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Database: UniProt
Entry: A0A178AFD5_9PLEO
LinkDB: A0A178AFD5_9PLEO
Original site: A0A178AFD5_9PLEO 
ID   A0A178AFD5_9PLEO        Unreviewed;       794 AA.
AC   A0A178AFD5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=asparagine--tRNA ligase {ECO:0000256|ARBA:ARBA00012816};
DE            EC=6.1.1.22 {ECO:0000256|ARBA:ARBA00012816};
GN   ORFNames=IQ06DRAFT_320591 {ECO:0000313|EMBL:OAK95217.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK95217.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK95217.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK95217.1,
RC   ECO:0000313|Proteomes:UP000077206};
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; KV441723; OAK95217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AFD5; -.
DR   STRING; 765868.A0A178AFD5; -.
DR   InParanoid; A0A178AFD5; -.
DR   OrthoDB; 5481380at2759; -.
DR   Proteomes; UP000077206; 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; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 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:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:OAK95217.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          178..523
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REPEAT          501..589
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          600..684
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          691..782
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   794 AA;  86506 MW;  4FB69C1C00FF02CF CRC64;
     MLPIRRSACR FSLLRHNRFT TPASAQVSPS CRPRYNSTLC PDNIAELLRP SAAESKSVPP
     LVTDGQTLKV NGYVRSVRKQ KRIAFAAIGD GSTLHTVQAV LSPELAEGLS TGVAVTVTGT
     WTPSQGQGQS YELQVSDVQI LGENDAATSP IQKKYQTAEY LRTVPHLRPR LPFNALILRL
     RSLVTAQITN YFANQNFVQC HPPIITSSDC EGAGEVFTVT PGAAVKSDSG SASSVKEHED
     PFFGSPKYLT VSSQLHLEAL AQSVNKVWTL SPTFRAEKSD TARHLSEFYM LEAEMTFADD
     LQTVMDVVEN MLRAVTEGIQ SSAVGQELLE ARARDHSTDA TSLSHDALAH RWQGLIHGPW
     PRITYDTAIQ HLEDAVNNNN VEFEFAPKHA DGLQTEHERY IAESLGHGGP VFVTDYPRNI
     KPFYMAPTKD AKTGGRTAST VACFDLLVPE ICELVGGSMR EHRLSELLKS MDEHGLRHTA
     SAPSEDSEGS LQCYEALPPN FSLTANMLAG AFAGIAEHSV MYPVDLLKTR IQIINPSPGA
     MYSGISNAMV TISRVEGFGT LWRGLSSVVM GAGPAHAVYF ASYEATKHAL GGNEGGSEEH
     HPLAAAASGA AATISSDALM NPFDVIKQRM QMHGSIYKSV PHCAREVFRT EGIGAFYVSY
     PTTLCMTVPF TALQFMAYES FSKVMNPTGR YDPYTHCFAG GIAGGFAAGF TTPLDVIKTL
     LQTRGNATDA ELRNVSGLWQ AAKIIHQREG YRGYFRGLKP RIITTMPSTA ICWSAYEMAK
     AFFIKRSTDP SKSI
//
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