ID A0A0V0TJ98_9BILA Unreviewed; 1820 AA.
AC A0A0V0TJ98;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE SubName: Full=Telomere length regulation protein TEL2-like protein {ECO:0000313|EMBL:KRX39112.1};
DE Flags: Fragment;
GN Name=tag-52 {ECO:0000313|EMBL:KRX39112.1};
GN ORFNames=T05_740 {ECO:0000313|EMBL:KRX39112.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX39112.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX39112.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX39112.1};
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:KRX39112.1}.
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DR EMBL; JYDJ01000243; KRX39112.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..279
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 357..452
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 477..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX39112.1"
FT NON_TER 1820
FT /evidence="ECO:0000313|EMBL:KRX39112.1"
SQ SEQUENCE 1820 AA; 208136 MW; FB6AA4C951334695 CRC64;
LVRWQRLDEK CPDRETIDRI DLVEFNLISR TIRAKKYLQS IFRDCFRSVF SISHSNCRIG
KNAHVRPLSS KRFVGFDSLL CKTPPMLKLC FKQPKHAWIL VMEKMSEKCD GGLPEPSTET
QLAKIYDEFV TSERHYLEHL DLVIRYFADP LLCSKILTQR EVANIFGDLR SIRLVNQVLY
DRLMAGLEIA EAFGDLIHFM KLYSAYGRNY SASQQLLLQL LEKNKHFRQF CEMQECLPVL
KGLKLAALLI TPIQRIPRYK LLLEQILKLL DNSSRQHLQI SSGFSHIFAL LYCYISIALV
IYLLSGEILF AELVQQIGAL 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 RASKQAEADA NEELKQGSQW TRARQPHLLN EENTLEAGDV
ESDKRKEETL PEVVKPVEEA PKKRVGPPLR YPLPATWREP TNGWEEDQAV LKRRQKDLDK
GYNSEAYKKY IAAVPKSKRE KGIHPRTPNK YLKFSRRSWD SQVRLWRKML HVAVGEEYNS
DASFVSSSSC SDASSVVSEN EVTSLRRLSE NEESVEVGRK VDPVNESIPT NQQDDETLTE
SVHLICQSLE SKKFASYGAT HSRKAMSECK STTTTLLKRL LSASSRLELR SCLLDIGNYV
VENQNFGSFF RVGEVLLQAL KPSTFNMLLP VEQDELFYSI FLRANPADVV LLLSKPPDRI
SPFVVPKFVL IVERFCQHKL DQLFTSMANA DDGHRPCDRS MQGQLCQALF AIPDRMVGLL
KPREAKKRLT VYWNNFCSAY VRSLGQIDDQ LTGAVVNKSE LEMSFHGALL GKACLTGRQR
RLLEALLPFA LRRARNARRR GRRAWFDQLF RACPADAVKQ LFTDLILLLK SASDLHTLVD
DFGVVDDQAR FVLSRSLLFT SHFDTATVPR LVIGYLKLVG GEQEKVLLQE IFLLSLQNWS
FKSSIVNTTV QQQRYVAQTL LLTAKELVRR HWMEELENQA APFVLDGMYN HLGGLSSNVQ
QLGMVVGEAL VSMLKMPVED VKFNYEEDDF VASLRAMLED ELPLSEQESA EDILSDFTVL
SVDSTDEMIP IQINLRDSDD DEDEDNSETM TDHYQLEEDE QLMRRRKGQS SQLSYIEDCL
EQLLCVENDD YDCFEMALLS LEKVLFKERS TPGVGELAGH AAKVLLHLEN KFAQQLHDQL
RVKCLVGCVI SDPLNVAAYL CQEFHSRALT VGMRVEVLRV LCTAAELLSR DANNNTKQKQ
QHVENSLLKS GALAPEQWVR DGWRAVLQQR IEAKTVRRQK YDYQSADRCR VNRFASIAAG
IFDMLIDRRH TVHSTALREP LVLGVFVHTL ATLLLAAGHS AQLRSMAKLT ITVGWPEHCN
HEEPLVRAGL LFAFLAVLSR LPVELLFADL GEQNLRERVD WLERVRTGDL DPNCRQLAEL
TLNTWNQAIL RMADQIFTCN
//
