ID A0A4Y0BDM2_ANOFN Unreviewed; 2084 AA.
AC A0A4Y0BDM2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Regulatory protein SIR2 homolog 7 {ECO:0000256|ARBA:ARBA00043038};
DE AltName: Full=SIR2-like protein 7 {ECO:0000256|ARBA:ARBA00041832};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN018965-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN018965-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN018965-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000256|ARBA:ARBA00038170}.
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DR STRING; 62324.A0A4Y0BDM2; -.
DR EnsemblMetazoa; AFUN018965-RA; AFUN018965-PA; AFUN018965.
DR VEuPathDB; VectorBase:AFUN018965; -.
DR VEuPathDB; VectorBase:AFUN2_002843; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
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 CDD; cd01410; SIRT7; 1.
DR Gene3D; 2.20.28.200; -; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF1; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-7; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 90..337
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 369..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1486..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2010..2030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2065..2084
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 2084 AA; 231419 MW; D23F422F7F7572DB CRC64;
MRMKGITLSA ILEQGATRRR KSPPKEECPK KQKRDCWRKI ATVLNKCESK RTLEEQRLLE
SQPEVVKQIL ERRKRNVEYK ERVLETEDDP DVIERKALKL AQAIAKANHL IVYTGAGIST
SAKIPDYRGS QGIWTLLEQG KDIGEYDLSL ADPTFTHMAL FELHRRGILK HVLSQNCDGL
HLRSGLPRYS LSEVHGNMYV EVCKQCKPNA EYWRLFDTTQ FTARHYHKTN RRCRRCGGPL
IDTIVHFGER GQLKWPLNWA GVTPHTEKTD LILCIGSSLK VLRKYTWLWA TDRPIKKRPK
IFIINLQWTP KDKVSTLKIN GKCDQVMKLV MKHLDIDVPL YNRVKDPIFA HATLLLADEQ
HTASQPMLKK ATATKEEAAE EAKSNEREKE VKLEPNASAS TVVSPQQIYL NNLLFAQQQQ
ISTNYNHLLN AAGRSETRSS LLPACSLPPL VPYSMASGDA DQIKKEPVTP SLGNELKPLS
SPPVNVIKID TASNLFGNLR QVLNTMNSVQ VPVPLLLQPG VTLVQQSFVA NNASEKNKPS
PETQKKPPLC NKIQLIVKPV VVTNPPSLVP INLHRPEDVK PIPNELANQG SSSAVNNALK
MESTDEPSAV RKSVPKELWQ DEDIGDVDRL NIKSEITSNE PSGSVDMKEQ SVPMELKLEK
IEEKEEVVPA ELAEDITTIT AQNSIDMDTW AEKNKNTRVL LDMEQLNPIA DYTADTNGNT
LNGPEKMLNN PPCPDRDKVN TDDIECISIH SSSSECDAAQ REIDFETDIA WHTVGTANPS
KMVTTQSKGV SEHTNDKLNI EQRTIEDEEN YEKCQIEKMV QQDLLSIAQA IEMEQSLNTP
YDCSTIVPID REEIQNEYDK SITGTAPKDL EKCVPDAVQN RMALDISTIG ENNSTLELST
VSSPKRDQHD QAKDILHRLK ANGESSPKDG SIEDTSTNDV ISGVEVKVNN QESTHAISNR
LLEKHSIHDL NEILSDMKLL PEPMESNGKD TITSAECTAL NVKEQNNDVR HESHQIINEE
TTDLISNSTT DADHLSPFEA SPPVLNPLIA VSNNLEFCNQ DGSADSEIQA SVSYRQGSFD
ATKPATTMEQ VLSKIAIDLG SEESWRKYDT YDDDQLYSTS KDAIISEQLK SLEETNLQTP
LSEAVVQNED KQTDGASLAH NSNSIQMNGD IEKTNETSNG ESEDVKQQQR LSDRPTEKDH
PRNESCYQHQ TENGREDSNM HNQIDSLKQF EFPTSNAKSE ELMIAESHKT NHHDEVNSFV
PIVCAGRSSI ETFSTLDDGG TFKDTSSAYS LSETNNDHED KQHAKPEAAL QKMENQEHES
NSSSTIKTND GSTVNERCTE EELPLQRPKA DTDAEPIVQD ECAAKHIQKS SNQHKADEQL
HMVLSKTAEK ESSVSMDFNT NGQQSKENCL QAKKDDQKCL DTSLNCEKAP PIHKSTHHQN
MVKVVLSNSA LIELYEAAPR FADNYPPALK LLAPVKYSLP STHVAGKMSK PVDQQTSEHV
TRNDKTDEVN VNLEQQDSTP TSSGLNTLDH STTMLRSSPV PLCKKIQMPS ALLLAPPMHC
IGSALKVAPP NGAGNSIPPV SSVGTISPSF IPLQGGLTTN ASVAAYMLKN NSIISTNARF
PQGILGFPAG LGTNLVLLTS PPKHQVMTPS SNPTSVPTSP TATTPTTPAK SFRLESDEQT
DEEDGNSIKK RRSKRLESAR LHKQLATPEK TDSDTDTTID QWSPQERRRN NRASRSFDGA
HESDEMGDSS CGAGRSRSFR IRRKPEFLNI KHPEKKKKRT NDEPSLETAT CSKASTSGGY
QVKVANNSEL VTMTTMATLP TANRLFTISA PVAYFPTPFV STLGTSSDAI ISQQEKYKRI
LTYYKTAIQQ HQQSSTSNAL PQWYDVNYAY SGLHSIIHPP PPDVNLWGGS SIKLEPQQPL
EIECKFCFEN YSQYNCQFYP PQPAEFVVKA FRRGKVVVCE CCDFSDGEAE KTQPEMVAET
ASIATTSKAC GSGEVNSSSS IVSNEELQDQ TRRPLAEDHE PKEAEAATMS KRPKCESNSI
ANGSSSTVNA NGTNGAAHRP KVKPGWYGKG YRKHLRRKKR TSQG
//
