SIR7_RAT
ID SIR7_RAT Reviewed; 402 AA.
AC B2RZ55; F1LQY4;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=NAD-dependent protein deacetylase sirtuin-7;
DE EC=2.3.1.286;
DE AltName: Full=NAD-dependent protein deacylase sirtuin-7;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9NRC8};
DE AltName: Full=Regulatory protein SIR2 homolog 7;
DE AltName: Full=SIR2-like protein 7;
GN Name=Sirt7 {ECO:0000312|RGD:1305876};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: NAD-dependent protein-lysine deacylase that can act both as a
CC deacetylase or deacylase (desuccinylase, depropionylase and
CC deglutarylase), depending on the context. Specifically mediates
CC deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other
CC histone deacetylases, displays strong preference for a specific histone
CC mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac
CC is mainly present around the transcription start site of genes and has
CC been linked to activation of nuclear hormone receptors; SIRT7 thereby
CC acts as a transcription repressor. Moreover, H3K18 hypoacetylation has
CC been reported as a marker of malignancy in various cancers and seems to
CC maintain the transformed phenotype of cancer cells. Also able to
CC mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the
CC context of nucleosomes. Also mediates deacetylation of non-histone
CC proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1,
CC RAN, RRP9/U3-55K and POLR1E/PAF53. Enriched in nucleolus where it
CC stimulates transcription activity of the RNA polymerase I complex. Acts
CC by mediating the deacetylation of the RNA polymerase I subunit
CC POLR1E/PAF53, thereby promoting the association of RNA polymerase I
CC with the rDNA promoter region and coding region. In response to
CC metabolic stress, SIRT7 is released from nucleoli leading to
CC hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I
CC transcription. Required to restore the transcription of ribosomal RNA
CC (rRNA) at the exit from mitosis. Promotes pre-ribosomal RNA (pre-rRNA)
CC cleavage at the 5'-terminal processing site by mediating deacetylation
CC of RRP9/U3-55K, a core subunit of the U3 snoRNP complex. Mediates 'Lys-
CC 37' deacetylation of Ran, thereby regulating the nuclear export of NF-
CC kappa-B subunit RELA/p65. Acts as a regulator of DNA damage repair by
CC mediating deacetylation of ATM during the late stages of DNA damage
CC response, promoting ATM dephosphorylation and deactivation. Suppresses
CC the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase
CC complexes by mediating deacetylation of DDB1, which prevents the
CC interaction between DDB1 and CUL4 (CUL4A or CUL4B). Activates RNA
CC polymerase II transcription by mediating deacetylation of CDK9, thereby
CC promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA
CC polymerase II. Deacetylates FBL, promoting histone-glutamine
CC methyltransferase activity of FBL (By similarity). Acts as a regulator
CC of mitochondrial function by catalyzing deacetylation of GABPB1 (By
CC similarity). Regulates Akt/AKT1 activity by mediating deacetylation of
CC FKBP5/FKBP51. Required to prevent R-loop-associated DNA damage and
CC transcription-associated genomic instability by mediating deacetylation
CC and subsequent activation of DDX21, thereby overcoming R-loop-mediated
CC stalling of RNA polymerases. In addition to protein deacetylase
CC activity, also acts as protein-lysine deacylase (By similarity). Acts
CC as a protein depropionylase by mediating depropionylation of Osterix
CC (SP7), thereby regulating bone formation by osteoblasts (By
CC similarity). Acts as a histone deglutarylase by mediating
CC deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that
CC destabilizes nucleosomes by promoting dissociation of the H2A-H2B
CC dimers from nucleosomes. Acts as a histone desuccinylase: in response
CC to DNA damage, recruited to DNA double-strand breaks (DSBs) and
CC catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ),
CC thereby promoting chromatin condensation and DSB repair (By
CC similarity). Also promotes DSB repair by promoting H3K18Ac
CC deacetylation, regulating non-homologous end joining (NHEJ). Along with
CC its role in DNA repair, required for chromosome synapsis during
CC prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By
CC similarity). Involved in transcriptional repression of LINE-1
CC retrotransposon via H3K18Ac deacetylation, and promotes their
CC association with the nuclear lamina. Required to stabilize ribosomal
CC DNA (rDNA) heterochromatin and prevent cellular senescence induced by
CC rDNA instability (By similarity). Acts as a negative regulator of SIRT1
CC by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase
CC activity (By similarity). {ECO:0000250|UniProtKB:Q8BKJ9,
CC ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000250|UniProtKB:Q9NRC8,
CC ECO:0000255|PROSITE-ProRule:PRU00236};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:47664, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:87828, ChEBI:CHEBI:87829;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47665;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47669;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD(+) = 3''-O-
CC propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:23500, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13758,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:138019, ChEBI:CHEBI:145015;
CC Evidence={ECO:0000250|UniProtKB:Q8BKJ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23501;
CC Evidence={ECO:0000250|UniProtKB:Q8BKJ9};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NXA8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8};
CC -!- ACTIVITY REGULATION: NAD-dependent protein-lysine deacetylase and
CC deacylase activities are activated by nucleic acids. Histone
CC deacetylase activity is activated by DNA. Protein-lysine deacylase
CC activity is activated by RNA. H3K18Ac histone deacetylase activity is
CC inhibited by methylation at Arg-390. H3K18Ac histone deacetylase
CC activity is inhibited by deubiquitination by USP7.
