ID V9K7K7_CALMI Unreviewed; 1512 AA.
AC V9K7K7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Bifunctional aminoacyl-tRNA synthetase {ECO:0000313|EMBL:AFO94046.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94046.1};
RN [1] {ECO:0000313|EMBL:AFO94046.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFO94046.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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DR EMBL; JW861529; AFO94046.1; -; mRNA.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00807; GlnRS_core; 1.
DR CDD; cd10309; GST_C_GluProRS_N; 1.
DR CDD; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR CDD; cd00936; WEPRS_RNA; 3.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 3.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR InterPro; IPR017449; Pro-tRNA_synth_II.
DR InterPro; IPR033721; ProRS_core_arch_euk.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00463; gltX_arch; 1.
DR NCBIfam; TIGR00408; proS_fam_I; 1.
DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 3.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 3.
DR SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 3.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 2.
DR PROSITE; PS51185; WHEP_TRS_2; 3.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:AFO94046.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 756..812
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 829..885
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 902..958
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1045..1296
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 299..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 170435 MW; 8693F367E98091E9 CRC64;
MASTLVVNVS CPPLDALLTV EHVKDSISIS VEEGKETLLR VSKDVMFNDV NSIVRYLARV
DTKSNLYGSN LLQHAEVDHW LEFSGTRLAD SALFPDAVQE LDCALSLRTF LVGNGLTLAD
LCVWAKLKGS TPYQKQLSQN KAPTHVKRWY NFLGSQDPFQ SVGKKWAAAA ATAAPQNRVR
NEKKEDRGKF VELPGAEVGK VIVRFPPEAS GYLHIGHAKA ALLNQHYQVS FKGKLIMRFD
DTNPEKEKED FEKVILEDIS MLQIKPDRFT YTSDYFDTIM NFAEKMIKDG NAYVDNTPAE
QMKQEREQRV ESKNRSNSVE KNMQMWQEMI KGSEFGQTCC LRAKIDMASN NGCMRDPTIY
RCKIAPHPRT GTKYKIYPIY DFACPIVDSF EDVTHALRTT EYHDRDEQYY WIIDALEIRK
PYIWEYSRLN LNNTVLSKRK LTWFVNEGLV DGWDDPRFPT VRGVLRRGMT VEGLKQFITA
QGGSRSVVNM EWDKIWAFNK KVIDPVAPRY TAILQDQVVP VNIPGTQEEM KEVAKHPKNP
EVGVKPVWYG AKVLIEGADA ETFTEGEMVT FINWGNIIIT KINRDSKGKI VSLNAKLNLE
NKDYKKTTKI TWLVETTQAP CIPTICVNYE HLINKPVLGK DENFKDYVNQ NSKQEEQMLG
DPCLKELKKG DIIQLQRRGF FICDQPYEPV SPYSCKESPC VLIYIPDGHT KEMPTSGSKE
KSKADATKKA TKTDSTAKVA SPAVVAIPPS TCDTVDLVSL YNKVAAQGEM VRDLKSKKAP
REEVDTAVKS LLAMKAEYKQ KAGMEYKPGN LPTPTSIVAS TPTNVDSSSN KMLHNKVFEQ
GEVLRKLKAD KAPKDKIDKA LKSLLALKAE YKQKTGQEYK PGNVPSSASS AISTPVSSNA
LDSKALHDNV AEQGEIVRKL KAEKASKETI DTAVKILLDL KSQFKTLMGT DYKPTASADD
KNKNKKEKQN KSEKQNKSEK TEEGQKKDAT KELDKGSGNG GAGEGQGPKK QTRLGLEAKK
IVNLADWYSQ VITKAEMIEY YDVSGCYVLR PWSYAIWESI KDFFDREIKK LGVENCYFPM
FVSQAALEKE KSHVADFAPE VAWVTRSGKT ELAEPIAVRP TSETVMYPAY AKWVQSHRDL
PIKLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHTAFATRE EAAEEVLQIL DLYARVYEEL
LAIPVVKGRK TEKEKFAGGD YTTTVEAFVS ASGRAIQGAT SHHLGQNFSK MFEIVFEDPK
KPGEKQFAYQ NSWGITTRTI GVMTMIHGDD QGLVLPPRVA CVQVIVIPCG ITNSLSETDK
DSLMKKCGEY LDRLTNVGIR ARTDVRDNYS PGWKFNHWEL KGVPIRVEIG PRDMKNHQFV
AVRRDTGAKL SIPEGEAETK LKELLEEIYD NLYNRAAQDL KEHMVVADTM EHFQEELDSG
KIVQIPFCGD IDCEDWIKKT TARDQDVEPG APSMGAKSLC IPFNPLCDLK PGATCISGKE
PAKYYTLFGR SY
//
