SEY1_PHANO
ID SEY1_PHANO Reviewed; 859 AA.
AC Q0V302;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 66.
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=SNOG_01612;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT91261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH445326; EAT91261.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001792248.1; XM_001792196.1.
DR AlphaFoldDB; Q0V302; -.
DR SMR; Q0V302; -.
DR STRING; 13684.SNOT_01612; -.
DR GeneID; 5969093; -.
DR KEGG; pno:SNOG_01612; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; Q0V302; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
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..859
FT /note="Protein SEY1"
FT /id="PRO_0000384994"
FT TOPO_DOM 1..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 764..766
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 788..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 49..291
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 525..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 476..496
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 820..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 859 AA; 96449 MW; 2547CBA633B2C3C3 CRC64;
MMMNSHFAGV GDNVDKEAYG HGIQVVDEDK VFNNNLSTYL NIEKVIPAGF NYHLISVFGS
QSTGKSTLLN YLFGTQFGVM AEQERRQTTK GIWMSKNKRP EGGSAMAENI LVMDVEGTDG
RERGEDQDFE RKSALFALAT SEVLIVNIWE HQVGLYQGAN MGLLKTVFEV NLQLFIKDSK
TIPKSLLFFV IRDHLGTTPL KNLQNTLTQD LSKLWSTISK PKGLENSRIE EYFDFAFVAL
PHKILQPEKF EEAVTKLSLR FKEGYNDPKT SGLVDEAELP IFQPQYHRRI PADGFPAYAE
GIWDQIVHNK DLDLPTQQEL LAQFRCDEIS REVLVLFDET IAPLEEKQAE DTRMGKPSVI
AELGAAMNAA RSTVFKDFET NASRYHKGVY KRKQAELEGK VDTRLKALSQ KQLNAAHKSG
VESFSDAVSA AVKAGQKKGA SYDFAQIVDS EKKKAIAQFG EQAKSIVIEG ASWSSFEHEL
KVYRKDLDDV SGRLRKDEMR RLATRIERWV RSRLDESVGL EFNKLGTGRG GSGAPEHGER
PPSEKDLWDR VWAIFTETVS SAEKRFTDRA QSFDASPEEV DVGLWRLRRK SWGVLRAKID
EEVMEGNILL KLRENFEDKF RYDEQGVPRI WRPTDDIEGI YTKARESTIT VIPLLARFKL
SKTSAPPPLD AWIGDAPASV TPADEEDLTP IGGLDEEEGK SLEEEMTVLS DAKQADLLIR
FKKTADGVYV EAKRSAIGGI TQVPLYFYGL LVALGWNEIV AVLRNPVYFI FLILCAVGAY
VTYTLNLWGP MIRMGNAASA QALEVGKERL REFLESSESG RQAMAMSGNQ PRGESVRMNR
LNGNGKKDED AEVEDLDDI
