109; Sey1; 1.
DR   InterPro; IPR030386; G_GB1_RHD3_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008803; RHD3/Sey1.
DR   InterPro; IPR046758; Sey1/RHD3-like_3HB.
DR   PANTHER; PTHR45923; PROTEIN SEY1; 1.
DR   PANTHER; PTHR45923:SF2; PROTEIN SEY1; 1.
DR   Pfam; PF05879; RHD3_GTPase; 1.
DR   Pfam; PF20428; Sey1_3HB; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03109};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03109};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03109};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_03109, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03109,
KW   ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM        1..683
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        705..707
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   TRANSMEM        708..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        729..755
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   DOMAIN          36..253
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51715"
FT   BINDING         46..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   755 AA;  88660 MW;  84AE973FC7BE39AA CRC64;
     MSEQSQNQYH HLIDDQCQLI PGLTNFIRQS GLGQSHNSYN IVSIIGSQNS GKSTLLNRVF
     GTNFQMLSGS SRTQTTKGIW VSRDKEQNIL ILDVEGSNSR QRGKAEKGSE FYERSTALFA
     LAFSQILIIN CNSLNLGHES EYSIIKIIME MNIRLFRSDQ VKQMLIIIRD FNDEVDNFKE
     VTESIRNEIY GIWGEIQKPP EFANVQPEQI FKIDFFTSSH FQYQRQKFES DMVQLRDRFI
     NPGNPFNLFK GYNYNTNIPI EALEDLATTL WDTIQKNEDL NLPNQKLQAS QVRCLKIKDQ
     AIDLINQDLQ KLKQDAESNY LTNFNERAQN IVTRSLHHYD TESQYYVEKI KLEMRKVLND
     ELKTALYPIF NQQITSLQQN IKNELKNNLD ALDSRNTSFI KYMDDLSFIR QQIKQVILQG
     LHQSLPFNEY KVDWEITKID SQLSKVLEEI INNAREIQFV KYINSQEKTI KNSIDNLISN
     CFDTLDLEFW TTIRSGFNQI LKENETRIRD QISQFFDHSR VDKEMNNIIH QSHQFLQDDI
     QKKIRELSYY LLKRFKRTFL KDEKGLTRKW KELEEPVIQQ LFLDSRKSIE DILQEFTRFK
     VSPPQSHQFS ARMSNMFSSE IVGRAQMNDE VRQAKQSLDF SSEDFSVLLD TSQINKIKQQ
     FIDESEEEYN QVLRQRNTSF NTNVPKWMWV VLVFFMYDDV LRWMANPLLL YPIILLGSFI
     GLCVATGYQS IPKVLFQQIF GQLTTLLGPL LLKIK
//
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