ID A0A093HQJ2_TYTAL Unreviewed; 1702 AA.
AC A0A093HQJ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Transcription elongation factor spt6 {ECO:0000256|PIRNR:PIRNR036947};
GN ORFNames=N341_08992 {ECO:0000313|EMBL:KFV56853.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV56853.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV56853.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV56853.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription elongation factor that enhances transcription
CC elongation by RNA polymerase II (RNAPII).
CC {ECO:0000256|PIRNR:PIRNR036947}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036947}.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000256|ARBA:ARBA00009253,
CC ECO:0000256|PIRNR:PIRNR036947}.
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DR EMBL; KK395161; KFV56853.1; -; Genomic_DNA.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:UniProtKB-UniRule.
DR GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
DR CDD; cd00164; S1_like; 1.
DR CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.10.650; RuvA domain 2-like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 1.10.10.2740; Spt6, Death-like domain; 1.
DR Gene3D; 1.10.150.850; Spt6, helix-hairpin-helix domain; 1.
DR Gene3D; 1.10.3500.10; Tex N-terminal region-like; 1.
DR Gene3D; 3.30.420.140; YqgF/RNase H-like domain; 1.
DR InterPro; IPR041692; HHH_9.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028083; Spt6_acidic_N_dom.
DR InterPro; IPR042066; Spt6_death-like.
DR InterPro; IPR032706; Spt6_HHH.
DR InterPro; IPR028088; Spt6_HTH_DNA-bd_dom.
DR InterPro; IPR035420; Spt6_SH2.
DR InterPro; IPR035018; Spt6_SH2_C.
DR InterPro; IPR035019; Spt6_SH2_N.
DR InterPro; IPR028231; Spt6_YqgF.
DR InterPro; IPR023323; Tex-like_dom_sf.
DR InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR InterPro; IPR017072; TF_Spt6.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR PANTHER; PTHR10145; TRANSCRIPTION ELONGATION FACTOR SPT6; 1.
DR PANTHER; PTHR10145:SF6; TRANSCRIPTION ELONGATION FACTOR SPT6; 1.
DR Pfam; PF14635; HHH_7; 1.
DR Pfam; PF17674; HHH_9; 1.
DR Pfam; PF14641; HTH_44; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF14633; SH2_2; 1.
DR Pfam; PF14632; SPT6_acidic; 1.
DR Pfam; PF14639; YqgF; 1.
DR PIRSF; PIRSF036947; Spt6; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 2.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF158832; Tex N-terminal region-like; 1.
DR PROSITE; PS50126; S1; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:KFV56853.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW Protein biosynthesis {ECO:0000313|EMBL:KFV56853.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036947};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR036947}.
FT DOMAIN 1225..1280
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1323..1429
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1702 AA; 196485 MW; 921E63BF53B672E1 CRC64;
MSDFVESEAE ESEEEYNQDG EVVPRVTKKF VEEDEDDEEE EEINLDDQDE QGNLKGFIND
DDDEEEEEEA SDSGDSEDDV GHKKRKRTFD DRLEDDDFDL IEENLGVKVK RQKFRRVRKM
SDDEDDEEED YGKEEHEKEA IAEEIFQDGE GEEGGEAVEA PVAPPEEEEE EEEDESDIDD
FIVDDDGQPL KKPKWRKKLP GYTDAALQEA QEIFGVDFDY DEFEKYNEYD EEMEEEYEYE
DEEAEGETRV RPKKTAKKRV SRRSIFEMYE PSELESSHLT DQDNEIRMTD MPERFQLRSI
PVKSAEDDEL EEEADWIYRN AFATPTISLQ ESSDYLDRGQ ASSSFSRKGP STIQKIKEAL
NFMRNQHFEV PFIAFYRKEY VEPELHINDL WRVWQWDEKW TQLKIRKQNL TRLFEKMQAY
QYEQISADPD KPLADGIRAL DTTDMERLKD VQSMDELKDV YNHFLLYYGR DIPKMQNAAK
AARKKQKRIR EDGEEEEGEG EDAEDDEQKG PELKQASRRD MYTICQTAGL DGLAKKFGLT
PEQFGENLRD SYQRHETEQF PAEPLELAKD YVCSQFPSPE AVLEGARYMV ALQIAREPLV
RQVLRQTFQE RAKINISPTK KGKKDIDEAH YAYSFKYLKN KPVKELRDDQ FLKMSLAEDE
ALLTIDISID MKGVEGYGSD QTYFEEIKQF YYRDEFSHQV QEWNRQRTMA IERSLNQFLY
VQMAKELKNK LLVEAKEYVL KSCSRKLYNW LKVASYRPDQ QVEEDDDFMD ENQGKGIRVL
GIAFSSARDH PVFCALVNGE GEVTDFLRLP HFTKRRNAWR EEEREKKAQD IETLKKFLLN
KKPHVVTIAG ENRDAQMLME DVKRIVHELD QGQQLSSIGV ELVDNELAIL YMNSKKSENE
FRDYPPLLRQ AVSLARRIQD PLIEFAQVCS SDEDILCLKL HPLQEHVVKE ELLNALYCEF
INRVNEVGVD VNRAIAHPHS QALLQYVCGL GPRKGTHLLK ILKQNNTRLE NRTQLVTMCH
MGPKVFINCA GFIKIDTASL GDSTDSYIEV LDGSRVHPET YEWARKMAVD ALEYDESAED
ANPAGALEEI LENPERLKDL DLDAFAEELE RQGYGDKHIT LYDIRAELSC RYKDLRTPYR
SPNTEEVFNM LTKETPETFY IGKMVICNVT GIAHRRPQGE SYDQAIRNDE TGLWQCPFCQ
QDNFPELSEV WNHFDSGSCP GQAIGVKTRL DNGVAGFVPT KFLSDKVVKR PEERVKVGMT
VHCRIMKIDI EKFSADLTCR TSDLMDKNNE WKLPKDTYYD FDSEAADHKQ EEDLKRKQQR
TTYIKRVIAH PSFHNISFKQ AEKMMETMDQ GDVIIRPSSK GENHLTVTWK VNDGIYQHVD
VREEGKENAF SLGSTLWINT EEFEDLDEIV ARYVQPMASF ARDLLNHKYY QDCNSGDKKK
LEELLIKTKK EKPTFIPYFI SACKDLPGKF LLGYQPRGKP RIEYVTVTPE GFRYRGQGFP
TRWFKDHYQD PVPGITPSSS SRTRTPASIN ATPANINLAD LTRAVNALPQ NMTSQMFSAI
AAVTGQGGQN PNAPPAQWAS SQYGYGGSGG GSSAYHVFTT PAQQPVATPL MTPSYSYTTP
SQPITTPQYQ LQAHTTPQST PTNSHAAIDW GKMAEQWLQE KEAERRKQKQ RLTPRPSPSP
MIESTPMSIA GDATPLLDEM DR
//
