ID A0A178DS10_9PLEO Unreviewed; 879 AA.
AC A0A178DS10;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN ORFNames=IQ07DRAFT_647697 {ECO:0000313|EMBL:OAL46062.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL46062.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL46062.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL46062.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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DR EMBL; KV441655; OAL46062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DS10; -.
DR STRING; 765867.A0A178DS10; -.
DR InParanoid; A0A178DS10; -.
DR OrthoDB; 5481380at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0048250; P:iron import into the mitochondrion; IEA:UniProt.
DR CDD; cd04318; EcAsnRS_like_N; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00457; asnS; 1.
DR PANTHER; PTHR45758:SF4; MITOFERRIN-1; 1.
DR PANTHER; PTHR45758; MITOFERRIN-1-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:OAL46062.1};
KW Ligase {ECO:0000313|EMBL:OAL46062.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 180..521
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REPEAT 586..674
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 685..769
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 776..867
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 879 AA; 95562 MW; 6ED00FF054598CF7 CRC64;
MSRLLPVRRR AFWSPSLVPY RRPAPPYAHV LPPCLLRCSS TFCPSNIAAL LRPYPLSSSS
QQAPPDGETV TINGYVRTVR KQKRIAFAAI GDGSTLQTVQ AVLAPQLAEG LSTGAAVSVT
GKWTPSQGQG QAYELQAEEV KVLGENDAAT NPIQKKYQTA EFLRTIPHLR SRLPFNSLIL
RLRSLVTAQV TSYFAKHDFV QCHPPIITSS DCEGAGEVFT VAPGPSTTPG HSSTNQTKRT
EEPFFGSPKY LTVSSQLHLE ALAQSVNKVW TLSPTFRAEK SDTARHLSEF YMLEAELAFV
DDANAVMDVI EDMLRSVATE LQSSFVGQEL LEARAQDQEQ DGASTSHNDL ARRWQGLVNG
PWPRVTYEYA VQHLKDAVAQ SRVDFEFAPG HEDGLQTEHE RFLAEDLGRG GPIFVTDYPR
NIKPFYMAPS TDLAADGQGA TVACFDLLVP EICELVGGSM REHRLLNLLN SMKDHNLLPA
SESDHEASEA SLQCNISNLT STRRLDLPIA PSASTLEARF PLPEIDTPAV AKLEATAPSP
GRLMATHDRP AVPLEDEHEY SSRAPHLPPD TIANICASYE ALPPNFSLSA NMLAGAFAGI
AEHSVMYPVD LLKTRMQIVN PSPSAMYSGI SNAMVTISRA EGFTALWRGL SSVVMGAGPA
HAVYFASYEA TKHALGGNEG GSEEHHPLAA AASGAAATIS SDALMNPFDV IKQRMQLHGS
TYKSVPQCAR EVFRTEGIGA FYVSYPTTLC MTVPFTALQF MAYESISKVM NPTGRYDPYT
HCFAGGIAGG FAAGLTTPLD VIKTLLQTRG NATDAELRNV SGLWQAAKII HQREGYRGYF
RGLKPRIITT MPSTAICWSA YEMAKAFFIA RSTNASTAI
//
