ID H2AY39_KAZAF Unreviewed; 803 AA.
AC H2AY39;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=GB1/RHD3-type G domain-containing protein {ECO:0000259|PROSITE:PS51715};
GN Name=KAFR0G02570 {ECO:0000313|EMBL:CCF59289.1};
GN Synonyms=SEY1 {ECO:0000256|HAMAP-Rule:MF_03109};
GN ORFNames=KAFR_0G02570 {ECO:0000313|EMBL:CCF59289.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF59289.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF59289.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC Concentrated in punctae along the ER tubules. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03109}.
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DR EMBL; HE650827; CCF59289.1; -; Genomic_DNA.
DR RefSeq; XP_003958424.1; XM_003958375.1.
DR AlphaFoldDB; H2AY39; -.
DR STRING; 1071382.H2AY39; -.
DR GeneID; 13887268; -.
DR KEGG; kaf:KAFR_0G02570; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; H2AY39; -.
DR OrthoDB; 1606at2759; -.
DR Proteomes; UP000005220; Chromosome 7.
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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03109}; GTP-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03109};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03109};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03109};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03109,
KW ECO:0000256|SAM:Phobius}.
FT TOPO_DOM 1..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TRANSMEM 699..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 720..722
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TRANSMEM 722..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 744..803
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT DOMAIN 47..276
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000259|PROSITE:PS51715"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
SQ SEQUENCE 803 AA; 92552 MW; FF1316B752E88BC6 CRC64;
MAPDNHDHTL GHESIQLVNE SKEFSTELLP YLQKIASSNV DNLVQPHESY HVISVFGSQS
SGKSTLLNIL FNTTFDTMDA KVKRQQTTKG IWLSHTKQVN TTKSANTPLA SDMFILDVEG
SDGAERGEDQ DFERKAALFA ISVSEVLIVN LWEQQIGLYQ GNNMGLLKTV FEVNLSLFGK
RHEHKILLLF VIRDHVGVTP LSSLSDSLIS SLENMWKELN KPQGCEDLAL YDLFDLKFVG
LSHKLLQEEK FVNDVKALGT CFSFPEKEEY YFKKEYHHLL PLDGWSMYAE NCWEQIEHNK
DLDLPTQQIL VARFKTNEIL NESFDASFIN DDTFNSELKI LIDDIDLKDS LFELLKVAKN
KCIEQYDILA SRYNKMVYME NRAELLKKIS SFLYDNAVVE LSENFINKLF TDMEDKMKVR
AQGLSFSEQL DDCVDSINAD YDLLLDNFMD SELIVIDLKE SLKARLDDLL LGKVNELRTK
ETDLILSRIR KNLKFSIKEQ ILPLLANPTL QIWDDVMSAF YDLIDEALVP FKSQDSDDLD
FGIGLSDNED KNIADRIKLS GWLTLTVMIH DYLTEDTIVG LLRDRFENKF RFADDDTPIL
WKNEQQIDTS FRLAKEHAME ILSVLSIVKT SDNVEVVPEI PNYLLENEYT DELGIYHIDR
FAHILNELQK EKISKQFRRQ INLTVLDAKR SIITSTNHIP MWIYAIIVVL GWNEFMLVIR
NPVFVTLLLI GSVAFYFIHK FDLWGPVLSV VNTAIGETKE TLKDKLRTFV LEEDYATAKN
RDMKDTQSFE TEIVNEKIDK LDD
//
