SEY1_COCIM
ID SEY1_COCIM Reviewed; 866 AA.
AC Q1DL22; A0A0D6K9M2; J3K1Z5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
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}; ORFNames=CIMG_08991;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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. {ECO:0000255|HAMAP-Rule:MF_03109}.
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}.
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DR EMBL; GG704915; EAS27787.1; -; Genomic_DNA.
DR RefSeq; XP_001239370.1; XM_001239369.2.
DR AlphaFoldDB; Q1DL22; -.
DR SMR; Q1DL22; -.
DR STRING; 246410.Q1DL22; -.
DR EnsemblFungi; EAS27787; EAS27787; CIMG_08991.
DR GeneID; 4558309; -.
DR KEGG; cim:CIMG_08991; -.
DR VEuPathDB; FungiDB:CIMG_08991; -.
DR InParanoid; Q1DL22; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..866
FT /note="Protein SEY1"
FT /id="PRO_0000384981"
FT TOPO_DOM 1..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 768..770
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 771..791
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 792..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 48..305
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 840..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 58..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 866 AA; 98347 MW; AA800566DAF1ECF5 CRC64;
MVSNGHFAYA EDDPVASYEH GVQVVDEDKE FNPNLSKYLA YEGVTPAGFN YHLISVFGSQ
STGKSTLLNY LFGTHFSVMS ETERRQTTKG IWMSKNKRQD CERENSLPHL QNNRMADNIL
VMDVEGTDGR ERGEDQDFER KSALFALATS EVLIVNIWEH QVGLYQGANM GLLKTVFEVN
MQLFLKDKKS TPRSLLFFVI RDFLGTTPLQ NLQNTLMQDL QRIWTSLSKP PGLENSTIED
YFDFEFAALP HKNFQTDKFV AEVKKLSMRF REGHRDPSKG NKTEGGIFLS EYHRRIPADG
FAVYAEGIWD QIVNNKDLDL PTQQELLAQF RCDEISREVL VAFDEAVVPF ETKQAEAAQS
GNPEVFAGLG PAMKNARVKT LSAFETEASR YHKRVFQMKR AELEDKMDTR LKVLFSGQLT
AAHKSGIAQF SDAVSAAVKA GQKKGASYDF ADIVNKEKRI ALERFEDDAK ATVIEGACWS
NYTQELALYQ KDLEKISAQL RKDEMRRLAT RVERWVRSRL GESVGLEFNA LGSGRGGSGA
PETGDKPSED TIWDRIWSIF VATVLEAEQR FTERASSFDA SLEEVDVGLW RLRRKAWGVL
RSKIDEEMME GNLLLKLREN FEDKFRYDSA GVPRIWRPTD DIEGLYTKAR ESTLTLIPLL
SRFRLQETNA TPQLDRWVGY TPSAATPADE EDLVPIGGVD DDGKSLEEEM TMLSETKRQD
LTVRFKKAAD GVYVEAKRSA IGGMTQIPVY FYILLLALGW NEIIAVLRNP VYFFMLFLCS
VAAYIIYQLN LWGPMVKMAE AASHQAVEEG KKRLRDLLEP SDIGHHGMKY KNGTEQYEMS
HVRSGRNATK INERDDDDEV EGEETW
