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Database: UniProt
Entry: Q9VYY3
LinkDB: Q9VYY3
Original site: Q9VYY3 
ID   UBA5_DROME              Reviewed;         404 AA.
AC   Q9VYY3; B4F5S5; B4F5S6; B4F5S7; B4F5S8; B4F5S9; B4F5T0; B4F5T1;
AC   B4F5T3; C0MLQ2; C0MLQ9; C0MLR0; Q8SYN2;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 132.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
GN   Name=Uba5 {ECO:0000303|PubMed:26872069,
GN   ECO:0000312|FlyBase:FBgn0030305};
GN   ORFNames=CG1749 {ECO:0000312|FlyBase:FBgn0030305};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-17;
RP   LEU-GLU-THR-GLU-22 INS; ASP-73; SER-163; GLN-169; ILE-309;
RP   ILE-309-310-ILE; SER-333; ARG-335 AND THR-385.
RC   STRAIN=ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377,
RC   ZBMEL384, ZBMEL398, ZBMEL84, and ZBMEL95;
RX   PubMed=18477586; DOI=10.1093/molbev/msn111;
RA   Baines J.F., Sawyer S.A., Hartl D.L., Parsch J.;
RT   "Effects of X-linkage and sex-biased gene expression on the rate of
RT   adaptive protein evolution in Drosophila.";
RL   Mol. Biol. Evol. 25:1639-1650(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-73; LYS-325 AND
RP   GLN-364.
RC   STRAIN=MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17,
RC   MEL18, MEL19, and MEL20;
RX   PubMed=19126864; DOI=10.1093/molbev/msn297;
RA   Parsch J., Zhang Z., Baines J.F.;
RT   "The influence of demography and weak selection on the McDonald-
RT   Kreitman test: an empirical study in Drosophila.";
RL   Mol. Biol. Evol. 26:691-698(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=26872069; DOI=10.1371/journal.pone.0149039;
RA   Duan R., Shi Y., Yu L., Zhang G., Li J., Lin Y., Guo J., Wang J.,
RA   Shen L., Jiang H., Wang G., Tang B.;
RT   "UBA5 mutations cause a new form of autosomal recessive cerebellar
RT   ataxia.";
RL   PLoS ONE 11:E0149039-E0149039(2016).
CC   -!- FUNCTION: E1-like enzyme which activates UFM1.
CC       {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with Ufc1. Interacts with
CC       Ufm1. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}.
CC       Nucleus {ECO:0000250|UniProtKB:Q9GZZ9}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown shows aberrant
CC       neuromuscular junctions in the larval muscle and abnormal wings,
CC       locomotive defects and a shortened lifespan in the adult fly.
CC       RNAi-mediated knockdown in the nervous system results also in
CC       aberrant neuromuscular junctions characterized by reduced number
CC       of type Ib boutons and increased bouton size in the larval muscle.
CC       {ECO:0000269|PubMed:26872069}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL49051.1; Type=Frameshift; Positions=177; Evidence={ECO:0000305};
DR   EMBL; AM999161; CAQ53523.1; -; Genomic_DNA.
DR   EMBL; AM999162; CAQ53524.1; -; Genomic_DNA.
DR   EMBL; AM999163; CAQ53525.1; -; Genomic_DNA.
DR   EMBL; AM999164; CAQ53526.1; -; Genomic_DNA.
DR   EMBL; AM999165; CAQ53527.1; -; Genomic_DNA.
DR   EMBL; AM999166; CAQ53528.1; -; Genomic_DNA.
DR   EMBL; AM999167; CAQ53529.1; -; Genomic_DNA.
DR   EMBL; AM999168; CAQ53530.1; -; Genomic_DNA.
DR   EMBL; AM999169; CAQ53531.1; -; Genomic_DNA.
DR   EMBL; AM999170; CAQ53532.1; -; Genomic_DNA.
DR   EMBL; FM246273; CAR94199.1; -; Genomic_DNA.
DR   EMBL; FM246274; CAR94200.1; -; Genomic_DNA.
DR   EMBL; FM246275; CAR94201.1; -; Genomic_DNA.
DR   EMBL; FM246276; CAR94202.1; -; Genomic_DNA.
DR   EMBL; FM246277; CAR94203.1; -; Genomic_DNA.
DR   EMBL; FM246278; CAR94204.1; -; Genomic_DNA.
DR   EMBL; FM246279; CAR94205.1; -; Genomic_DNA.
DR   EMBL; FM246280; CAR94206.1; -; Genomic_DNA.
DR   EMBL; FM246281; CAR94207.1; -; Genomic_DNA.
DR   EMBL; FM246282; CAR94208.1; -; Genomic_DNA.
DR   EMBL; FM246283; CAR94209.1; -; Genomic_DNA.
DR   EMBL; FM246284; CAR94210.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAF48050.1; -; Genomic_DNA.
