SEY1_USTMA
ID SEY1_USTMA Reviewed; 845 AA.
AC Q4PEQ0; A0A0D1CZ41;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 86.
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=UMAG_12136;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003141; KIS71518.1; -; Genomic_DNA.
DR RefSeq; XP_011387503.1; XM_011389201.1.
DR AlphaFoldDB; Q4PEQ0; -.
DR SMR; Q4PEQ0; -.
DR STRING; 5270.UM01413P0; -.
DR EnsemblFungi; KIS71518; KIS71518; UMAG_12136.
DR GeneID; 23567897; -.
DR KEGG; uma:UMAG_12136; -.
DR VEuPathDB; FungiDB:UMAG_12136; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; Q4PEQ0; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
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..845
FT /note="Protein SEY1"
FT /id="PRO_0000155137"
FT TOPO_DOM 1..749
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 771..773
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 795..845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 112..334
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 823..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 831..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 845 AA; 94786 MW; 1EC0C5B2FD179334 CRC64;
MELNVDSAKQ LLAEHEQELQ SAHDAHSILL ASQPITAATT HPNATASNAA RAVPVVAPSS
VPTPTAASTP FISTQPPAPA QTGRMQLIDE QQKFNSADFS PHLENWGLAD AGFGYDLCAV
LGSQSTGKST LLNKLFGTNF DVMSESARQQ TTKGIWMCKG LKMNVLVMDV EGTDGRERGE
DQDFERKSAL FSMASAEVLI VNLWEHQVGL YQGANMGLLK TVFEVNLGLF QASRAKTAGA
KDKTLLLFVI RDHIGVTPLE NLSATIMADL TKIWHSLSKP QGLELSKITD FFDFMFTTLP
HKILQPAEFD KAVDVLRNRF VNPKDPNFVF KTEYHKRIPA DGLAHYLESI WEQVMTNKDL
DLPTQQELLA QFRCDEIANV AFAHFATSIK DFRKHIEGGS VVESLGADMA LHRSTALSKF
DRDASRYHQE VYKRKRIDLL DKLNGSLSPF FLGQLKNLHR LMLQSFKQAV LDRMRTEPNY
DFGEVVSSEK RTALAKFSAA AQAVLLTDTD WTIDDEVVEL DVEIQSISDT MRVEETKKMV
AQIERTFNKN IGEPVELALK SAKRSMWDEV LISFSTLLEQ AEATYVRKAT SFNCTDDENE
HALLALRRKS WMSMRAKVDE QTADSVIAAK LRNSFEDGFR YDDAGVPRVW KPEDDMDGAF
RKARDETLEL IALYAKIQAV DTTLMRELRS KFEDAEPVGL VVEDEAFDWH ATLSVLSETR
KNDIGMRFRK EADAMYVEAK RATVSSIAQV PLWMYGVMLV LGWNELMAIL SSPVYFAFLL
VLIASAYIVW RLNLSGPLIS VLRAVANEVH RLADAQLRTH FSQPLREPRP PAESRPAEQI
ELEPN
