ID A0A2J5I501_9EURO Unreviewed; 1555 AA.
AC A0A2J5I501;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000256|ARBA:ARBA00015492};
GN ORFNames=BDW42DRAFT_199041 {ECO:0000313|EMBL:PLN84912.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN84912.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NEMF family.
CC {ECO:0000256|ARBA:ARBA00008318}.
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DR EMBL; KZ559508; PLN84912.1; -; Genomic_DNA.
DR OrthoDB; 129892at2759; -.
DR Proteomes; UP000235023; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProt.
DR Gene3D; 3.90.870.10; DHBP synthase; 1.
DR Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR Gene3D; 3.40.50.11030; Threonylcarbamoyl-AMP synthase, C-terminal domain; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR021846; NFACT-C.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR InterPro; IPR006070; Sua5-like_dom.
DR InterPro; IPR038385; Sua5/YwlC_C.
DR InterPro; IPR005145; Sua5_C.
DR NCBIfam; TIGR00057; L-threonylcarbamoyladenylate synthase; 1.
DR PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR Pfam; PF11923; NFACT-C; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
DR Pfam; PF05833; NFACT_N; 1.
DR Pfam; PF03481; Sua5_C; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT DOMAIN 1160..1364
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT REGION 445..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 336..367
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 445..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..800
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1555 AA; 169422 MW; FAC82444E5688F0C CRC64;
MKQRFSSLDV KVISQELSAE LVNLRVSNIY DLSSRIFLFK LAKPDHRKQL VVDSGFRCHV
TQYSRTTATA PSGFVTRMRK FLKSRRITSI TQIGTDRVID FAFSDGMYHM FLEFFAGGNV
IVTDSEYNIL TLFRQVPAGV GEEEMRVGLR YSVTNKQNYG GVPDITDERI RTTLGRAAEV
FAREDGAPKK SKKKRNADVL RKALSQGFPE YPPLLLDHAF AVRGVDPATP LEEVLGDEGL
LGAVRGVLEE AQGEWRRLST GEHHPGFIVA KEDAKAAAKE QAGDGEDDKA GLLYEDFHPF
RPRQFEGRPG VKVLEFPSLN ATVDEYFSSI ETQKLESRLT EREEAAKKKL DAVRQEHEKR
IGALKDQQDL NVRKAGAIED NVYRVQEAID AVNGLIAQGM DWVEIARLIE MEQGRGNPVA
AIIKLPLKLY ENTITLLLGE AGDEQEEAEQ LFSESESESE DEGESVQAAQ RASTALTIDV
DLGLSPWANA TQYYDQKKNA AVKEQRTAQS SSKALKSHEK KVKDDLKRGL KQEKQVLRQA
RNPFWFEKFL FFISSEGYLV LGGHDGMQSE ILYRRHLQKG DIFVNADLDG ATPMIVKNRA
GPGVPIPPST LSQAGNLCVA TSSAWDSKAI MPAWWVHAHQ VTKTASSGGG LLPVGQFEAK
GEKNFLAPSQ LVLGFAVMFQ ISKESLRNHK VQMFEDTAAT EVPTEQQVAG TADGAQTVEE
KKDTDQVETI EASAQPEKPE AQNSESDDEK DPDSVPAGNP LQRGVSELTL AGKPAEEEEE
AKDEPEGEDG EQDDEQAAAD EAESIASSQP QDKRELSARE RRMLRQGKPI DSDPNQKGTP
SPAPSTKSAA SKQQPPAPTR GRKAKAKKAA AKYADQDDEE RELALRLLGA NKAKAEKAAA
AAEAKAKREK EAEAQKQRRK AQHERAAQAE QKRQALFEEG GGDDYDEETA AAERADLSWI
PALVGTPHPE DEILAAIPVC APWAALGRYK YRVKLQPGAV KKGKAVKECV GRWVSEMTVG
KVKKEHAEDA GISRADAEKI RAREGELVKG WKDTEIINTV PVGKVRIMTG SSGGGGDGKA
KGKGGGGGKQ GGKGGKKNAG GVPRCLTRSF TSAAASVPVA MSCYLTTRVA PVVRLNEEGP
GGRTLAEWWA SERSSQTPEA IAIQEAARLL QTSDIPVAFP TETVYGLGAD ATRSEAVRGI
YKAKQRPSDN PLIVHVDSLG MLDRLLNPDL VSPTRATKTP RNTIPPIYQP LIERFWPGPL
TILLANPSGS LLAKEVTSTL TTFGVRMPAS PLARLLIHAT DRPLAAPSAN ASTKPSPTTA
EHVYHDLQGR IELILDGGPC GVGVESTVVD GTCDPPVILR PGGIGIEELR ACPGWEKVGI
AYDDGTSEVK EVPRAPGMKY RHYSPRARVV LFEPGSNAQA ISKRILHDME DSAVGVRKVG
TVRTRHWARG LGLLSEAEMT ESLKTLPSPV LDLVGFSVPV DDDKVKDAAA SKEMFDCYLG
DDIESVARRL FFALRAMDEL GVDIIYVEGI SDQDGDLSAA VMNRLRKAAE AEIKV
//
