ID A0A5N6TF01_9EURO Unreviewed; 918 AA.
AC A0A5N6TF01;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=adenosylmethionine decarboxylase {ECO:0000256|ARBA:ARBA00012357};
DE EC=4.1.1.50 {ECO:0000256|ARBA:ARBA00012357};
GN ORFNames=BDV25DRAFT_134339 {ECO:0000313|EMBL:KAE8144820.1};
OS Aspergillus avenaceus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=36643 {ECO:0000313|EMBL:KAE8144820.1, ECO:0000313|Proteomes:UP000325780};
RN [1] {ECO:0000313|EMBL:KAE8144820.1, ECO:0000313|Proteomes:UP000325780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 18842 {ECO:0000313|EMBL:KAE8144820.1,
RC ECO:0000313|Proteomes:UP000325780};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|ARBA:ARBA00001928};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1. {ECO:0000256|ARBA:ARBA00004911}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TAF6 family.
CC {ECO:0000256|ARBA:ARBA00007688}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
CC {ECO:0000256|ARBA:ARBA00008466}.
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DR EMBL; ML742430; KAE8144820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6TF01; -.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000325780; Unassembled WGS sequence.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:InterPro.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd08050; TAF6C; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR Gene3D; 1.25.40.770; TAF6, C-terminal HEAT repeat domain; 1.
DR InterPro; IPR048283; AdoMetDC-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001985; S-AdoMet_decarboxylase_euk.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR InterPro; IPR037796; TAF6.
DR InterPro; IPR011442; TAF6_C.
DR InterPro; IPR046344; TAF6_C_sf.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR NCBIfam; TIGR00535; SAM_DCase; 1.
DR PANTHER; PTHR10221; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 6; 1.
DR PANTHER; PTHR10221:SF9; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 6; 1.
DR Pfam; PF01536; SAM_decarbox; 1.
DR Pfam; PF02969; TAF; 1.
DR Pfam; PF07571; TAF6_C; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
DR PROSITE; PS01336; ADOMETDC; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Reference proteome {ECO:0000313|Proteomes:UP000325780};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 3..66
FT /note="TATA box binding protein associated factor (TAF)
FT histone-like fold"
FT /evidence="ECO:0000259|SMART:SM00803"
SQ SEQUENCE 918 AA; 101938 MW; 6124C31DC538CB37 CRC64;
MSVWNPDNIR DVAESVGIVN LNNDVTENLA RDVEYRIAQV LEEALKFMRH SRRTLLTTQD
VAQALRVLDV EPLYGYESSR PLRFGEASLG PGQPLFYVED EEVDFEKLIN APLPKVPREI
SFTAHWLAVE GVQPSIPQNP TAADSRNLEL MSKGPNANST LAAMSGSGNV AVKPLVKHVL
SKELQLYFEK VCSAFLDESS EEYRTSAYSS LREDPGLHQL VPYFVQFISE KVTHGLKDIF
VLTQVMHMSE ALVQNKSLYV DPYVASLVPP ILTCLIGRQL GGNADLSEQF ALREIAASLL
GLIAKKYSHS SHTLKPRLAR SCLKTFLDPS KPFGAHFGAI IGLQAVGGAE AVRVLVVPNL
PTYGTLLKDG LAEENPRRPE AEKVLTVLMG VLGTLRENQM SLANGHQGTM TDELRSRLSG
KVGEFLAAKI NEAGGIEMAH AILEQAISSS ARPDTLIGIG IFQYEGPEKL LEVWFAPSAD
NLGSSQPTGL KAVPEEIWKD MLDLVNCQVL SIVSSEDVDA YLLSESSMFV WPHKLILKTC
GTTTLLSGLP RILEIAALFA GFPKSPRPSG GVGIAAAPYR VFYSRKNFLF PDRQRGPHRS
WRDEVRTMDR LFLNGSAYMI GKMNGEHWYL YLTEPNTLLT PPASPKGDEE VTETKFLQIP
NGSLPKGIES NDETLEVLMT DLDEENAKQF YLEHATSIAE RRYRNFDKDN GDHVDVFSNN
SDMDLEDTDG TRILPPELTT EGHALGTVVS ESCGLSDVYP KDKFPDSRID AYLFTPCGFS
ANGVIPTPDP KANTHYFTVH VTPEPHCSYA SFETDVPHSQ NGQTTVDIVQ QVVNIFKPGR
FTVTLFENKP SEAEVGAVGE MKYIERQAVR RTDKMEHLEG YRRVDRIVHD LDGYDLVFRY
YERLDWKGGA PRLGEERV
//
