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Database: UniProt
Entry: A0A1I7V8P3_LOALO
LinkDB: A0A1I7V8P3_LOALO
Original site: A0A1I7V8P3_LOALO 
ID   A0A1I7V8P3_LOALO        Unreviewed;      1511 AA.
AC   A0A1I7V8P3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Suppressor of Ty 6 homolog {ECO:0000256|PIRNR:PIRNR036947};
OS   Loa loa (Eye worm) (Filaria loa).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX   NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_11091};
RN   [1] {ECO:0000313|Proteomes:UP000095285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Loa loa.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:EN70_11091}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- FUNCTION: May regulate transcriptional elongation by RNA polymerase II.
CC       {ECO:0000256|PIRNR:PIRNR036947}.
CC   -!- SUBUNIT: Interacts with glp-1 and lin-12.
CC       {ECO:0000256|PIRNR:PIRNR036947}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR036947}.
CC   -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000256|ARBA:ARBA00009253,
CC       ECO:0000256|PIRNR:PIRNR036947}.
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DR   STRING; 7209.A0A1I7V8P3; -.
DR   WBParaSite; EN70_11091; EN70_11091; EN70_11091.
DR   eggNOG; KOG1856; Eukaryota.
DR   Proteomes; UP000095285; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:UniProtKB-UniRule.
DR   GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
DR   CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR   CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 1.10.10.650; RuvA domain 2-like; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   Gene3D; 1.10.10.2740; Spt6, Death-like domain; 1.
DR   Gene3D; 1.10.150.850; Spt6, helix-hairpin-helix domain; 1.
DR   Gene3D; 1.10.3500.10; Tex N-terminal region-like; 1.
DR   Gene3D; 3.30.420.140; YqgF/RNase H-like domain; 1.
DR   InterPro; IPR041692; HHH_9.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR042066; Spt6_death-like.
DR   InterPro; IPR032706; Spt6_HHH.
DR   InterPro; IPR035420; Spt6_SH2.
DR   InterPro; IPR035018; Spt6_SH2_C.
DR   InterPro; IPR035019; Spt6_SH2_N.
DR   InterPro; IPR028231; Spt6_YqgF.
DR   InterPro; IPR023323; Tex-like_dom_sf.
DR   InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR   InterPro; IPR017072; TF_Spt6.
DR   InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR   InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR   PANTHER; PTHR10145; TRANSCRIPTION ELONGATION FACTOR SPT6; 1.
DR   PANTHER; PTHR10145:SF6; TRANSCRIPTION ELONGATION FACTOR SPT6; 1.
DR   Pfam; PF14635; HHH_7; 1.
DR   Pfam; PF17674; HHH_9; 1.
DR   Pfam; PF00575; S1; 1.
DR   Pfam; PF14633; SH2_2; 1.
DR   Pfam; PF14639; YqgF; 1.
DR   PIRSF; PIRSF036947; Spt6; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00732; YqgFc; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 2.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF158832; Tex N-terminal region-like; 1.
DR   PROSITE; PS50126; S1; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR036947};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR036947}.
FT   DOMAIN          1211..1268
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          1310..1417
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          1..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..117
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..256
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1511 AA;  176605 MW;  92D9786AB3FDE890 CRC64;
     MSEFLDNQAE ESENSGETTD TSIDDDDLEP RAKRKRKQKK KKEKAKKTKR IRSDDEDDEE
     DDDGEDDEAK IQKEMAGFVV DEDEAEEDGD DNEDDDRSDI EKDDDLELDD EDLDLLNDNL
     DIQQRPAGGR VVIESDEEED RDRSKSNLYD KDDLAGDDDQ RSDYRESERR VYDGDEGSGT
     ESEHSEDDFI VTDDGQQPQH RQRRYRFADV PEQAIDDARE IFGVDDFNFA EFYDEDAEPG
     EDEDEYPEDE EQEELEGGDV SRSRKMKPKE KRATLMDTIE PAELEEKLLS PMDKRIQLDD
     RPERFQLRRV PVCEADEHEL EIEAKWIYQY AFDNATLSEQ EESCLTVLSN LDLRIDERAK
     IAAEAPDKIK EALKFIRNQL FEANRNFFSL FPFYRKEYVE SCLVINDLWK VYQWDEKWCH
     LQQRKKRLLE LMKRMLNYQM ENDNAAGMRI VTEQDMNEVH GVQTVEGLMD VSTKFQLYYG
     PEVPKMIDWE KIQNLSEDDP EREAAEMRFR AATRTDKYML CVQNGLSGMA SRFGLTPLQF
     AENLDWKRHD IVQDDEEPLK AAEQYVCQSF PTPEAVLTGA IHVVAKQLSR EPKVRELLRL
     RYRLRLKISV CPTKKGREEI DENHKLWPRR YIRDKPVASL RHDEYLWYVQ AHAGGLLNLK
     LHCDTEDDVR FEKTMLQEFL SEQPYHRDEY SRVVDTWNKI REEAVTVCVN NFLLPVFERE
     AHERLLQEAK DYVIKQSTQN LYDRIKTAAY RNVHDDDDDD FESGFASGTR VLSIAYPEER
     DQASFCALLD QDGQVLDHLR LIHITKSMNS KRPGEADLKR QDMVHLRKFI EKRRPCVIAI
     CGENMDAYYL RRDIESLLHE ISGMAKEIPV EIVDNEAAKI YMHSKQAIAE FPNYPLMLRQ
     AVSLGRLLLD PLIEYAHLCN TDDDILCVSY HPLQSEVNKE ELLFALSLEF INRVNEVGVD
     VNRCLEYSHT SYLLQFVCGL GTRKAVHLLK ILKQNDNLLE SRTKLVTLCR MGPKVFMNSA
     GFIKIDTAKV SERTDAYVEV LDGSRVHPET YEWARKMAVD ALEIDDAADP TSALEEILQN
     PDKLKDLDLD AFAEELARQG FGNKSITLYD IRAELNHRYK DLRIPYESPS AEKIFTMLTK
     ETSDSIGKLV MGRVMHIVYR KPRDPEERER VPPIRDERTG QWKCQYCYKP DFNNTNEVWQ
     HIDSCPGQPV GVKVRFDSGI TGFIPNKYLS DRPDSFVDPS ERVRRNQPIY CRILELDPDK
     FSATCSCRSS DLRGLQPQNS EFDRYFDKLK YQDDDEKDKK LREKRKIVTY FVKRVISHPS
     FHNVTFKDAE RMLQKFEQGE AIIRPSSKSV SHLTVTWKVA DGIYQHIDIK EEGKQHQFSL
     GKTLLIGTEE FEDLDEILAR HIQPMAALAR DVLSHKYFLD GKRAEDRDAI ESYLFDEKKR
     NPQRIPYTLT PSQEYPGKFV VSYLPRNKAR HEYMTVTPEG FRFRQQLFQS LEVVLSWFKV
     HYREPPPGMY R
//
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