ID A0A3B4X3T3_SERLL Unreviewed; 1080 AA.
AC A0A3B4X3T3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000010307.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000010307.1}
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; A0A3B4X3T3; -.
DR Ensembl; ENSSLDT00000010682.1; ENSSLDP00000010307.1; ENSSLDG00000008112.1.
DR GeneTree; ENSGT00440000037640; -.
DR Proteomes; UP000261360; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 174..265
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 270..297
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 416..443
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 468..495
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 590..617
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 1028..1055
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..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 1080 AA; 119999 MW; 4F22DED59DD01C14 CRC64;
MSDSEDSDFS DNQSERSSDG EAEEVEENEE EANSPVGSDK VAEEEGEDLD DEEEYDEEEE
EDDDDRPRKK PRHGGFILDE ADVDDEYEDE EDQWEEGAED ILEKVSNMDH VVLDEDHSGS
RRLQNLWRDS REEALGEYYM RKYAKSSAGE HYSGGSEELS DDITQQQLLP GVKDPNLWTV
KCKIGEERAT AIALMRKFIA YQFTDTPLQI KSVVAPDHVK GYIYVESYKQ THVKAAIEGI
GNLRMGFWNQ QMVPIKEMTD VLKVVKEVTN LKPKSWVRLK RGLYKDDIAQ VDYVEPSQNT
ISLKMIPRID LDRIKAKMSL KDWFAKRKKF KRPAQRLFDA EKIRSLGGEV SHDGDFMIFE
GNRYSRKGFL FKSFAMSAVI TDGVKPTLSE LEKFEDQPEG IDLEVVTESG KEREHNLQAG
DNVEVCEGEL INLQGKILSV DGNKITIMPK HEDLKDPLEF PAHELRKYFR MGDHVKVIAG
RYEGDTGLIV RVEENFVILF SDLTMHELKV LPRDLQLCSE TASGVDAGGQ HEWGELVQLD
PQTVGVIVRL ERETFQVLNM HGKVLTVRHQ AVNRRKDNRF AVALDSEQNN IHVKDIVKVI
DGPHSGREGE IRHLFRGFAF LHCKKLVENG GMFVCKTRHL VLAGGSKPRD VTNFTVGGFA
PMSPRISSPM HHGGGGAQQR GGGGGGGGGM GRGRGRRDNE LIGQTVRISQ GPYKGYIGVV
KDATESTARV ELHSTCQTIS VDRQRLTTMG AKRHGGMTST HGRTPMYGPQ TPMYGTGSRT
PMYGSQTPLH DGSRTPHYGS QTPLHDGSRT PGQSGAWDPN NPNTPSRNEE EYDFGYDDEP
SPSPQGYGGT PNPQTPGYPE VPSPQVNPQY NPQTPGTPAM YNTEQYSPYA APSPQGSYQP
SPSPQSYHQV APSPVGYQNT HSPASYHPTP SPMAYQASPS PSPVGYSPMT PGAPSPGGYN
PHTPGSNIEQ GSSDWVTTDI LVRVKDSFMD LMGQTGVIRS ITGGMCSVFM QESEKVVSIS
SDHLEPVTPT KNNKVKVILG EDREATGILL SIDGDDGIVR MELDDQLKIL NLRFLGRLEH
//