ID K0RCM6_THAOC Unreviewed; 971 AA.
AC K0RCM6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU003985, ECO:0000256|RuleBase:RU364024};
DE Includes:
DE RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
DE Includes:
DE RecName: Full=General transcription factor IIH subunit 4 {ECO:0000256|RuleBase:RU364024};
GN ORFNames=THAOC_37249 {ECO:0000313|EMBL:EJK44232.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK44232.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK44232.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK44232.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
CC -!- FUNCTION: Component of the general transcription and DNA repair factor
CC IIH (TFIIH) core complex which is involved in general and
CC transcription-coupled nucleotide excision repair (NER) of damaged DNA.
CC {ECO:0000256|RuleBase:RU364024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000256|RuleBase:RU003985};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364024}.
CC -!- SIMILARITY: Belongs to the TFB2 family.
CC {ECO:0000256|RuleBase:RU364024}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC ECO:0000256|RuleBase:RU003985}.
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:EJK44232.1}.
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DR EMBL; AGNL01050001; EJK44232.1; -; Genomic_DNA.
DR AlphaFoldDB; K0RCM6; -.
DR EnsemblProtists; EJK44232; EJK44232; THAOC_37249.
DR eggNOG; KOG1252; Eukaryota.
DR eggNOG; KOG3471; Eukaryota.
DR Proteomes; UP000266841; Unassembled WGS sequence.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:InterPro.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.30.70.2610; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR005859; CysK.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR040662; Tfb2_C.
DR InterPro; IPR004598; TFIIH_p52/Tfb2.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01139; cysK; 1.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF253; CYSTEINE SYNTHASE 1; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF03849; Tfb2; 2.
DR Pfam; PF18307; Tfb2_C; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW ECO:0000256|RuleBase:RU003985}; DNA damage {ECO:0000256|RuleBase:RU364024};
KW DNA repair {ECO:0000256|RuleBase:RU364024};
KW Nucleus {ECO:0000256|RuleBase:RU364024};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW ECO:0000256|RuleBase:RU003985};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW Transcription {ECO:0000256|RuleBase:RU364024};
KW Transcription regulation {ECO:0000256|RuleBase:RU364024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 487..540
FT /note="Transcription factor Tfb2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18307"
FT DOMAIN 628..928
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 701
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 807..811
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 901
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 670
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 971 AA; 106229 MW; 4C848F3555E49262 CRC64;
MPPRKRKASS APAAKRKKTA TGQSAAPAEA EAEIVSDLIV DPQEILLSTS SSIFEYLERL
PPSTVRTIYA LPSPRGPTVA AAVVRSSCLT DMARQCTLRL VTCGGSFKVQ SIVEGWINRH
GRKDALIALR RMEAMGIIEP TLGLATRPGE AAELEEADDT AKREKMLAKD AVLTPEFNEA
MKLYLITSSS SPWPTVTNEQ IALYKKTGEQ EDGKPSRDPP SRRELEAHTQ SQWDSVLHFL
VGSDDSDRKG VNGIEEPNVA MVNFLTRIGL MQEDPDFTGK DRSRAPLVIT SKGYEFMLRD
TNAQVWQFVL QYLNSMAHHD LKDTIRKEAL SFLICLGSCR IGEGYFSSVL GSKSARVLMK
DFARFGLLFV CRVAGKTAFY PTRVAVNLVA SNEKGGSRQS DALLPSVAAT RSLEEAMNAP
DPTRSHLAVI SYKRLPNVVF FHLTRDSIKS AFRLGVTADQ ILRFLQVHAH PMMRSGNQPM
PPANVRDQIL LWDRERRRVV MDEVWVHQCR DDAEFSAVGM YASDSEALAW GNAHTNKLYL
QCDSGSFQME APPYDLSTYL TGLTGDHLEA KGEEGPRERK KHSDLDRDCD MLRSAATASV
RIFGSYKPQV SLHLQQTRSI VNVASRPSDL VGNTPLIDLQ KILKSRGVDV SNGVKLYGKL
ESLGPCSSVK DRLGRSMIDD AEAKGLLTPG ESVLVEPTSG NTGIALAFIA RERGYKCILT
MPETMSVERR MMLMSLGAEV VLTPKETAVP GALAKAKEIV AGLPEGKGII LQQFENEANV
RIHRETTGPE IWKDTDGLID IFVSGVGTGG TVSGVSQFIK PLKPDMKTVA VEPMEQMLIT
AAKGGEKIGE QGPHKIQGMG AGLVPAVLDL DIIDEVVPIH SDEAADMANE LWMIGLPVGI
SSGAIVAAAT KVCERDEAAG KMVVCVIPSF GERYFTHPMF SEIKNAAESL EKQPLPEPFD
NREYGFATER G
//
