ID SEY1_AJEDR Reviewed; 875 AA.
AC C5GMK3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=BDCG_05428;
OS Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER-3 / ATCC MYA-2586;
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; EQ999977; EEQ90308.1; -; Genomic_DNA.
DR AlphaFoldDB; C5GMK3; -.
DR SMR; C5GMK3; -.
DR STRING; 559297.C5GMK3; -.
DR VEuPathDB; FungiDB:BDCG_05428; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; YAEGVWD; -.
DR OrthoDB; 1606at2759; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 CDD; cd01851; GBP; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR046758; Sey1/RHD3-like_3HB.
DR PANTHER; PTHR45923; PROTEIN SEY1; 1.
DR PANTHER; PTHR45923:SF2; PROTEIN SEY1; 1.
DR Pfam; PF05879; RHD3_GTPase; 1.
DR Pfam; PF20428; Sey1_3HB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..875
FT /note="Protein SEY1"
FT /id="PRO_0000384967"
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..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 49..307
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 676..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 482..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 843..865
FT /note="Basic and acidic 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 875 AA; 98869 MW; 0BA48C1F3691E30C CRC64;
MVANGHFASN GEGQDSGSYE HGVQVIDEDK EFNPNVSRYL TYENVTPAGF NYHLISVFGS
QSTGKSTLLN HLFGTHFSVM SETERRQTTK GIWLSKNKRV ESSKDRDPQM KMADNILVMD
VEGTDGRERG EDQDFERKSA LFALATSEVL IVNIWEHQVG LYQGANMGLL KTVFEVNLEL
FLKDNKSTPR SLLFFVIRDF VGTTPLQNLQ NTLLQDLNRI WSSLSKPAGL ENSTINDYFD
FAFAGLPHKN FQPEKFVDEV QKLSTRFRNA HRDPNNVDSR GTGSIEGGIF LPEYHRRIPA
DGFAVYAEGV WDQIVNNKDL DLPTQQELLA QFRCDEISRE ALVAFDEAIS PFESKQAEAV
QAGSPQVLGG LGPVMRNARM NAVKNFDAEA SRYHKRVYQM KKSELEEKID TRLKALFLGQ
LNAAHRSGVQ DFSESVSAAV KAGQKRGASY DFAEIVSRER QLAIEKFEKE ARSTLVEDAP
WSNYQQELSL YQKDLERISG QLRRDEMRRL ATRVERWVRS RLGESVDLEF NALGSGRGGS
GAPEFGDKPS ENTIWDRVWT IFVDTVLDAE RRFTERASSF DASLDEVDVG LWRLRRKSWG
VLRAKIEEEV MEGNLLLKLR ENFEDKFRYD DAGVPRIWRP TDDIESVYTQ ARESTLTLIP
LLARFRLAET NAPPPLDKWI GHTPSSATPA DEEDLTPIGG VDEDEGKSLE EEMTMIGEAK
KQDLIVRFKK TADGVYVEAK RSAIGGITQV PLYFYGLLLA LGWNEIMAVL RNPAYFFLLF
VCAIGAYVTY QLNLWGPIIK MTEAASHQAL EEGKRRLRDF LEASDTGRQA MAMSGARNAT
EEHEMSNLNR KSGERGGQKY RGEDVADDDD VDDDF
//
