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Database: UniProt
Entry: A0A0D8XMK6_DICVI
LinkDB: A0A0D8XMK6_DICVI
Original site: A0A0D8XMK6_DICVI 
ID   A0A0D8XMK6_DICVI        Unreviewed;      1525 AA.
AC   A0A0D8XMK6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative arginine--tRNA ligase {ECO:0000313|EMBL:KJH45858.1};
GN   ORFNames=DICVIV_08086 {ECO:0000313|EMBL:KJH45858.1};
OS   Dictyocaulus viviparus (Bovine lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX   NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH45858.1, ECO:0000313|Proteomes:UP000053766};
RN   [1] {ECO:0000313|EMBL:KJH45858.1, ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH45858.1,
RC   ECO:0000313|Proteomes:UP000053766};
RA   Mitreva M.;
RT   "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX   PubMed=26856411; DOI=10.1038/srep20316;
RA   McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA   Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA   Sternberg P.W., Gasser R.B., Mitreva M.;
RT   "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT   lungworm biology and support future intervention.";
RL   Sci. Rep. 6:20316-20316(2016).
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DR   EMBL; KN716382; KJH45858.1; -; Genomic_DNA.
DR   STRING; 29172.A0A0D8XMK6; -.
DR   Proteomes; UP000053766; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd17678; RUN2_DENND5; 1.
DR   Gene3D; 1.20.58.900; -; 3.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR047278; DEN5A/B.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004012; Run_dom.
DR   InterPro; IPR037213; Run_dom_sf.
DR   InterPro; IPR004853; Sugar_P_trans_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR46070; PINSTRIPE, ISOFORM A; 1.
DR   PANTHER; PTHR46070:SF1; PINSTRIPE, ISOFORM A; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   Pfam; PF02759; RUN; 2.
DR   Pfam; PF03151; TPT; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
DR   SMART; SM00836; DALR_1; 1.
DR   SMART; SM00593; RUN; 2.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF140741; RUN domain-like; 2.
DR   PROSITE; PS50826; RUN; 2.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:KJH45858.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053766};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        816..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        842..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        882..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        934..952
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        958..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        990..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1029..1050
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1057..1077
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1083..1105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          174..469
FT                   /note="RUN"
FT                   /evidence="ECO:0000259|PROSITE:PS50826"
FT   DOMAIN          654..803
FT                   /note="RUN"
FT                   /evidence="ECO:0000259|PROSITE:PS50826"
FT   REGION          347..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1525 AA;  172177 MW;  BEEB7F142187EB64 CRC64;
     MFTSLIDAKI LSQWETPDDN LVIFDTRIAK MREKFGLSMV RTPTYESTPS FGDSEELISK
     REEMLDYVVP GPHELAGAVS MNYNGVWPEQ INTALLEGAS ISVIGRPNST YGSTGLVGDS
     PDLIAKQQLK FVDQLLYETK GTVICLGKTK RMLVDKMGKE ALQLGHFDAG INGVEENTLV
     ASFCDLLERI WAHGLTKKQG KSSLWSFVLQ HQDLEKTCLS TKALSSSMLT PGDGRRHTIK
     RTPSLSYCEV PSPVILQPTN ENDFACALSE IVETIQREFG KSDDDNVPVW SRSILRAANF
     FADKLTTTPK DEIHGVPFAT SAKRHSSTLL KNSSSVSDFS SPNWNGEIRR SAESSDSPRR
     RSQSRPRSPE TGARVLLAPL PTHIAYDLKN VLRMTEIKTD IGYARAFVRL ALERKLLHKH
     LATLLANNHL LSELYKPYAF VRCEDEREQF LYHILSLNAA QFRCFTNTFT KTKMDYQVVI
     VTGGWRGSLP AVWVMHKNLG VLSTLRIGHS PGTEKPPNWY LEYIIVRNEI TGQMYRFPCG
     RWFGQSAEDR RWFGNSCDVS LERLLVAEPI CGNDSADLTF GALPNSPVRG TRRGRVSSRS
     QTPQRDRSPS QSRTYSSTSS SKARVTEIQQ VLGESVNSLV KYFYSEKHTK SELAYLLCGE
     HGLINAIEQA FQFGRHTSVW LFRQPSPWDY IEKVCSWLMD VLRRRDTKWT PEQCELVTHT
     LKLVRKISNR TALGKDAKFH VFILLMIRDH ILSGFLQVMA WTPITAQLYD EVSFLRAPVH
     LTYLSRLLDS LNEFNFSLDP SLTYGVMGNS ILLKRFSAAF FYGVTSIIVV FVNKILLTNF
     RFPSFLVVGF GQMVATVIVL FSARALHLVS FPSFDYSIPR KIMPLPLFFV VNLVSGLGGT
     QLINLPMFTV LRRFSILMTM VLEYYILGVS ATRAVRISVC LMIAGSIIAA LFDLTFDLWG
     YILIGVNDIC TAALGVYTKQ KLEAKELGKY GLMFYNSLFM LLPTVLLTFY TGDMNRALNF
     MLSSQMSPSI WACFFVSCVC GFILNYSLVL CTHFNSALTT TCVGPIKNII VTYAGMFSSG
     DYIFHWTNFI GINISVMGSI LYTYATFRKK STDQRILTVV PSSKLESQIK NLLRKTSFSQ
     VHRAVGNQVV SLNYLGDWGT QFALIATYWP KVRPSDSFWD SCSDVDKIRA ITDCYIVANK
     KRKLDEEFQV EVRKNFAEME NGIIKWQYES ENVIAARRLV ADLIKNNTVR RTVNGLWIVD
     IPNDDLNEEI ASILNRDKIY HADRYLYVVD RAQRKHFEAL RVILTKIGRD DLALKVEHIP
     YGRVKGLSTR LGRTEIVEEI ISRGKELALR FMKNSKTFKL SSEEEEEVAH KLSLSTVIFN
     EVKRAKSAEY EFSFKNAFDL DHNNALSLQV RHSRLCSIEA KNHELLPLLD KCDSIPEETP
     DFSKLAVHLS QFSTVIHAAV EQSESCHLVV YLLELSHHIG KVTSQARIKG QPVEVAVPRL
     LLLSASRAVL NEGMSLLGAS PVTAM
//
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