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Database: UniProt
Entry: A0A068S627_9FUNG
LinkDB: A0A068S627_9FUNG
Original site: A0A068S627_9FUNG 
ID   A0A068S627_9FUNG        Unreviewed;      1099 AA.
AC   A0A068S627;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 34.
DE   RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN   ORFNames=LCOR_08365.1 {ECO:0000313|EMBL:CDH57425.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH57425.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH57425.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The SPT4-SPT5 complex mediates both activation and inhibition
CC       of transcription elongation, and plays a role in pre-mRNA processing.
CC       This complex seems to be important for the stability of the RNA
CC       polymerase II elongation machinery on the chromatin template but not
CC       for the inherent ability of this machinery to translocate down the
CC       gene. {ECO:0000256|ARBA:ARBA00024691, ECO:0000256|PIRNR:PIRNR036945}.
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}.
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:CDH57425.1}.
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DR   EMBL; CBTN010000046; CDH57425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068S627; -.
DR   STRING; 1263082.A0A068S627; -.
DR   VEuPathDB; FungiDB:LCOR_08365.1; -.
DR   OrthoDB; 24955at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; cd06083; KOW_Spt5_3; 1.
DR   CDD; cd06085; KOW_Spt5_5; 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; IPR041976; KOW_Spt5_3.
DR   InterPro; IPR041978; KOW_Spt5_5.
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; PF12815; CTD; 1.
DR   Pfam; PF00467; KOW; 1.
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; 5.
DR   SMART; SM00738; NGN; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:CDH57425.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW   Protein biosynthesis {ECO:0000313|EMBL:CDH57425.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036945}.
FT   DOMAIN          145..235
FT                   /note="NusG-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00738"
FT   DOMAIN          239..266
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          391..418
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          443..470
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          663..690
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          758..952
FT                   /note="Spt5 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01104"
FT   DOMAIN          1038..1065
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          285..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..35
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..84
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1099 AA;  120228 MW;  6DD2FD53CDDA7ECD CRC64;
     MKRQDEYEDD VPFDEEDEDE DFEDEEDEDE EEEAVCINGE RPRKRAANPF IDEMALVDED
     EEEEEEEEEY GREDGFIDEE PEEIPSEAAM QRRHLDLDRR RREMEGMDDE QVAAFYAQKY
     GGRRAQAFKS SEEIPQQLLL PSVTDPNLWV VKCKPGKERD IVLGIMKRYF DRQYSDQPLE
     TFSAFARESL KGYIYIEARR LAHVQQAIAN IPNIFQTTLQ LVPIKDMVDS INIPKKETDI
     PVGGWVRVKR GVYTGDLGKV LEVSDSQDTA VIKLIPRLAL EPQEEEIERK RKKGSSATRP
     PPRFFNPERL SKRHIASLQK KGPYWVLGTD SFRDGYLEKN MKVSSLQIED VSPSLEEITR
     FIGDSGGDGD RALDLSAASL QSVNDAQATS LLQTGDTVEV IEGDMIHSVG TIDNVSDSSV
     VVSLNFGGYA KQVTLPAKQV RKKFNAGDHV KVIHGQRKDE SGMIVKVDGN VVTMLSDISM
     DEVQVFAKDL REAADVTLGK TVMGNYELHD LVQIDFHTVG VIIKVNKNSV KVLTQNGDVR
     TLEPHLITSK LDSKRAIATD ANGNSITAGA TVMEARGERR TCTILHVYRH LVFLHSRENM
     VDYGVWISPT RSVISVAAKE RPNISQQKRT QQPNGPNFRG GFDGRGRGRG GRGGFFGGRG
     GRDHLVSKTV RITQGPHKGY IGIVKDSTDT MARVELHTNC KVVNVDKTKL VLVDGNGGTL
     GPVVSDTRGA SDFAAPRPMA TPKRYGDGAM TPRHYSDGSR TPRHLASGAQ TPAWGMNNRT
     PNPYSSDNSR SSAWDAGAKT PNPYASSSYA DGSKTPAWDS GSKTPSWKAE TPRWSSSGGR
     TPGYNDYGNK SPTWSSRYDD RETAPTPAPH TLAPSTPAAS SNNVAPSPAP YPQTPGANYP
     QTPYDSAPTP YDGAPTPGVN LAPATPAAVN APTPAAHMLS APTPGGYIPS TPAGTVQPQT
     PFVPAGGDYG TVDDQNEDSD DWPIEDIEVK LTSSHGSGQK GQLASIISVD HNGRTCTVRM
     NEGGAQEHIP FTKMEPVRPS KRDPVKVLLG QHRGGIGALI GVDGQDGILR LRGQGPAFKF
     VSINAVGKYT GDEALDGNH
//
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