DR   EMBL; AY071429; AAL49051.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_572722.2; NM_132494.3.
DR   ProteinModelPortal; Q9VYY3; -.
DR   SMR; Q9VYY3; -.
DR   BioGrid; 58505; 3.
DR   IntAct; Q9VYY3; 2.
DR   STRING; 7227.FBpp0073354; -.
DR   PaxDb; Q9VYY3; -.
DR   PRIDE; Q9VYY3; -.
DR   EnsemblMetazoa; FBtr0073505; FBpp0073354; FBgn0030305.
DR   GeneID; 32094; -.
DR   KEGG; dme:Dmel_CG1749; -.
DR   UCSC; CG1749-RA; d. melanogaster.
DR   CTD; 79876; -.
DR   FlyBase; FBgn0030305; Uba5.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   InParanoid; Q9VYY3; -.
DR   KO; K12164; -.
DR   OMA; ETHNYNI; -.
DR   OrthoDB; 1092362at2759; -.
DR   PhylomeDB; Q9VYY3; -.
DR   Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   GenomeRNAi; 32094; -.
DR   PRO; PR:Q9VYY3; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0030305; Expressed in 50 organ(s), highest expression level in arthropod fat body.
DR   ExpressionAtlas; Q9VYY3; baseline and differential.
DR   Genevisible; Q9VYY3; DM.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071566; F:UFM1 activating enzyme activity; ISS:FlyBase.
DR   GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0071569; P:protein ufmylation; ISS:FlyBase.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Golgi apparatus;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN         1    404       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000391944.
FT   ACT_SITE    250    250       Glycyl thioester intermediate.
FT                                {ECO:0000250}.
FT   METAL       226    226       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       229    229       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       303    303       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       308    308       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING      83     83       ATP; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     104    104       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     127    127       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     150    150       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     184    184       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   VARIANT      17     17       T -> S (in strain: ZBMEL157 and
FT                                ZBMEL377). {ECO:0000269|PubMed:18477586}.
FT   VARIANT      22     22       E -> ELETE (in strain: ZBMEL186 and
FT                                ZBMEL191).
FT   VARIANT      73     73       Y -> D (in strain: MEL02, ZBMEL84,
FT                                ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191,
FT                                ZBMEL229, ZBMEL377, ZBMEL384 and
FT                                ZBMEL398). {ECO:0000269|PubMed:18477586,
FT                                ECO:0000269|PubMed:19126864}.
FT   VARIANT     163    163       T -> S (in strain: ZBMEL95).
FT                                {ECO:0000269|PubMed:18477586}.
FT   VARIANT     169    169       R -> Q (in strain: ZBMEL229).
FT                                {ECO:0000269|PubMed:18477586}.
FT   VARIANT     309    310       LV -> II (in strain: ZBMEL145, ZBMEL191).
FT   VARIANT     309    309       L -> I (in strain: ZBMEL84, ZBMEL384 and
FT                                ZBMEL398). {ECO:0000269|PubMed:18477586}.
FT   VARIANT     325    325       E -> K (in strain: MEL18).
FT                                {ECO:0000269|PubMed:19126864}.
FT   VARIANT     333    333       P -> S (in strain: ZBMEL384).
FT                                {ECO:0000269|PubMed:18477586}.
FT   VARIANT     335    335       H -> R (in strain: ZBMEL186).
FT                                {ECO:0000269|PubMed:18477586}.
FT   VARIANT     364    364       E -> Q (in strain: MEL17).
FT                                {ECO:0000269|PubMed:19126864}.
FT   VARIANT     385    385       S -> T (in strain: ZBMEL186 and
FT                                ZBMEL384). {ECO:0000269|PubMed:18477586}.
FT   CONFLICT    177    177       L -> M (in Ref. 5; AAL49051).
FT                                {ECO:0000305}.
SQ   SEQUENCE   404 AA;  44167 MW;  C9C2EFE14D18062F CRC64;
     MSHAIDELQA IIADLKTELE TEPKSSGGVA SNSRLARDRI DRMSAEVVDS NPYSRLMALQ
     RMNIVKDYER IRYKAVAIVG VGGVGSVTAD MLTRCGIGKL ILFDYDKVEL ANMNRLFFTP
     DQAGLSKVAA AAATLSFINP DVEIETHNYN ITTVENFDRF LDTISQGGRI AGQPVDLVLS
     CVDNFEARMA INAACNERNL NWFESGVSEN AVSGHIQFIR PGDTACFACA PPLVVAENID
     EKTLKREGVC AASLPTTMGI TAGFLVQNAL KYLLNFGEVS DYLGYNALSD FFPKMTLKPN
     PQCDDRNCLV RQKEFQARPK PVLIEEKAVS EEPLHATNEW GIELVAEDAP ESNTTPAETP
     VMGEGLRLAY EAPEKSSETS EETVSAATAD ETSLEDLMAQ MKSM
//
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