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Database: UniProt
Entry: A0A2T7PK21_POMCA
LinkDB: A0A2T7PK21_POMCA
Original site: A0A2T7PK21_POMCA 
ID   A0A2T7PK21_POMCA        Unreviewed;      1062 AA.
AC   A0A2T7PK21;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN   ORFNames=C0Q70_04987 {ECO:0000313|EMBL:PVD33727.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD33727.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD33727.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD33727.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD33727.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PVD33727.1}.
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DR   EMBL; PZQS01000003; PVD33727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PK21; -.
DR   STRING; 400727.A0A2T7PK21; -.
DR   EnsemblMetazoa; XM_025231482.1; XP_025087267.1; LOC112559962.
DR   OrthoDB; 24955at2759; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
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; cd06086; KOW_Spt5_6; 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; IPR041980; KOW_Spt5_6.
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; PF00467; KOW; 3.
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; 6.
DR   SMART; SM00738; NGN; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036945}.
FT   DOMAIN          179..270
FT                   /note="NusG-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00738"
FT   DOMAIN          275..302
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          423..450
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          475..502
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          597..624
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          706..733
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          769..917
FT                   /note="Spt5 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01104"
FT   DOMAIN          1011..1038
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..67
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..105
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..838
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1062 AA;  116433 MW;  B6D97672EBBE1543 CRC64;
     MSDSEDSPFS DAESEGGDQN ESKNDGSDAG QEGSDAEDKP GDDDNEVDEE GGDDDEDEED
     YDDEDEEEGI GRPKKKKRRG ALGFIIDEAD VDEEDEDDEE WEEGAEELID RKSTYEGPSA
     KEIESHQRLN QILESQDEDE IEAYYRQRYG DSTAMDRFGD GEEMSDEITQ QGRLPGVKDP
     NLWVVKCRMG EEKAVVVHLM RKMIAFQNTD EPLQIKSVVA KEGLKGYIYI EAYKQIHVKQ
     AIEGIGNLRV GCYNQQMVPI REMTDVLKVV KETANLKPKT WVRLKRGIFR DDLAQVDYVE
     PSQNVVHLKM IPRIDYTQPR GILRSSANQD QGKKRKRRPP QKLLDVDAVR SIGGEVSTDG
     DFVIFEGNRY NRKGFLFKSF AMSAIVSEGI KPTLVELEKF EEQPEGIDVE LAPEKASGEI
     VHNLAPGDVV EVAEGELINL QGKVIKVDGN KITFLPNHKD LKNPLEFPAN ELRKFFKMGD
     HVKVIRGRYE GDTGLIVRVE EKMIVLFSDL TMHELKVLPK DIQLCTDMAT GVDSLGQFQF
     GDLVQLDPQT VGVIVRLEKE NFQVLNMHNK VVSVKPQSIT RKKDTRHAVA LDSENNNIQV
     KDVVKVIDGP HSGRQGEIMH LYRSFAFLMS RMMTENGGYF VCRTRHLVLA GSSRQNLAAP
     MGGMAPMSPR LSSPAHPSSG GGGGGGGGGG AGSAGRGRGG MTRRDRELIG QTVRIKQGPF
     KGYIGIVKDA TEDTARVELH SSCKTISVDK SRLLTLTGPR AGTATSTYGG RTPVYGGQTP
     MYGSRTPMYG SQTPLHDGSR TPHYGGQTPL HDAGSRTPSG GNSAWDPSSA NTPSRNNDFD
     YPYEEASPTD YATTPNPATP GYQADAPSPV GPYTPQTPGS TYSPYHPTTT SPATFQANSP
     GYVGTPSPAG YQPSPSPGGY AGTPSPAGIG FSPMTPGAPF TPQTPGTAMD HNLSDWHTTD
     ILVKVKETHD DPDLIYQTGV IRSISGGMCS VYIMENDKVV NIACEHLEPV APTKHEKAKV
     ILGDERETVG TVLSIDGCDA VFKIDEKNIR MLPVKHLCRM QS
//
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