SEY1_CANAL
ID SEY1_CANAL Reviewed; 790 AA.
AC Q9C0L9; A0A1D8PQG6; Q59RG8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109}; Synonyms=NAG6;
GN OrderedLocusNames=CAALFM_C604570WA; ORFNames=CaO19.2151, CaO19.9698;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / CAF2-1;
RX PubMed=11298769; DOI=10.1046/j.1432-1327.2001.02135.x;
RA Yamada-Okabe T., Sakamori Y., Mio T., Yamada-Okabe H.;
RT "Identification and characterization of the genes for N-acetylglucosamine
RT kinase and N-acetylglucosamine-phosphate deacetylase in the pathogenic
RT fungus Candida albicans.";
RL Eur. J. Biochem. 268:2498-2505(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION.
RX PubMed=12076781; DOI=10.1111/j.1574-6968.2002.tb11238.x;
RA Yamada-Okabe T., Yamada-Okabe H.;
RT "Characterization of the CaNAG3, CaNAG4, and CaNAG6 genes of the pathogenic
RT fungus Candida albicans: possible involvement of these genes in the
RT susceptibilities of cytotoxic agents.";
RL FEMS Microbiol. Lett. 212:15-21(2002).
CC -!- FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1
CC family proteins to generate and maintain the structure of the tubular
CC endoplasmic reticulum network. Has GTPase activity, which is required
CC for its function in ER organization (By similarity). Required for
CC virulence and resistance to cycloheximide. {ECO:0000255|HAMAP-
CC Rule:MF_03109, ECO:0000269|PubMed:12076781}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC Concentrated in punctae along the ER tubules. {ECO:0000255|HAMAP-
CC Rule:MF_03109}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB056468; BAB43823.1; -; Genomic_DNA.
DR EMBL; AB052111; BAB43817.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30373.1; -; Genomic_DNA.
DR RefSeq; XP_712426.1; XM_707333.2.
DR PDB; 5CA8; X-ray; 2.30 A; A=1-692.
DR PDB; 5CA9; X-ray; 2.80 A; A=1-692.
DR PDB; 5CB2; X-ray; 2.90 A; A=1-692.
DR PDBsum; 5CA8; -.
DR PDBsum; 5CA9; -.
DR PDBsum; 5CB2; -.
DR AlphaFoldDB; Q9C0L9; -.
DR SMR; Q9C0L9; -.
DR BioGRID; 1229054; 1.
DR STRING; 237561.Q9C0L9; -.
DR PRIDE; Q9C0L9; -.
DR GeneID; 3645961; -.
DR KEGG; cal:CAALFM_C604570WA; -.
DR CGD; CAL0000187915; NAG6.
DR VEuPathDB; FungiDB:C6_04570W_A; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q9C0L9; -.
DR OrthoDB; 418635at2759; -.
DR BRENDA; 3.6.5.5; 1096.
DR PHI-base; PHI:512; -.
DR PRO; PR:Q9C0L9; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
DR GO; GO:0008645; P:hexose transmembrane transport; IMP:CGD.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR45923; PTHR45923; 1.
DR Pfam; PF05879; RHD3; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..790
FT /note="Protein SEY1"
FT /id="PRO_0000155129"
FT TOPO_DOM 1..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 714..716
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 738..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 55..284
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT BINDING 65..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT CONFLICT 270
FT /note="D -> G (in Ref. 1; BAB43823/BAB43817)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> T (in Ref. 1; BAB43823/BAB43817)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="I -> V (in Ref. 1; BAB43823/BAB43817)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5CA9"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5CA9"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 170..191
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 212..229
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 259..273
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:5CA9"
FT HELIX 312..343
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 358..374
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:5CB2"
FT HELIX 379..396
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 398..422
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 423..427
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 433..448
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:5CA9"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 473..504
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 511..523
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 525..528
FT /evidence="ECO:0007829|PDB:5CB2"
FT TURN 536..545
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 546..561
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 564..579
FT /evidence="ECO:0007829|PDB:5CA8"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:5CA9"
FT HELIX 593..608
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 611..614
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:5CA9"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:5CB2"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:5CA8"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:5CA9"
FT STRAND 655..659
FT /evidence="ECO:0007829|PDB:5CA8"
FT HELIX 661..684
FT /evidence="ECO:0007829|PDB:5CA8"
SQ SEQUENCE 790 AA; 90239 MW; D0FA8BCF80F5CA56 CRC64;
MELSEGELSH TSSSSSFVPV DQRQLQDAIQ IIDENKHFNT GILDYINKTS PADVGNNYHI
ISVFGSQSTG KSTLLNRLFN TNFDVMDESN RQQTTKGIWL AYSPVVSTTL GHTTSKSNIL
VMDVEGTDGR ERGEDQDFER KAALFALSTS EVLIINIWET QVGLYQGANM GLLKTVFEVN
LSLFGKSKLE THNDHKVLLL IVIRDHVGVT PVESLAKTFT SDLQNMWSSL AKPAELEHLQ
FADFFDVTFH ALNHKVLQPK EFGEGINRLD DRLVVSNELF KPEYHHDVPI DGWTMYAERC
WEQIETNKDL DLPTQQILVA QFKCDEIVES VFQEFLAKYQ HHFKEVDAAP DFEELGALFA
DLRQDAFEDY DASASRYNKA VYEQKRKKLR WLINDKLKEV FDVHAKNLCN TLLEKFEKDL
VALKGKDFAV NVKTLSTKLV EDVNFQVSLM SLQGDLSLDE IILALTKDID AIVAKQQVIE
LNSIVNKSVK KLSASLSKSI QFELGDPNEE TWDNVLQQFK GVYEKFGGDF GLGTSSTQNQ
QAIEKFKFKS WCQFYDVTHK LISREKLLAL LQDRFDDKFR YDENGLPKLY LNEQDLEKTF
AVAKQHALQV LPILTFAKLA DGSEIVPDYD IFDSKLREQF LGGYDDSDDE EDHCFAEIIT
EQEKSEVLAK FKKEVDAKYI ETKRSIVQHI TQIPYYIYLI ILVLGWNEFM AIIRNPLFFS
LSIVLGATVY VLYYLGLLRP ALVVAQRTMD EVIVMAKTKL REVLIDDHEV TGRQLNKMAG
SKENIELDDM
