ID U4UGU2_DENPD Unreviewed; 2399 AA.
AC U4UGU2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=glycylpeptide N-tetradecanoyltransferase {ECO:0000256|ARBA:ARBA00012923};
DE EC=2.3.1.97 {ECO:0000256|ARBA:ARBA00012923};
GN ORFNames=D910_07177 {ECO:0000313|EMBL:ERL89816.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL89816.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL89816.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000256|ARBA:ARBA00009469}.
CC -!- SIMILARITY: Belongs to the SF3B1 family.
CC {ECO:0000256|ARBA:ARBA00005754}.
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DR EMBL; KB632191; ERL89816.1; -; Genomic_DNA.
DR STRING; 77166.U4UGU2; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:UniProt.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd04112; Rab26; 1.
DR CDD; cd17083; RAWUL_PCGF3; 1.
DR CDD; cd16735; RING-HC_PCGF3; 1.
DR Gene3D; 3.40.630.170; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022677; NMT_C.
DR InterPro; IPR022678; NMT_CS.
DR InterPro; IPR022676; NMT_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR015016; SF3b_su1.
DR InterPro; IPR038737; SF3b_su1-like.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR12097:SF0; SPLICING FACTOR 3B SUBUNIT 1; 1.
DR PANTHER; PTHR12097; SPLICING FACTOR 3B, SUBUNIT 1-RELATED; 1.
DR Pfam; PF01233; NMT; 1.
DR Pfam; PF02799; NMT_C; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF16207; RAWUL; 1.
DR Pfam; PF08920; SF3b1; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00975; NMT_1; 1.
DR PROSITE; PS00976; NMT_2; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
DR PROSITE; PS51420; RHO; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 2191..2230
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2399 AA; 269727 MW; 90668A701C452953 CRC64;
MGGVHAVMDL ATPVPLKSPS RELSLALLGK MSGKEERNSP KKPPKGDADP APELESESAN
GTGEDPTGLA NPLNTITINE LKAAMELYTL SQKPAKTPEE ALKKSYQFWN TQPVPKMDEK
VTVNEAIEPA CDPXDIRQEP YSLPGGFKWD TLHLDDPLIL TELYTLLNEN YVEDDDAMFR
FDYQPEFLKW ALQPPGWKSD WHCGVRVVHS GRLVGFISAI PATLDIYKKR QRMVEINFLC
VHKKLRAKRM APVLIREITR RVNLTGVFQA VYTAGIVIPK PVSTCTYWHR SLNPRKLIEV
KFSYLSRNMT MQRTLKLYKL PDAPATPGFH KLRPQDVDGA HRLLNQYLGR FEMAPHFSKE
DFVHWFTPRP NIIESFVVET GGQITDFVSY YTLPSSVMHH PVHKNLKAAY SFYNVSTRTP
WVALMQDALI SAKQLGFDVF NALDLMDNAQ FLEPLKFGIG DGKLQYYLYN WKCPSMAPNN
VGLVCRPRKP QLVLSCPNLT LRWLDIEAQI RDIQSKKKEA PPEGGEKGVS LGESGFFDSE
IYDGKDKKYE GYVTSIAAND EVDDEEEEVG YSQKRTGLGA PVALLNDIAQ SEKDYDPFAD
RRRPTIADRE DEYRQKRRRM IISPERADPF ADGTCGKTPE VNARGYTQIM KETLLKGEEN
EVRRKIIERA KDGTLKPQNG DAKPAPKKRG RWDQTVEETF IPAKKKTLSV STPSTAATPV
WEGDAGLTQK TPADIRWDET PGHKGSETPG ATPGQSTRMW DATPGAATPG RETPGHDKAS
SRRNRWDETP KTERETPGHS SGWAETPRTD RTGADLIQET PTPGASKRRS RWDETPSAAT
PSVSMTPGAM TPQTPHGTPG HATPMLTPGG STPVGTKAMA MATPTPGHLA SMTPEQLQAF
RWEREIDERN RPYSDDELDA MFPPGYKVLP PPAGYIPIRT PARKLTATPT PLVGQTPVGF
FMQNEDKSAK YMDNQPKGQN LPFMKPEDAQ YFDKLLVDVD EEALSPEEQK ERKIMKLLLK
IKNGTPPMRK AALRQITDKA REFGAGPLFN QILPLLMSPT LEDQERHLLV KVIDRILYKL
DDLVRPYVHK ILVVIEPLLI DEDYYARVEG REIISNLAKA AGLATMISTM RPDIDNIDEY
VRNTTARAFA VVASALGIPS LLPFLKAVCR SKKSWQARHT GIKIVQQIAI LMGCAILPHL
KSLVEIIEHG LVDEQQKVRT ITALGIAALA EAATPYGIES FDSVLKPLWK GIRTHRGKGL
AAFLKAIGYL IPLMDAEYAN YYTREVMLIL IREFQSPDEE MKKIVLKVVK QCCSTDGVEP
QYIKEEILPQ FFKHFWNHRM ALDRRNYRYC HVVPAQPSFG AALAILVRQL VDTTVEIANK
VGASEIINRI VDDLKDENEA YRKMVMESIE KIMGNLGAAD IDSRLEEQLI DGILYAFQEQ
TTEDVVMLNG FGTIVNQLGK RVKPYLPQIC GTILWRLNNK SAKVRQQAAD LISRIAVVMK
TCQEEKLMGH LGVVLYEYLG EEYPEVLGSI LGALKAIVNV IGMTKMTPPI KDLLPRLTPI
LKNRHEKVQE NCIDLVGRIA DRGPEYVSAR EWMRICFELL ELLKAHKKAI RRATVNTFGY
IAKAIGPHDV LATLLNNLKV QERQNRVCTT VAIAIVAETC SPFTVLPALM NEYRVPELNV
QNGVLKSLSF LFEYIGEMGK DYIYAVAPLL EDALMDRDLV HRQTACAAIK HMALGVYGFG
CEDALVHLLN YVWPNIFETS PHLVQAFMDA IEGMRVALGP IKVLQYSLQV SIRKGFDRVE
ITGLCAFQGL FHPARKVRDV YWKIYNSLYI GGQDALVAGY PRIANDPKNQ YIRYELDYIL
PMGASEAEMG GPSALAGSLA GGALILVASR SRSWPFPSAV LVGCLFACRS SSQSVAQQAA
ICLSRLERFF WSGSGQSRRA PQWALPSRPA KAPTMTDRED SMDDDVFEAV EARLEVPEDG
QRGTHSPTGY RGYQPSIDVI NLCNQLEDAE VPVHKTILLG DSGVGKTSLL VKFDTGKFES
SKFSATVGIG FTTKVVQVDD SKVKLQIWDT AGQERFRCVT HAYYRDAHAL LLLYDVTNKK
SFDNIRAWLG EIKDYAHDDV VIMLLGNKAD CGSDRAIKRE EGERLAREYR VTFMETSAKS
GQNVELAFHA IARQLVERRI RLRSINNHIA CKICKGYLID ATTVTECLHT FCKSCLVKHL
EENNTCPICS IVIHQSHPLQ YISFDRTMQD IVYKLVPNLM EVELSREREF YRVRGLPNPK
DIPLQNLDLN SEDLQHDPHA ASDYHRQDEQ VNVCLECISA NLRALKRRYI RCSAQATILH
LKKFIAMKIL NGMDQYREID ILCNEELLGK DHTLKFVVVT RWRFQNAPLT LQYRPKIDI
//
