ID A0A2A3EIS1_APICC Unreviewed; 1736 AA.
AC A0A2A3EIS1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Transcription elongation factor spt6 {ECO:0000256|PIRNR:PIRNR036947};
GN ORFNames=APICC_06058 {ECO:0000313|EMBL:PBC31089.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC31089.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC31089.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC31089.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-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; KZ288250; PBC31089.1; -; Genomic_DNA.
DR STRING; 94128.A0A2A3EIS1; -.
DR Proteomes; UP000242457; 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; 2.
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; SM00316; S1; 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; 2.
DR SUPFAM; SSF158832; Tex N-terminal region-like; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Elongation factor {ECO:0000313|EMBL:PBC31089.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW Protein biosynthesis {ECO:0000313|EMBL:PBC31089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242457};
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 1223..1278
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 466..496
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1736 AA; 200447 MW; A6E1625260A8E11A CRC64;
MADYLDAEAE ESEEEEELDV NERKKLKKLK AMQDSDDEDD DEEDEGEVPG LIDDNPIEDD
NDGEDSDGSD YSRKRKKSDD EDFDDRLEDE DYDLLEENLG VKVERKRRFK RLRRIQDEES
EGEEEREVDD ERDAIANELF QGSGEEDEER SEVSHRGEVE GFDEEESEDE DDFIVDGDGI
PIAEKRKKKK PIFSDAALQE AQDIFGIDFD YDEFGKYGED EFEDEEDEEE DDYIHDEIED
RPRRSKQHLK KKSTKKSIFE VYEPSELIRG HFTDIDNEIR TTDIPERMQL RAVPITSTIE
GSDELDLEAE WIYKQAFCQP TISIQDAHLN EEAKERARKG PQTVNKIKKA LDFMRNQNFE
VPFISFYRKE YVLPELNIND LWKIYKFDMK WCQLKQRKEN LLKLFEKMRN FQLDEIMKNP
DAPLSDNIRI IKDDDIERLK NIQTFEELND VYRHFMLYYN EDVSVMQEDI RKKEKEAQKK
AKLEKRKKQI EEAEENGEDF PEEIADVDDE EEEIDESLKK PIRKGPYYIC KKAGLDGLAK
RFGLSPEHFA ENLRDNYQRH EVDQDPTEPA IVANDFCSAI FNTNEEVLKA AQLMVAIQLA
HEPLVRKCVR EMYMERAKLS IKPTKKGIKE IDEAHAIYGL KYVKNKPVRD LVGDQFLKLI
IAEEDKLVTL SFSDIIEGNT SNNYIDEIKQ LYYRDEFSKS VQDWNTLRTG SVEIALNRII
IPQLKKELRS NLLVEAKECV MKACCRKMYN WIKIAPYTCE FPEEDDEEWN TSKGIRVMGV
AYVPDPSQAA FTCIISPDGE CTDYLRLPHI LKRKNSFRDN EKVLKEADLL AIKNFIATKK
PHVVIVSGET REALMIVADI KECISNLIEE EQYPSIKVEI CDNELAKVYA NSNRSISEFR
DYPELLRQAI SLARRIQDPL LEFSQLCTID EEILCLKYHS LQDQLSKEDL IENLYLEFIN
RINEVGVDLN RAVQQPYTAN LVQFVCGLGP RKGQALIKIL KQTNQRLENR TQLITACHMG
PKVFVNCAGF IKIDTNSLGD STEAYVEVLD GSRVHPETYE WARKMAVDAL EYDDEDANPA
GALEEILESP ERLKDLDLDA FAEELERQGF GNKCITLYDI RAELNCRYKD LRISYQSPNT
EKLFDILTKE TPETFYVGKL VLATVVGISH RKPQGEQLDQ ANPVRNDETG LWQCPFCLKN
DFPELSEVWN HFDAGACPGK ATGIRLRLDN GISGYIHVKN LSDKHVANPE ERVRVGQVIH
CRIIKIEVER FSVECTSKTS DLVDKNHEWR PQRDVYYDTE AEDKDIKTEE DTKKVQQRQT
YVKRVIIHPN FYNIGFAEVE KLMQTMKQGE AIIRPSSKGA DHLTVTWKVT DNIYQHIDIR
EEGKENTFSL GRSLWIGNEE FEDLDEIIAR HINPMSAYVS ELIDFKYYKS NIEGIKDKAE
EILKEQKKQN PGGIPYIVSA AKNYPGKFLL SYLPRTRCRH EYITVSPDGF RFRGQMFSRL
SDLFRWFKEH FRDPIPGQST PGTPHGAMTS RTPYNGTTPG VNGVNPDTIQ RVAQNMPHHM
LHSLSKVANH TPHHYPPYTP GAASVSNYGV YGSTPYTPSG QTPFMTPYHT PHHPQTPSHA
QGPFLQPIPP ANSHRTTRSH RSASNSSNAT NWSKAAEAWA RSKQSTSKEF STPKYDESTR
KTPRNQEIQN ERATPRNRTP SVRTPSYKSP RGTPFTNSSP RSMSLSGDGT PLYDES
//
