ID R1H2G0_BOTPV Unreviewed; 1082 AA.
AC R1H2G0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=UCRNP2_632 {ECO:0000313|EMBL:EOD52589.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD52589.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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 -!- SUBUNIT: Component of the SPT4-SPT5 complex. Interacts with RNA
CC polymerase II. {ECO:0000256|ARBA:ARBA00025870}.
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 EMBL; KB915716; EOD52589.1; -; Genomic_DNA.
DR RefSeq; XP_007579957.1; XM_007579895.1.
DR AlphaFoldDB; R1H2G0; -.
DR STRING; 1287680.R1H2G0; -.
DR KEGG; npa:UCRNP2_632; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_1_1; -.
DR OMA; PYPVGYM; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
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; 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; 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; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 2.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 4.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 212..303
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 307..335
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 468..495
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 521..549
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 740..767
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 834..947
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 116526 MW; 7A1CDF0BE856BBF5 CRC64;
MASIRDADLA GSESDDEPFN YEPPVGSDNE DDGRRDNDQN HDDDDEDEVR HSRPASKKPS
RHQSPDEDEG GAAEDDEEGD DDEEGGDEED DEEEEDEDEE EVVGHHRKRR KRDARLQFID
VEAEVDEEDE EELDEDDELP EETHPDDLLD MPAGAENDDR RHRELDRQRE LEASMDAEKQ
AAALKERYGR NRASAVHSDV LPQRLLLPSV DDPTIWGVKC KPGKEKEVVY DIMKRFEDRL
MTREPLELCS VFERGSVMSG YIYVEARKQA SALAACENIS FCYPRGKMVL VPLKEMPDLL
RVKKSKELSE GMYVRIKGGG LYAGDLAQVT EVEANGNEVT IRLIPRLDYG LNEDPNALPD
ANKRKRPGTL TSRPPPRLFS ETEAKKKHIK FLTQENSLAG HRIWIYKKDR YIDGFLEKTV
KLNQLQTENV NPRLEEVTRF AAGGEDGTEN LDLAALAATL KQASTGADYM PGDMVEIYHG
EQQGVSGKAI GVHNDIVTLK VQEGELKGQT VEAPVKSLRK LFKEGDHVKV VGGSKYHDEV
GMVIKVRAER VTLLTDSTNQ EITVFSRDLR VASDSGGMQG DSKYDLFELV QLDASTVACV
IKVDRESLRV LDQNGQVRTL LPSNISNRVD RRKNAVATDR DGSEIRTEDT VKEYGGEQRQ
GRVLHIHRSY LFVQNKNRAE NAGCFVVRSG NVTTVAAKSG KVSSAGPDLS KMNPLMQRQD
LRQGPNGPGT MAPPKTMGRD RMLGKTVIVR KGAYKGLLGI VKDTTDLEAR VELHTKNKTI
TIPKETLSIK DPITGATIGA GGGGGGRGRG MPSQGGFGGS TPGSRVPGGW GQPGSRTPMA
AQSGGRTPAW GGGASRTPAW QQNGSSTSYG GAGGRTPAWQ SGGSSRTPAW ANSNDGNRTS
YGGGDGGRTA YGGSTSYGGN TAYGGSTAYG GNESPLFVPM YQNRNSTWSA SSRTPYGAGS
SSWGSGANDG GRTPAWGGSG GRTPAYQPNA GGAKDSSSQP TPGSWAHPTP GAFDAPTPGF
SAPTPAAADQ PTPRFGGGGY GGYGGYGATP AAAPTPAQYP ETPGGYGPPE TPAAAGDDAG
YD
//
