CRMA_ASPFU
ID CRMA_ASPFU Reviewed; 1537 AA.
AC Q4WYN6; Q4WYN7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Isocyanide synthase-NRPS hybrid crmA {ECO:0000303|PubMed:29844112};
DE Short=ICS-NRPS crmA {ECO:0000303|PubMed:29844112};
DE EC=1.-.-.- {ECO:0000305|PubMed:29844112};
DE EC=6.3.2.- {ECO:0000305|PubMed:29844112};
DE AltName: Full=Copper-responsive metabolite biosynthesis cluster protein A {ECO:0000303|PubMed:29844112};
GN Name=crmA {ECO:0000303|PubMed:29844112};
GN ORFNames=AFUA_3G13690/AFUA_3G13700;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND DOMAIN.
RX PubMed=29844112; DOI=10.1128/mbio.00785-18;
RA Lim F.Y., Won T.H., Raffa N., Baccile J.A., Wisecaver J., Rokas A.,
RA Schroeder F.C., Keller N.P.;
RT "Fungal isocyanide synthases and xanthocillin biosynthesis in Aspergillus
RT fumigatus.";
RL MBio 9:0-0(2018).
CC -!- FUNCTION: Isocyanide synthase-NRPS hybrid; part of the crm gene cluster
CC that mediates the biosynthesis of a yet unidentified copper-responsive
CC metabolite. {ECO:0000269|PubMed:29844112}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:29844112}.
CC -!- INDUCTION: Expressed in copper depleted conditions via the regulation
CC of the macA transcription factor. {ECO:0000269|PubMed:29844112}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the xanthocillin production.
CC {ECO:0000269|PubMed:29844112}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the isocyanide
CC synthase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL92216.1; Type=Erroneous gene model prediction; Note=The predicted genes AFUA_3G13690 and AFUA_3G13700 have been merged into 1 gene: crmA.; Evidence={ECO:0000269|PubMed:29844112};
CC Sequence=EAL92217.1; Type=Erroneous gene model prediction; Note=The predicted genes AFUA_3G13690 and AFUA_3G13700 have been merged into 1 gene: crmA.; Evidence={ECO:0000269|PubMed:29844112};
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DR EMBL; AAHF01000002; EAL92216.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAHF01000002; EAL92217.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_754254.1; XM_749161.1.
DR RefSeq; XP_754255.1; XM_749162.1.
DR AlphaFoldDB; Q4WYN6; -.
DR SMR; Q4WYN6; -.
DR STRING; 746128.CADAFUBP00003474; -.
DR EnsemblFungi; EAL92216; EAL92216; AFUA_3G13700.
DR EnsemblFungi; EAL92217; EAL92217; AFUA_3G13690.
DR GeneID; 3512307; -.
DR GeneID; 3512308; -.
DR KEGG; afm:AFUA_3G13690; -.
DR KEGG; afm:AFUA_3G13700; -.
DR eggNOG; ENOG502QRI9; Eukaryota.
DR eggNOG; ENOG502SJ3N; Eukaryota.
DR HOGENOM; CLU_001116_0_0_1; -.
DR InParanoid; Q4WYN6; -.
DR OrthoDB; 934123at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR007817; Isocyanide_synthase_DIT1.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR37285; PTHR37285; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF05141; DIT1_PvcA; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Ligase; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1537
FT /note="Isocyanide synthase-NRPS hybrid crmA"
FT /id="PRO_0000445290"
FT DOMAIN 941..1019
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29844112"
FT REGION 1..502
FT /note="Isocyanide synthase domain"
FT /evidence="ECO:0000305|PubMed:29844112"
FT REGION 351..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..752
FT /note="Adenylation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29844112"
FT REGION 1293..1526
FT /note="Transferase"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29844112"
FT COMPBIAS 354..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 977
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1537 AA; 170240 MW; 5A4BF182F1297D54 CRC64;
MFHKEAGISH LILDIILEHA LNKFDPAPDR LQGAAKNFLP IIERFVAAGT RIEACLPAFP
FKSANKVYKV LGSLPDKAEE LALDRLNTMC ARVREVYPPG LQVAIISDGI TYNDTWAYGE
ALRQMAAQKQ FMYIVFSRIK DLLDIPLPEQ MSEIVYVANC TTFRRLLLNK YERADLDIDH
EIASNPDTKL TYLGYRRFLE SDLKYIFPRG AHRSAHSYKR DCKYLAKQML IRGDAFAQAI
KTSYPNHLRL SIHESVAGTK LSISLLNTKT GFTTPWHCSV AQLANGEWIS APMGEFRKDD
RLELVYADGR PSHFREKPRE GDAFGISEST ASYLQRPKRL RASEYLGATL PSVPVSPGMS
SPSAASTSSS GASMQGSAAT TPETHSPPTF TWSGLEIVAE DNSNNASVPY GRRLIPQIMD
SLAATEPERI VFSLATFSGD SLEFRPISAR TFANAIDKTA WWLHNQVGRP DSIQPVGYIG
PHDLRHVLLT YACVKAGYAA LFLSPKNSTE GALAVLEATK CDLWINACDV SPVPLVKEVL
QKRPMNVLQL PQLDELLDAV STDPFPYTKK FDEAINDPFC FLHTSGTTGV PKPIPWSHGL
IGTMDAVRLL PPGADGDLPP WTTDWKTGDT IYSSFPMSHG AGIIMNILMP ALFNLHCVFG
PAGVLPNINL VDALAVSTRI DIWSMVPSLV DELGETPAVL SKLKSSKFIC ASGGPVSPVS
AGKVNEVIRV LNLTGTTEGL FMGNLIPPRE DWFWFCFHPY SGFEFKQVEP DTYEHWVHRN
EHWPLFQGIF HTFPEKQSIN FKDLYVRHPT KPNLWAFKGR SDDLVTEAFI TTHPAIKGCL
VFGTGKPQAG LLIELKDPLQ KTDELLDSIW ETVQQANSMS RHKNQLLRDF VAFATPDKPF
CRTDKGTVKR SATLKLYADY IERFYRSRND DLGGTFDFDM SSAHSIEDNV RKILAASLPD
VQEASADTDL FALGLDSLGV FAAIKTIRAA TGLGDQIGPR HIYANPTIAR LSAIIALLAA
AAESASDTTL CERPVDDVGA QIARMIAQHK ARQSFSLNAF DYVNPNHGMG LVLYFPIRDG
VSYEQVFANL QAGLNRTFDL IPALSGKMTD CSEQGIGYTK GDLCVTIPPL AKADSARNRL
VYKDLSAVLP SFDDLRKGGF APSAFSDTLA NFVSGGCILA VDLNHCCLDG LGAMVALKAW
AENCRYLQGD QSATCGWYDP ESFNHSLPEI LHRQEGWARP LHEIDPGTWG FLPFFPPEDE
ETNPRCEKAT EGSLPARPIF PLHPVWPLPR AERCLKTTMF LVTPEKLELL QQDVIADPAT
NGITPSISDI VQAFFWRAAI KARYRVATEI RKQKFSPDAV SILELPTDTR PHFSSRLPPT
YMGSMLILNR TSMPIETLCS AETSIAKVAL LLRQSAARIT PSLVHDAFTL LQSLPGHRRF
STANMGLEHM HAMISNMLLF PTSEIGFGDA FFANGGVPET MRPQLERGNG RFRFLAVFPL
RKDGGVELVL GTHREELEML VTDEEFTRYA RMVDTCC
