ID A0A421JA61_9ASCO Unreviewed; 2459 AA.
AC A0A421JA61;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Transcriptional activator SPT7 {ECO:0000313|EMBL:RLV85663.1};
GN ORFNames=JA9_001711 {ECO:0000313|EMBL:RLV85663.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV85663.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV85663.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV85663.1,
RC ECO:0000313|Proteomes:UP000286412};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:RLV85663.1}.
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DR EMBL; NSDU01000013; RLV85663.1; -; Genomic_DNA.
DR STRING; 2028340.A0A421JA61; -.
DR Proteomes; UP000286412; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR CDD; cd05510; Bromo_SPT7_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR037782; Spt7.
DR PANTHER; PTHR47343; TRANSCRIPTIONAL ACTIVATOR SPT7; 1.
DR PANTHER; PTHR47343:SF1; TRANSCRIPTIONAL ACTIVATOR SPT7; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50097; BTB; 2.
DR PROSITE; PS50012; RCC1_3; 2.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000286412}.
FT DOMAIN 356..426
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REPEAT 1209..1275
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1341..1404
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 1770..1847
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT DOMAIN 1905..1963
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 132..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2142..2459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 838..865
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 146..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2190..2208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2213..2271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2299..2402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2459 AA; 278599 MW; DB599624C98EE2FD CRC64;
MEKLASFQNN DPAVLLQLTK QLIERDFFST FLNHSQLKVL TRIVKSNDLD VWKHFLEGKI
AIEVEGTAEA EADADLGDFD DEFVTQLVMK VRYLLWEKAI DFYYSSESML NKGLEEVTDD
FELIDGLKMD EKVAEESSKD EEEPGVPVRE EEDDYDDDEE EDDEKQEDST KAQKEDEDVE
MTHTNYSNDK AVIKVPAEEL AEDTKKDEEN SVAEVPSDLI KELNKAYHTF EYDRETLSKR
RKLEKSNQQL DSDSQNEEAI KKENEGPSTD ENGVSATQTA SEPNLGPATF GVGSTSLRNL
LNTIQSHRDQ IPLDEHELRM LFMDVRKNRS KWANDERVGQ EELYEACERV VLDLRGYTEH
STPFLNKVSK REAPNYGLII KKPMDLNTVM KKLKSFSYNS KAEFVDDLML IWNNCLTYNA
DPKHFLRAHA IAMQKRTQKL IPTIPDITIK HRSEIEKEED DRDASVDPEG SSGAGAGKGL
QRHTIKEEAE ASVAEETPEV ETVEDSEHVD EVRETNDTQP SQTAPQAETD PAPVPDNAEN
NADTSRQMDG NESDSDIEVD NNENQNEGDQ DWRLLTAKSR ANYCSERAAL FDSENHLRLD
APAILRKSNE MDNFSHYLGN ESVSKSNSLL DNEEPYILEY DVAGGLPGIK YRGVSTEDQD
KYEQELVDKF LEVAEADANS IKSAFALSQD SGLNKVYTET ITEIQEVRKI CSKISLVRQM
QTQSFVHHSQ MKQPEIETIK EIDIDPISKL SNHDPFHESI QYPVLRRNIA KIAMQTGFET
TQPFAINTLT QVAARYMSNL IKTVKTHCES VSSNHLSNAE VILVSLVENG VNKPDDLYTF
VKERVLKQQA KLKDLRQKLS NFLRDLLRPG LENFTERSFE DNSEQFITGD FSSDLGDDFF
GFKELGLDKE FKMLSSSIPV YLLHSRLHNS YSSAGNELKR NKYSDLEDLP PIKLAASDIN
DQIELIKPFY QQLVEKTKSH YVKSQKKKGE STDLPPDEEL YIIEDEELPQ KQRNVRPRLP
PTGKISSAKK KPLSAGYFLP ELPKHDLVKR DVFGRTILHI LLLCNRHDLL RHLLKNNDVK
DVLVLSDYEN GWNCLHYAIF HKRILCFKVL MEYLRRETGS YMAPNSLMYD LVRCKDRNKY
TPFQLLDNDI KDLIWIPGYI DDNDRFHLTY RYVIQSEYAT DSPVIQQFRL RKSNIDFNHI
WWDDYRGGSD LYMSGSNKNY TLGLGDTSEV TNPSRVPFEQ FDISQRGTTI RDRLHRPRFK
QVGISKNHSL VLTTDLRLYS SGIGTRRGRS DHGSDNHKNS YRFNPIVIDD LETSPLANSS
ITGIVKFAIS DTHSLVLASN NCVYAFGSNI FGQLGASSTM RGLNTSNEDY EPTPVPVVGD
LKRNSDPIFG VAVSEVSSVA WSENGLFFWG LNTGQMGIPH DPTKKTVKGT FSGSIQHSPT
RVSLRDTIKL VQATPLCTFV VTTDNNIHVF TQYQHFKLPR LPVNIASEKH FDIFTPTKLT
KQPNIIKLCA KSHRLVCLVL DNGDVMSFTI DPTNSNMLKN IKYSTLWKSY DRDMKVVDLD
VSSDGSVILC TRNGSTFIKS SQNIQRRGSV NDVRLPIPVK KNKFRKVFNI NRVIKVSCDS
NFTSFAYMRD DIDVLPFELP KNSVLNDLEY LSPVIDATET RKQAELLRAD HTEDSWSNHY
YAHFLGVSAF INDHGAPIGD CEDISLPDSD ILQSRYHKRY SPFHKYGTHS DNMEEALDQS
KAQEHLHKSL LSNLDNDQWL PSSIAKSNHS DFSIKLSKGS CQHSIPIHRH LFRLRSPIFR
SFIDGDIVAE GNITGQYNEE ERSLTFKSSL QLKSLLIFIH YLYTGKIVSI WDSFPIRTDC
PPVVLAIKKD FFSLIGAFQM TNLNESKAIV QLRSLTESAT VSDDSDLITI VLSDGTAVCH
PSLLSSRSAY FETVLSDSWN GSKSLSLEGM TKRHFDVIMR HIYGVSDLNL FDEFVSETTH
LHEDFINFVM EIIEIADELL LLELKAIAQL AIKDLIDLQN ALTLLKFAES SNAKKLFMAC
SWYIYNNLEM FLLDNSFQDL TLDVSSKLEK HILFFHHCKV ADFANAKKEI NPALEYNWMQ
ENSGQFVKDF VYSMAEAHDS KFMKAGRTSF TPLVDEKYLP KVKASDKRRS SRKSTSARKN
SALLELQEEM AKLRRSSDTK SQGNGAKYSE SAIEEDDSDF EPVSRRRQKS SSRMKPVSPS
SVSPTDSPSV SAVQSLNSSS TSLSQSAARN TGAKLTSPKP STSQSKPKTS AGPPVPTAFD
SQPVLGQPIL GRPVLGGKSE NAQDTSTKKG TSVKFKFGQR PSQKERRMQY QVGTSSVTSA
NPEETRSVSG PWKSEATSPA AQPGKNSSLE TLPILGSSSW SSDPPTSNGR TPSLTSIMLQ
ESSRIEEAKA STEKRSLQDI QQEQMFEKWW QEEAERIQRQ QNPPPQHGKP RRKKNQSKK
//
