SEY1_ASPCL
ID SEY1_ASPCL Reviewed; 865 AA.
AC A1CPP3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 64.
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=ACLA_023280;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW07614.1; -; Genomic_DNA.
DR RefSeq; XP_001269040.1; XM_001269039.1.
DR AlphaFoldDB; A1CPP3; -.
DR SMR; A1CPP3; -.
DR STRING; 5057.CADACLAP00002723; -.
DR EnsemblFungi; EAW07614; EAW07614; ACLA_023280.
DR GeneID; 4701515; -.
DR KEGG; act:ACLA_023280; -.
DR eggNOG; KOG2203; Eukaryota.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
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:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:EnsemblFungi.
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..865
FT /note="Protein sey1"
FT /id="PRO_0000384969"
FT TOPO_DOM 1..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 767..769
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 791..865
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 47..303
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 673..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 478..504
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 699..719
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 824..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 865 AA; 97603 MW; 9385298ADC5C8C22 CRC64;
MAPCHSRDAS IMIDSYEHGV QVIDENKEFK NPNISKYLSL ENVTHAGFNY HLISVFGSQS
TGKSTLLNHL FGTHFSVMAE RERRQTTKGI WMSKNKNGGE VSADHSARMA DNILVMDVEG
TDGRERGEDQ DFERKSALFA LATSEVLIVN IWEHQVGLYQ GANMGLLKTV FEVNLQLFLK
DKNTTHRSLL FFVIRDFVGT TPLQNLQTTL MEDMSRLWDS ISKPPGLENS SVHDYFDFQF
YGLPHKSYQP EQFVAETKKL SLRFREGQRD PAMDARRGKF SEGGVFLPEY HRRIPADGFS
RYAEGIWDQI VNNKDLDLPT QQELLAQFRC DEIMREVMLV FDEAITPFEE KQSQAARLGE
PEVLGGLGAA MRSSRTKAIN EFEIEASRYH KGVYQRKQEE LEDKIDTRLK ALLQGQLNAA
HKSGINEFTE AVSAAVKMGQ KHGTGYDFAE IVNGEVRKAV AKYEDVARST VVESTSWRDY
SQELSLYEKE LAEVSGRLRR EEMRRLASRV ERWVQSRLGD SVGLEFNALG SGRAGGGAPE
SGEKPSEKAF WDRIWNVFVE TVLDAERRFT DRASSFDASL EEVDVGLWRL RRKSWGVLRA
KVDEEMTEGN LLLKLRENFE DKFRYDDAGV PRIWRPTDDI EGIYTRARES TLTLIPLLSR
FRLAETSAPP PLDRWIGHTP SSATPADEED LPPIGGVDEE EGKSLEEEMT ILSEAKSQEL
TVRFKKSADG VYVEAKRSAI GGMTQVPLYF YGLLLALGWN EIVAVLRNPA YFFLLFVCAV
GAYVTYQLNL WGPIIKMTEA ASNQALVEGK KRLREFLESS DTGRQAIAMS TSGAGSGRSG
EQYEMSDFSQ KSKTASPADE DTDTL
