ID   SEY1_NEUCR              Reviewed;         862 AA.
AC   Q9P5X6; Q1K8N0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
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; ORFNames=B3E4.060, NCU09610;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; AL355931; CAB91394.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34138.1; -; Genomic_DNA.
DR   PIR; T49593; T49593.
DR   RefSeq; XP_963374.1; XM_958281.2.
DR   AlphaFoldDB; Q9P5X6; -.
DR   SMR; Q9P5X6; -.
DR   STRING; 5141.EFNCRP00000009417; -.
DR   EnsemblFungi; EAA34138; EAA34138; NCU09610.
DR   GeneID; 3879530; -.
DR   KEGG; ncr:NCU09610; -.
DR   VEuPathDB; FungiDB:NCU09610; -.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   InParanoid; Q9P5X6; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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   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..862
FT                   /note="Protein sey1"
FT                   /id="PRO_0000155136"
FT   TOPO_DOM        1..744
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        745..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        766..768
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        769..789
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        790..862
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          53..288
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          485..506
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..862
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         63..70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   862 AA;  96417 MW;  41CE6DD50996777A CRC64;
     MNGHFAAVDN GNGSSPDSNA HSFEHGIQVI NEDKQYNTNL NEYLNETHVA EAGFNYHLIS
     VFGSQSTGKS TLLNHLFGTQ FSVMSERERR QTTKGIWMSK NKNEGKMADN ILVMDVEGTD
     GRERGEDQDF ERKSALFALA TSEVLIVNIW EHQVGLYQGA NMGLLKTVFE VNMQLFLKDK
     QNQTRSLLFF VIRDHIGVTP LANLRNTLIQ DLTHIWSSIS KPAGLENSKI EDYFDFAFAA
     LPHKILQPDK FISEVQNLGS RFIAGHRNKD SDATDDQELT GGVFLPEYHR RIPADGLSIY
     AEGIWDQIVS NKDLDLPTQQ ELLAQFRCDE IAREVQIAFD AAIAPLEEQQ AESTRAGKPA
     VLPNLGQIGA EAREKCVKNF ETQASRYHKG VYTTKRAELE DKIDNRLKAL YQAHLTAAHK
     AGVTAFSEAV ANAVKAGQKA GGAYEFAEIV EKQKTKTLEI FKKEAQSLAI PGVAWSNFKP
     QYLIFEKELD EVSARLRKEE MRRLAIRVER WVKSRLGDAI GLEFNKLGSG RGGSGAPESG
     EKPATEKDIW DRVWKAFISI VGEAESRFTD RAKSFEASDD EVQVGLWRLR RKSWVALREK
     IEEEVMESNI LMKLRENFED KFRYDEDGVP RIWRPSDDIE GIYTRAREST LGLVPLLSRF
     RLTSTSAPPD LIEFVGPQPH GVEPGDEEDL TPIGGVDEDE GKSLEEETTI LSEPKKQDLV
     VRFKKMADGV YVEAKRSAIG GITQVPLYFY AVLLVLGWNE FVMVLRNPIL FLLLLLISGG
     TYVAYSLNLL GPMMQMANAA STQGMEIGKA KLRDFLENHE GARGALGMPP KNAQRVESGI
     SMDTLDSNGK RKETGLGAED DI