ID A0A016TRF7_9BILA Unreviewed; 980 AA.
AC A0A016TRF7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dynamin-type G domain-containing protein {ECO:0000259|PROSITE:PS51718};
GN Name=Acey_s0083.g1655 {ECO:0000313|EMBL:EYC05227.1};
GN Synonyms=Acey-fzo-1 {ECO:0000313|EMBL:EYC05227.1};
GN ORFNames=Y032_0083g1655 {ECO:0000313|EMBL:EYC05227.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC05227.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001270};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004374}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009995}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC05227.1}.
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DR EMBL; JARK01001419; EYC05227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016TRF7; -.
DR STRING; 53326.A0A016TRF7; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008053; P:mitochondrial fusion; IEA:InterPro.
DR CDD; cd09912; DLP_2; 1.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR006884; Fzo/mitofusin_HR2.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR PANTHER; PTHR10465:SF0; TRANSMEMBRANE GTPASE MARF-RELATED; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF04799; Fzo_mitofusin; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF111479; Fzo-like conserved region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 849..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..558
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
SQ SEQUENCE 980 AA; 111177 MW; CD0F2C6DAAC8AD26 CRC64;
MDINSMDPTG EDIIETFASF PNVTFIWKYE GDDTSSFNAV PNIHPMKWVP QTDLLADKRL
SLFITHGGMN SMLESMFHGK PMIVIPLFGD QQLNSKNVIR IGTGMLVDRN NLNKNTLTEA
IQRTLGNKKI AREAAFVASS LAGRPQQYRE DIAKWAKIII EHGKMNHLLL HSRNMNLIQY
YGLDILAFLI SRFTAQHFYG AKMYGVTHGG AGDSSRLNLS LKTARRMNGE AEPLLRFAEA
KKVLGEIYTD LGKHVDELDE VYKGIVEPTG GGAGDSECMV PDEQAAEIEL FRESINTIME
TFRRDNMKVV FFGRTSNGKS TTINAMLHAK ILPQGMGHTT CCFLQVQGCN EDTGYLLLED
NPTRIPIDQL SKIGHALSSD NSGLPAMGQD SLLRVFYPKG RGETENRLLQ NDVVILDSPG
VDLSPEFDSW IDKHCLDADV FVLVLNAEST LTQAEKSFFH RVAKKLSKPN VFILNNRWDA
SAAESEHVED VKQQHLTRFR QFLVNELEVA TDRDVKDRIF FVSSREMLDS RLKARGLIKT
PYQMDGHQVR AMEFEMFERQ FEQCISRAAI RTKFEAHNRR ANEIIARMRA NVDVVHAAAT
KAKESLEYSL KRSTQVFNDC RMNFAQFERA YREQTERLRA EVHLKVSADF SEEIMRLEAI
VDRFNMPFLD TTQGIIEYKR ALAEFTDKCV SSDLEARCTG GLMSRIWNLE NDMFQYVTKI
LAEPYQHKLE EVWRYRAPFK FSICVDAPAL TKDFHEDLEF RFTFGLSAII RRIIAYRSGQ
PVTAIQANLL TPMALRNAGR SNEDLHNEAM QKAVEENAMM TQMVLTSASY LANGSIGLLV
VGGIVYRAVG WRVIAVTAAA YGGLYVWERM RWNSHAKEQH LKEQFRSHLA ARMQQVGAAH
TTHCETQAMR EMDQVFDGLR ATVAGVHREM KEELDKSKKE IEKVDGTLKS LLTIKGKTAF
LLRNLEQFAT TFLRADTPSP
//
