ESAG8_TRYBB
ID ESAG8_TRYBB Reviewed; 630 AA.
AC P23799;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Putative adenylate cyclase regulatory protein;
DE AltName: Full=Leucine repeat protein;
DE AltName: Full=VSG expression site-associated protein F14.9;
GN Name=ESAG8; Synonyms=T-LR;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EATRO 164;
RX PubMed=2247064; DOI=10.1128/mcb.10.12.6436-6444.1990;
RA Smiley B.L., Stadnyk A.W., Myler P.J., Stuart K.;
RT "The trypanosome leucine repeat gene in the variant surface glycoprotein
RT expression site encodes a putative metal-binding domain and a region
RT resembling protein-binding domains of yeast, Drosophila, and mammalian
RT proteins.";
RL Mol. Cell. Biol. 10:6436-6444(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EATRO 1125;
RX PubMed=2259625; DOI=10.1093/nar/18.24.7299;
RA Lips S., Revelard P., Pays E.;
RT "A gene from the VSG expression site of Trypanosoma brucei encodes a
RT protein with both leucine-rich repeats and a putative zinc finger.";
RL Nucleic Acids Res. 18:7299-7303(1990).
CC -!- FUNCTION: May interact with adenylate cyclase to regulate its activity.
CC -!- FUNCTION: May be involved in the postranscriptional regulation of genes
CC in VSG expression sites.
CC -!- DEVELOPMENTAL STAGE: Expressed only in the bloodstream form of the
CC parasite.
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DR EMBL; M58701; AAA32117.2; ALT_TERM; Genomic_DNA.
DR EMBL; X55978; CAA39448.1; -; Genomic_DNA.
DR PIR; A36359; A36359.
DR PIR; S13724; S13724.
DR AlphaFoldDB; P23799; -.
DR SMR; P23799; -.
DR GO; GO:0005929; C:cilium; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00367; LRR_CC; 8.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW cAMP biosynthesis; DNA-binding; Leucine-rich repeat; Metal-binding; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="Putative adenylate cyclase regulatory protein"
FT /id="PRO_0000056366"
FT REPEAT 115..123
FT /note="LRR 1"
FT REPEAT 124..148
FT /note="LRR 2"
FT REPEAT 149..170
FT /note="LRR 3"
FT REPEAT 171..195
FT /note="LRR 4"
FT REPEAT 196..218
FT /note="LRR 5"
FT REPEAT 219..242
FT /note="LRR 6"
FT REPEAT 243..266
FT /note="LRR 7"
FT REPEAT 267..289
FT /note="LRR 8"
FT REPEAT 290..313
FT /note="LRR 9"
FT REPEAT 314..336
FT /note="LRR 10"
FT REPEAT 337..359
FT /note="LRR 11"
FT REPEAT 360..382
FT /note="LRR 12"
FT REPEAT 383..405
FT /note="LRR 13"
FT REPEAT 406..428
FT /note="LRR 14"
FT REPEAT 429..451
FT /note="LRR 15"
FT REPEAT 452..474
FT /note="LRR 16"
FT REPEAT 475..497
FT /note="LRR 17"
FT REPEAT 498..520
FT /note="LRR 18"
FT REPEAT 521..543
FT /note="LRR 19"
FT REPEAT 544..566
FT /note="LRR 20"
FT REPEAT 567..589
FT /note="LRR 21"
FT REPEAT 590..613
FT /note="LRR 22"
FT REPEAT 614..630
FT /note="LRR 23"
FT ZN_FING 10..46
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 22
FT /note="V -> L (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="L -> F (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="Q -> E (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="F -> C (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="N -> S (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="M -> V (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="L -> P (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="K -> R (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="T -> S (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="Y -> H (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="M -> L (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 504..506
FT /note="IWN -> FGI (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="C -> L (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="D -> E (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 543..546
FT /note="EITT -> KLQP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="V -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="L -> V (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="K -> E (in Ref. 2; CAA39448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 69999 MW; A65A35B5DCE50F7E CRC64;
MTGRSTYGMC AVCREPWAEG AVELLPCRHV FCTACVVQRW RCPSCQRRIG GRRKANPHLL
REIADVTMEL KRYRKGRSGI DVTQMARKLG GGGVTTSSEI FRRLEGSKNG RWKILNLSGC
GSELQDLTAL RDLEALEDLD LSECANLELR ELMVVLTLRN LRKLRMKRTM VNDMWCSSIG
LLKFLVHLEV DGSRGVTDIT GLFRLKTLEA LSLDNCINIT KGFDKICALP QLTSLSLCQT
NVTDKDLRCI HPDGKLKMLD ISSCHEITDL TAIGGVRSLE KLSLSGCWNV TKGLEELCKF
SNLRELDISG CLVLGSAVVL KNLINLKVLS VSNCKNFKDL NGLERLVNLE KLNLSGCHGV
SSLGFVANLS NLKELDISGC ESLVCFDGLQ DLNNLEVLYL RDVKSFTNVG AIKNLSKMRE
LDLSGCERIT SLSGLETLKG LEELSLEGCG EIMSFDPIWS LYHLRVLYVS ECGNLEDLSG
LQCLTGLEEM YLHGCRKCTN FGPIWNLRNV CVLELSCCEN LDDLSGLQCL TGLEELYLIG
CEEITTIGVV GNLRNLKCLS TCWCANLKEL GGLERLVNLE KLDLSGCCGL SSSVFMELMS
LPKLQWFYGF GSRVPDIVLK ELKRRGVHIF
