ID A0A2K6FXN9_PROCO Unreviewed; 1083 AA.
AC A0A2K6FXN9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN Name=SUPT5H {ECO:0000313|Ensembl:ENSPCOP00000018749.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000018749.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000018749.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036945}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000256|ARBA:ARBA00006956,
CC ECO:0000256|PIRNR:PIRNR036945}.
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DR AlphaFoldDB; A0A2K6FXN9; -.
DR Ensembl; ENSPCOT00000029393.1; ENSPCOP00000018749.1; ENSPCOG00000021231.1.
DR GeneTree; ENSGT00440000037640; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032784; P:regulation of DNA-templated transcription elongation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; NusG, N-terminal domain; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR041980; KOW_Spt5_6.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN-like_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; SUPPRESSOR OF TY 5; 1.
DR PANTHER; PTHR11125:SF7; TRANSCRIPTION ELONGATION FACTOR SPT5; 1.
DR Pfam; PF00467; KOW; 2.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 172..263
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 268..295
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 415..442
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 467..494
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 589..616
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 699..726
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 768..904
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT DOMAIN 1030..1057
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..958
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 120394 MW; 70D9D617F2C8E42A CRC64;
MSDSEDSNFS EEEDSERSSD GEEAEVEEEQ RSAAGSEKEE EPEEEEEEEE EEEYDEEEEE
EDDDRPPKKP RHGGFILDEA DVDDEYEDED QWEDGAEDIL EKASNIDNVV LDEDRSGARR
LQNLWRDQRE EELGEYYMKK YAKSSVGETV YGGSDELSDD ITQQQLLPGV KDPNLWTVKC
KIGEERATAI SLMRKFIAYQ FTDTPLQIKS VVAPEHVKGY IYVEAYKQTH VKQAIEGVGN
LRLGYWNQQM VPIKEMTDVL KVVKEVANLK PKSWVRLKRG IYKDDIAQVD YVEPSQNTIS
LKMIPRIDYD RIKARMSLKD WFAKRKKFKR PPQRLFDAEK IRSLGGDVAS DGDFLIFEGN
RYSRKGFLFK SFAMSAVITE GVKPTLSELE KFEDQPEGID LEVVTESTGK EREHNFQPGD
NVEVCEGELI NLQGKILSVD GNKITIMPKH EDLKDMLEFP AQELRKYFKM GDHVKVIAGR
FEGDTGLIVR VEENFVILFS DLTMHELKVL PRDLQLCSET ASGVDVGGQH EWGELVQLDP
QTVGVIVRLE RETFQVLNMH GKVVTVRHQA VTRKKDNRFA VALDSEQNNI HVKDIVKVID
GPHSGREGEI RHLYRSFAFL HCKKLVENGG MFVCKTRHLV LAGGSKPRDV TNSTMGGFSP
MSPRISSPMH PSAGGQCGGF GSPGGGGGGM SRGRGRRDNE LIGQTVRISQ GPYKGYIGVV
KDATESTARV ELHSTCQTIS VDRQRLTTVG SRRPGGMTST YGRTPMYGSQ TPMYGSGSRT
PMYGSQTPLQ DGSRTPHYGS QTPLHDGSRT PAQSGAWDPN NPNTPSRAEE EYEYAFDDEP
TPSPQAYGGT PNPQTPGYPD PSSPQVNPQY NPQTPGTPAM YNTDQFSPYA APSPQGSYQP
SPSPQSYHQV APSPAGYQNT HSPASYHPTP SPMAYQASPS PSPVGYSPMT PGAPSPGGYN
PHTPGSGIEQ NSSDWVTTDI QVKVRDTYLD TQVVGQTGVI RSVTGGMCSV YLKDSEKVVS
ISSEHLEPIT PTKNNKVKVI LGEDREATGV LLSIDGEDGI VRMDLDEQLK ILNLRFLGKL
LEA
//
