ID A0A0V1DD40_TRIBR Unreviewed; 1799 AA.
AC A0A0V1DD40;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 20.
DE SubName: Full=Telomere length regulation protein TEL2-like protein {ECO:0000313|EMBL:KRY59284.1};
DE Flags: Fragment;
GN Name=Telo2 {ECO:0000313|EMBL:KRY59284.1};
GN ORFNames=T03_1241 {ECO:0000313|EMBL:KRY59284.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59284.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59284.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59284.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TEL2 family.
CC {ECO:0000256|ARBA:ARBA00006133}.
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:KRY59284.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDI01000014; KRY59284.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 1.10.8.1120; Histone RNA hairpin-binding protein RNA-binding domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.25.40.720; Telomere length regulation protein 2, C-terminal domain; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029344; SLBP_RNA_bind.
DR InterPro; IPR038294; SLBP_RNA_bind_sf.
DR InterPro; IPR038528; TEL2_C_sf.
DR InterPro; IPR019337; Telomere_length_regulation_dom.
DR PANTHER; PTHR15830; TELOMERE LENGTH REGULATION PROTEIN TEL2 FAMILY MEMBER; 1.
DR PANTHER; PTHR15830:SF10; TELOMERE LENGTH REGULATION PROTEIN TEL2 HOMOLOG; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF15247; SLBP_RNA_bind; 1.
DR Pfam; PF10193; Telomere_reg-2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 121..297
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 327..422
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 447..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY59284.1"
FT NON_TER 1799
FT /evidence="ECO:0000313|EMBL:KRY59284.1"
SQ SEQUENCE 1799 AA; 205915 MW; 0567ED352DA8D05A CRC64;
LVRWQRLDEK CPDRETIDRI DLVEFNLISR TIRAKKYLQS IFRDCFRSVF SISHSNCRIG
KNAHVRPLSS KRFVGFDSSL CKTRTMLKLR FKQPKHAWIL VMEKMSEKCD GGLPEPSTET
QLAKIYDEFV TSERHYLEHL DLVIRYFADP LLCSKILTQR EVANIFGDLR SIRLVNQVLY
DRLMAGLEIA EAFGDLIHFM KLYSAYGRNY SASQQLLLQL LEKNKHFRQF CEMQECLPVL
KGLKLAALLI TPIQRIPRYK LLLEQILKLL DNSSRQHLQI SKLVQQIGAL AETVDSCIEE
FENSAKIIAV QNMLDGCAPK LVMPGRKLLK EGLLNKMSSS NSGFRHRMFW LFTDIILYAK
PAMKKKNRYQ CCCILPLRHC MIERILGRSM FRLICKDEVL LLHAEQYSVM DEWVVAIENA
IRYLLECRKS LRKESSNSFP MHRQALKLHR SRSSFTEKLS SRKTQIPNDD PKPTKKRRSF
LLSLLSKLGG RWSSRNRRQS GDDSLAEVET NNSRMTNSVS LFSTGSRLPL DNIAEETSIL
GRRPKEPPPK NHRLTLVLCK KSRMKMSPIP LNWLLKSNRY DYSRRLESSS LSTSGIKSSV
FELFGECDDY VLDFGEKSWA DIMEEEELYE KEKLSRMNTQ QNEANVIAPF VEESTSETIV
PEHEVAAVDF SQLHSTYAQQ MLSKSEPSHE EPSTFARRNR RMRRPVAPGP RASKQAEVDA
NEELKQGSQW TRARQPHLLN EENTLEAGDV ESDKRKEETL PEVVKPVEEA PKKRVGPPLR
YPLPATWREP TNGWEEDQAV LKRRQKDLDK GYNSEAYKKY IAAVPKSKRE KGIHPRTPNK
YLKFSRRSWD SQVRLWRKML HVAVGEEYNS DASFVSSSSC SDASSVVSEN EVTSLRKLSE
NEESVEVGRK VDPVNESIPT NQQDDETLTA HCRNLCICKS LNLICQSLES KKFASYGASH
SRKAMSECKS TTTTLLKRLL SASSRLELRS CLLDIGNYVV ENQNFGSFFR VGEVLLQALK
PSTFNMLLPV EQDELFYSIF LRANPADVVL LLSKPPDRIS PFVVPKFVLI VERFCQHKLD
QLFTSMANAD DGRRPCDRSM QGQLCQALFA IPDRMVGLLK PREAKKRLTV YWNNFCSAYV
RSLGQIDDQL TGAVVNKSEL EMSFHGALLG KACLTGRQRR LLEALLPFAL RRARNARRRG
RRAWFDQLFR ACPADAVKQL FTDLILLLKS ASDLHTLVDD FGVVDDQARF VLSRSLLFTS
HFDTATVPRL VIGYLKLVGG EQEKVLLQEI FLLSLQNWSF KSSIVNTTVQ QQRYVAQTLL
LTAKELVRRH WMEELENQAA PFVLDGMYNH LGGLSSNVQQ LGMVVGEALV SMLKMPVEDV
KFNYEEDDFV ASLRAMLEDE LPLSEQESAE DILSDFTVLS VDSTDEMIPI QINLRDSDDD
EDEDNSETMT DHYQLEEDEQ LMRRRKGQSS QLSYIEDCLE QLLCVENDDY DCFEMALLSL
EKVLFKERST PGVGELAGHA AKVLLHLENK FAQQLHDQLR VKCLVGCVIS DPLNVAAYLC
QEFHSRALTV GMRVEVLRVL CTAAELLSRD ANNNTKQKQQ HVENSLLKSG ALAPEQWVRD
GWRAVLQQRI EAKTVRRQKY DYQSADRCRV NRFASIAAGI FDMLIDRRHT VHSTALREPL
VLGVFVHTLA TLLLAAGHSA QLRSMAKLTI TVGWPEHCNH EEPLVRAGLL FAFLAVLSRL
PVELLFADLG EQNLRERVDW LERVRTGDLD PNCRQLAELT LNTWNQAILR MADQIFTCN
//