ID A0A915LG62_MELJA Unreviewed; 1308 AA.
AC A0A915LG62;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181};
DE AltName: Full=DRB sensitivity-inducing factor large subunit {ECO:0000256|ARBA:ARBA00029645};
DE AltName: Full=Transcription elongation factor spt5 {ECO:0000256|ARBA:ARBA00021370};
OS Meloidogyne javanica (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne; Meloidogyne incognita group.
OX NCBI_TaxID=6303 {ECO:0000313|Proteomes:UP000887561, ECO:0000313|WBParaSite:scaffold11669_cov179.g15796};
RN [1] {ECO:0000313|WBParaSite:scaffold11669_cov179.g15796}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SPT5 family.
CC {ECO:0000256|ARBA:ARBA00006956}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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DR WBParaSite; scaffold11669_cov179.g15796; scaffold11669_cov179.g15796; scaffold11669_cov179.g15796.
DR Proteomes; UP000887561; Unplaced.
DR GO; GO:0032044; C:DSIF complex; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
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 FunFam; 2.30.30.30:FF:000013; Transcription elongation factor SPT5; 1.
DR FunFam; 2.30.30.30:FF:000016; Transcription elongation factor SPT5; 1.
DR FunFam; 3.30.70.940:FF:000005; Transcription elongation factor SPT5; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
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; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
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; 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; PF23042; KOW1_SPT5; 1.
DR Pfam; PF23284; KOW2_Spt5; 1.
DR Pfam; PF23291; KOW4_SPT5; 1.
DR Pfam; PF23290; KOW5_SPT5; 1.
DR Pfam; PF23288; KOW6_SPT5; 1.
DR Pfam; PF23037; KOWx_SPT5; 1.
DR Pfam; PF00153; Mito_carr; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 2.
DR PROSITE; PS50920; SOLCAR; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000887561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}.
FT DOMAIN 112..201
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 206..233
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 351..378
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 403..430
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 525..559
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 702..729
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 765..905
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT DOMAIN 949..976
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REPEAT 1189..1278
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..859
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1308 AA; 144902 MW; 3F333FFB7B1F0B42 CRC64;
MSSDENESVH SDADLNEEPV NSDDNLSGGE EDTTQDTIDD QEEDNNFEKE RSLKRKANEA
GHREGLSDMT EEEMERYFQE RHAAQVATHQ GELDEDAYDD ITQNGLLPST KDPNLWIVRC
RLGEEKNTCL QLMRKFLAFQ NTEEPLQIKS VVVKEGLKGM IYIEAFKKAH VAKAIEGISA
LNQFQITMVP IKEMADTLRV VKDTPTLKPG SYVRLTRGIY KDDLAQVDLV DVAQNRVHLK
LVPRIDYTRL RGALKNQEEN RPLRNKRRPL PAPFDLDRIK AIGGEVTNDG DFYIFESSHY
RRGFLYKAFP MNSIIVDGVR PSLTELEHFQ DSAEDLKKEL ESTHLREKKH NFSPGDNVEV
TDGELANLRG KIQSIDGDKV VILPEHEDLN EPLTLNAYEL KKYFKAGDHV RVIGGRYEGD
TGLIVRVEDK MVILLSDLTM SEMKILPKDV QLCAEIATGV ERMGQYQYQD LVMLDKETVG
VIVRLEREHV EVLNMHGKVV RINPQTIDCK RESRFMKALD SQKNTIQVGD MVKVVDGPFA
PRKESDEEKQ GELKHLYRNW AFVYSRKHSI NGGIFVCKAK QLQLIGGAKA LDSMPASAMD
TADLLKSPHP LESPRPVSGG GSVRGGDQGG GFNRGFRFVV IHPPKAVEMS NKGNDVELPL
FDISTSFGGL IFQCLANSHS GGSVATGSIF TGAGRQTVRR NMQIIGKTVR VRSGPMKGYI
GIVKDATDST VKVELHTMPK TVNFNIDKVM EVGGDVPSGV MDVGGAATPG AAGAFGRTPM
YGGAQTPMYG GAATPMHDSY GSRTPHYGSS TPAYDGSRTP RQSSASWDPT VSNTPAHSSA
HFDDDEFGTS GFGTGGFGGA ATPAGSSGGG NRFGANTPMG MTPRNDTFNE YASSQTSSPH
PSRTPVGASP AGPQEIPDHE LKSGSWCGVE MCVNVRRTFS DESFFGLEGA IRTVKARVVY
GNHKGTEGTM ISVEGDEGVM QSTGGVRLFP LPILYFQLIK MAANLALKTS TENSYFYLFK
SPTIIMPPVG IMRRLVYSPS SRLFYKQVYE KNFTREKFFN GAIMATRLAA LNLREHKWDK
FQEISTKTLT NYLINRLPQI KEEDLYQNLN FTQNQICHMD ENVKETQFTL VNQFRWLLAG
AAAGLAVDLS LYPLDTIKVA LGSAPGSALF FISYSSCKEF LNTKMAVKQT PLTDAVSASI
GEIFACIARV PTEIIKQRAQ TNPQKRPLQI FGELIKEGEG RRKKFKFLAI YKGYFSTLFR
EIPFSFIEFP LWEFLKQKRR KLTNKECSPL ESAACGSIAG LIAAGITT
//
