ID K9F4W2_PEND1 Unreviewed; 1026 AA.
AC K9F4W2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 08-NOV-2023, entry version 42.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=PDIP_88380 {ECO:0000313|EMBL:EKV04330.1};
OS Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV04330.1, ECO:0000313|Proteomes:UP000009886};
RN [1] {ECO:0000313|Proteomes:UP000009886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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}.
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:EKV04330.1}.
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DR EMBL; AKCU01000543; EKV04330.1; -; Genomic_DNA.
DR RefSeq; XP_014530509.1; XM_014675023.1.
DR AlphaFoldDB; K9F4W2; -.
DR GeneID; 26237152; -.
DR KEGG; pdp:PDIP_88380; -.
DR HOGENOM; CLU_003537_1_1_1; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000009886; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006354; P:DNA-templated transcription elongation; IEA:InterPro.
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 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; 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; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 5.
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 Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 300..327
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 460..487
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 513..541
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 636..661
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 725..752
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 833..977
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 111511 MW; 14CAC3738A855722 CRC64;
MSNFLNHDFG SEDEEDDFNP APQEDSDIEE PRAKPSKKQH LSGDGANEED VKYSRNTHAF
EEEDAKDIED DEEENELDDD DEEEEEEDEE EDVARPQKRM KRVANPFIED EAGVDDEEDE
GDDEEDELAE YGMETHPDDL DALPQGTETD DRRHRQLDRQ REIDASMDAE KQAQMLKERY
GRNRAAATDS LVIPKRLLLP SVEDPSIWGG RCKPGKEKEV VYSIQKRIEE RPAGSRNPIR
IISAFERGNI MQGWFYCEAR RQADVIEGLD AINFYYPSQK LTLVPVKEMP DLLRVQKSEE
LLPGGWIRIK RGKYIGDLAQ IEEVETNGLN VTVRLVPRLD YGMNDDAFGA PAPDAKRKRG
AVSTVRPPQR LFSETEAKKK HAKYLSSTSG LGGKSWNYLN DNYVDGFLIK DMRVQHLNAK
NVNPRLEEVT MFARGGEDGT ANLDLASLAE TLKNSTAEDS YQPGDPVEVY RGEQQGLIGR
TVSTRGDIVS LQVTEGELAG QTIDAPVRTL RKRFREGDHV KVIGGSRYQN ELGMVVQVKD
DTVTLLSDMS MQEITIFSKD LRLSAEMAAD GQLGIYDVHD LVQLDAATVA CVIKVDRESL
RVVDQNGSIR NILPTQIANK ITPRRDAVAT DRNGAEIRSG DTVREVYGEQ RSGVIRHIHR
SFLFLHNKAQ AENAGIAVVR TTNVVTVSAR GGRPTGPDLT KMNPALAMRT PGGGAAMPPP
RRGRDQLIGK TVTIRKGRYK GLVGIVRDAD DSSAQVELYT SNKPVHIPRD ILTPKDPVSK
QPLSMGRGRG GGGPGGRTPH TSSGGPRRDS WAGGRTPIAA ADSSRTPAWN GAAARTPAWG
GVSGSRTPAW KNDGSRTANP YDGNRTAYGG VGSRTPSWTS GSKTPYDSSS GFDAFASGSR
TPGWNAGGAN TGGRTPGWNS MSASRDQREF DDAPTPGGNY SAPTPGAYAA PTPGAPTPGG
WPESAPTPGG AFSAPTPGGP SKRDYDAPTP AAFDAPTPTM GGMAATPGAG YGGNDGGPRY
DDSPSP
//
