ID A0A1G4BED8_9PEZI Unreviewed; 1054 AA.
AC A0A1G4BED8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Sir2 family protein {ECO:0000313|EMBL:OHE99738.1};
GN ORFNames=CORC01_04874 {ECO:0000313|EMBL:OHE99738.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE99738.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHE99738.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE99738.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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:OHE99738.1}.
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DR EMBL; MJBS01000033; OHE99738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4BED8; -.
DR STRING; 1209926.A0A1G4BED8; -.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000176998; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd06174; MFS; 1.
DR CDD; cd01408; SIRT1; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR23507:SF1; GH08173P; 1.
DR PANTHER; PTHR23507; ZGC:174356; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998};
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}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT TRANSMEM 39..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 560..820
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 690
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 698
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 701
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 725
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 1054 AA; 114748 MW; CC167B73C25288EF CRC64;
MAPTKTVDDR NGDIEGRPEE ETPLLSHDLP STVAPSKSYQ LRVIVLAVTF ILIVEVGAWL
QVPPAYQLME KIICHQRYPD HIISSEDDDI CKGPDVQGDL AMIRGWQNSF DCVPPLLTAI
PYGVVADKYG RRPVLSLAML GITLELLWML LPLLWPDVLP LWTMWFGAAF QFIGGGAGMI
QAMTWTMISD VVPVSNLIGA IALVGELVVA PLSAYLLSKN PWLPLTVGMA LLIIGTFLPP
FIPETLDLRR AADQEVEQTL QRSEEDARDK RTLREQIVFA VKNDMGHVYN FLIRSKSVIY
LVAGFNLTVI VKFVKVDIMS QYVHNLLGWS WAKATLLGTV STVTNIVMLL VVLPALSWLI
TKRTGVHPLV RDLWLTRMSG ILLAIGCFMV AIAFAPWFLI TALVVFSMGT VYTNICRAIL
NAVVEPHTIG TLNTAIAWVE QVSLLVSAPV ISALLKAGNS AGGLWLGLPY MAATLMAIGG
TAIAFISLPS FTPIPSARET ATHTALPDFF PSPPTNPANL PIIGRRRRDK HPKGRPNSNR
PRKKMGNEES TMLDDSVQPK TLESRSLDAL ADYIKSGDVK KIAVMTGAGI STAAGIPDFR
SPGTGLYANL ARLNLPYAEA VFDISYFRKH PEPFYYLAKE LYPGKFYPTV SHAFIALLAK
KGLLQMNFTQ NIDCLERRAG VPDDKIIEAH GSFATQRCIE CGDVFPADRM EKHVQDEHVP
KCDSCGGLVK PDIVFFGEAL PEAFRNNTHL PAMADLIIVM GTSLSVYPFA GLAEASRSGV
PRLLLNRERV GQMGRRADDV VELGTCDAGV RKLATLLGWG DELEALWRGI VGEKEAERQL
ASAAGEGADD LEEEIRRVTE GVDIALKLDD NEEEDAAAEP TKDSEEVGSP LRQDGGSDTE
DAQNSIPKGV VQRMSKAIQG QEEIGTDIKD DRGREGRTIN GSEGAPQDAK DFRVEAKRKI
QLAAQGAATP LDEVAVIFDS TAPVAKMKHE DPKSADLLSG VSRYEETSAP PASIEKESSS
GQAQPTPAST TAQEASKTVE KVKEDAPSSG DAKF
//