CC {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- SUBUNIT: Interacts with UBTF and the RNA polymerase I complex.
CC Interacts with components of the B-WICH complex, such as MYBBP1A,
CC SMARCA5/SNF2H and BAZ1B/WSTF. Interacts with ELK4, leading to
CC stabilization at target promoters for H3K18Ac deacetylation. Interacts
CC with histone H2A and/or histone H2B (By similarity). Interacts with
CC DNMT1. Interacts with SIRT1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BKJ9, ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9NRC8}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9NRC8}. Chromosome
CC {ECO:0000250|UniProtKB:Q9NRC8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NRC8}. Note=Mainly localizes in the nucleolus
CC and nucleoplasm. Associated with rDNA promoter and transcribed region.
CC Associated with nucleolar organizer regions during mitosis. In response
CC to stress, released from nucleolus to nucleoplasm. Associated with
CC chromatin. In response to DNA damage, recruited to DNA double-strand
CC breaks (DSBs) sites. Located close to the nuclear membrane when in the
CC cytoplasm. {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- PTM: Methylation at Arg-390 by PRMT6 inhibits the H3K18Ac histone
CC deacetylase activity, promoting mitochondria biogenesis and maintaining
CC mitochondria respiration. {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains.
CC Deubiquitinated by USP7, inhibiting the H3K18Ac histone deacetylase
CC activity and regulating gluconeogenesis.
CC {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; CH473948; EDM06872.1; -; Genomic_DNA.
DR EMBL; BC167031; AAI67031.1; -; mRNA.
DR RefSeq; NP_001100543.1; NM_001107073.1.
DR AlphaFoldDB; B2RZ55; -.
DR SMR; B2RZ55; -.
DR STRING; 10116.ENSRNOP00000051834; -.
DR PhosphoSitePlus; B2RZ55; -.
DR PaxDb; B2RZ55; -.
DR PeptideAtlas; B2RZ55; -.
DR PRIDE; B2RZ55; -.
DR Ensembl; ENSRNOT00000054951; ENSRNOP00000051834; ENSRNOG00000036683.
DR GeneID; 303745; -.
DR KEGG; rno:303745; -.
DR CTD; 51547; -.
DR RGD; 1305876; Sirt7.
DR eggNOG; KOG1905; Eukaryota.
DR GeneTree; ENSGT00940000159703; -.
DR HOGENOM; CLU_023643_6_2_1; -.
DR InParanoid; B2RZ55; -.
DR OMA; HFGERGI; -.
DR OrthoDB; 1459156at2759; -.
DR PhylomeDB; B2RZ55; -.
DR PRO; PR:B2RZ55; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000036683; Expressed in thymus and 20 other tissues.
DR Genevisible; B2RZ55; RN.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005731; C:nucleolus organizer region; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0097372; F:NAD-dependent histone deacetylase activity (H3-K18 specific); ISS:UniProtKB.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; ISS:UniProtKB.
DR GO; GO:0061697; F:protein-glutaryllysine deglutarylase activity; ISS:UniProtKB.
DR GO; GO:0106231; F:protein-propionyllysine depropionylase activity; ISS:UniProtKB.
DR GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:1990258; P:histone glutamine methylation; ISS:UniProtKB.
DR GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR GO; GO:0016570; P:histone modification; ISS:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0036049; P:peptidyl-lysine desuccinylation; ISS:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007072; P:positive regulation of transcription involved in exit from mitosis; ISO:RGD.
DR GO; GO:0006476; P:protein deacetylation; ISS:UniProtKB.
DR GO; GO:0061698; P:protein deglutarylation; ISS:UniProtKB.
DR GO; GO:0106230; P:protein depropionylation; ISS:UniProtKB.
DR GO; GO:0062176; P:R-loop disassembly; ISS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:1901836; P:regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0009303; P:rRNA transcription; ISO:RGD.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Cytoplasm; DNA damage; DNA repair;
KW Metal-binding; Methylation; NAD; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc.
FT CHAIN 1..402
FT /note="NAD-dependent protein deacetylase sirtuin-7"
FT /id="PRO_0000419985"
FT DOMAIN 91..332
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 108..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 168..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 298..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT MOD_RES 390
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NRC8"
FT MOD_RES 390
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NRC8"
SQ SEQUENCE 402 AA; 45113 MW; 7A1E79AF09204A84 CRC64;
MAAGGGLSRS ERKAAERVRR LREEQQRERL RQVSRILRKA AAERSAEEGR LLAESEDLVT
ELQGRSRRRE GLKRRQEEVC DDPEELRRKV RELAGAVRSA RHLVVYTGAG ISTAASIPDY
RGPNGVWTLL QKGRPVSAAD LSEAEPTLTH MSITQLHKHK LVQHVVSQNC DGLHLRSGLP
RTAISELHGN MYIEVCTSCI PNREYVRVFD VTERTALHRH LTGRTCHKCG TQLRDTIVHF
GERGTLGQPL NWEAATEAAS KADTILCLGS SLKVLKKYPR LWCMTKPPSR RPKLYIVNLQ
WTPKDDWAAL KLHGKCDDVM RLLMDELGLE IPVYNRWQDP IFSLATPLRA GEEGSHSRKS
LCRSREEPPP GDQSAPLASA TPILGGWFGR GCAKRAKRKK AA
