ID A0A096P232_PAPAN Unreviewed; 1420 AA.
AC A0A096P232;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
GN Name=IARS1 {ECO:0000313|Ensembl:ENSPANP00000019407.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000019407.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000019407.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000019407.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000114};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR STRING; 9555.ENSPANP00000019407; -.
DR Ensembl; ENSPANT00000024612.3; ENSPANP00000019407.3; ENSPANG00000024723.3.
DR eggNOG; KOG0434; Eukaryota.
DR GeneTree; ENSGT00550000074921; -.
DR HOGENOM; CLU_001493_1_1_1; -.
DR OMA; EIIVIHK; -.
DR Proteomes; UP000028761; Chromosome 13.
DR Bgee; ENSPANG00000024723; Expressed in pancreas and 65 other cell types or tissues.
DR ExpressionAtlas; A0A096P232; baseline.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:Ensembl.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00392; ileS; 1.
DR PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF19302; DUF5915; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761}.
FT DOMAIN 175..796
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 851..1007
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 43..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1420 AA; 162384 MW; CF05F7EDBCFD8393 CRC64;
MNFRYEVSSQ INTNANKMKP RPRRPFPVGL HLHRRAHNPR ATSVYTTGTD TTRMHSGALS
AGSFSRRSRK ASKHHRRTTR TSGRNHVRRD QSAPGLLAGV RQRALIGRCE AGRLPWIPHF
QRVASPPRAE SQLGRRENFF QACWPPGLSR HGGLLSNKMV QQVPENINFP AEEEKILEFW
TEFNCFQECL KQSKHKPKFT FYDGPPFATG LPHYGHILAG TIKDIVTRYA HQSGFHVDRR
FGWDCHGLPV EYEIDKTLGI RGPEDVAKMG ITEYNNQCRA IVMRYSAEWR STVSRLGRWI
DFDNDYKTLY PQFMESVWWV FKQLYDKGLV YRGVKVMPFS TACNTPLSNF ESHQNYKDVQ
DPSVFVTFPL EEDETVSLVA WTTTPWTLPS NLAVCVNPEM QYVKIKDVAR GKLFILMEAR
LSALYKLESD YEILERFPGS YLKGKKYRPL FDYFMKCKEN GAFTVLVDNY VKEEEGTGVV
HQAPYFGADD YRICMDFNII RKDSLPVCPV DASGCFTAEV TDFAGQYVKD ADKSIIRTLK
EQGRLLVAST FTHSYPFCWR SDTPLIYKAV PSWFVRVENM VDQLLKNNDL CYWVPELVRE
KRFGNWLKDA RDWAVSRNRY WGTPIPLWVS DDFEEVVCVG SVAELEELSG AKISDLHRES
VDHLTIPSRC GKGSLHRVSE VFDCWFESGS MPYAQVHYPF ENKREFEDAF PADFIAEGID
QTRGWFYTLL VLSTALFGQP PFKNVIVNGL VLASDGQKMS KRKKNYPDPV SIIQKYGADA
LRLYLINSPV VRAENLRFKE EGVRDVLKDV LLPWYNAYRF LIQNVLRLQK EEEIEFLYNE
NTVRESPNIT DRWILSFMQS LIGFFETEMA AYRLYTVVPR LVKFVDILTN WYVRMNRRRL
KGENGMEDCV MALETLFSVL LSLCRLMAPY TPFLTELMYQ NLKVLIDPVS VQDKDTLSIH
YLMLPRVREE LIDRKTESAM SQMQSVIELG RVIRDRKTIP IKYPLKEIVV IHQDPEALKD
IKSLEKYIIE ELNVRKVTLS TDKNKYGIRL RAEPDHMVLG KRLKGAFKAV MTSIKQLSNE
ELEQFQKTGT IVVEGHELHD EDIRLMYTFD QATGGTAQFE AHSDAQALVL LDVTPDQSMV
DEGMAREVIN RIQKLRKKCS LVPTDEITVY YKAKSEGRYL NNVIESHTEF IFATIKAPLK
PYPVSPSDKV LIQEKTQLKG SELEITLTRG SSLPGPACAY VNLNICANGS EQGGVLLLEN
PKGDNRLDLL KLKSVVTSIF GVKNTELAVF HDETEIQNET DLLSLSGKTL CVTAGSAPSL
ISSSSTLLCQ YINLQLLNAE PQECLMGTVG TLLLENPLGQ NGLTHQGLLY EAAKVFGLRS
RKLKLFLNET QTQEITEDIP VKTLNMKTVY VSVLPTTADF
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