ID G3Y092_ASPNA Unreviewed; 2448 AA.
AC G3Y092;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=CNH domain-containing protein {ECO:0000259|PROSITE:PS50219};
GN ORFNames=ASPNIDRAFT_128609 {ECO:0000313|EMBL:EHA23803.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA23803.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA23803.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA23803.1}.
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DR EMBL; ACJE01000009; EHA23803.1; -; Genomic_DNA.
DR STRING; 380704.G3Y092; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1087026; -.
DR HOGENOM; CLU_228166_0_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013745; Bit61/PRR5.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR PANTHER; PTHR12894; CNH DOMAIN CONTAINING; 1.
DR PANTHER; PTHR12894:SF27; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR-ASSOCIATED PROTEIN 1; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08539; HbrB; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF10366; Vps39_1; 1.
DR Pfam; PF10367; Vps39_2; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1542..1566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1573..1596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 440..801
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 469..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1625..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1951..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1646
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1906..1921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1975..1990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2010..2034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 288
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 211..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 2448 AA; 269742 MW; 9588D7C6BE637794 CRC64;
MVGLPARGKS LIAGKAMRYL AWVGIPARVF NVGSYRRAGT PQPNANFFDP HNTEGEKMRR
AAAEAAVSDM LQWFQSGKGV VAILDATNST KERRRWIHER CQEANVETLY VESICDDEDL
IMNNILEVKT TSPDYKGQDP EVAALDFRNR IRNYEKVYET IDDNEKHFTY VKLINVGSTV
IINQIKDYLS SRLVYYIQNL HIKPRSIWLS RHGESEYNLT GKIGGDSNIS ERGEAYARAL
PGLLKKSGVP PNTKIVIWTS TLKRTIQTAR HLAAETGFEK LEWKALDELD SGVCDGLTYE
QIAEKYPEDF AARDEDKYNY RYRGGESYRD VVIRLEPIIM ELERSENVII VTHQAVLRCI
YAYFLNTPQE QSPWMEVPLH TLIKLTPRAY GTEEQRFKAD IPAVSTWRAK GTKDITKAKK
KKMLSAFTAR PLVELKPRDR SRIESVLAYG DRVLAGLNNG SLRIYRVNEQ EEEPEEGEEG
GEGQQHEQHG QDTGKGGKKD TDQQGNGNGE AGIITNGTTN GTREHKKPTE LLREVEKFSR
YKIEQLALIK EAKVLVSLSG GYVSLHDLGT YALQEQLGKT KGATTFAVTS NIENDSETGV
PAIVSRVAVA VKRKIMLWVW RDMEMEGGVP MEMTLVSGIK TLTWVSGTRL VAGLGSGFVM
VDIEGGSGGT VTDLTGPSGI GGLGGQESTG RLAGVGVASM SYMGLGGSAP KPLATRLKEG
QVLLAKDINT HFIDVQGNSL GRRQIPWSHA PADIGYSYPF LLALHDSSKG VLEVRNPETL
SLLQSVPLPS ASIMHIPQPT ISLAHAGKGF LVASDRTIWR MEALSYDTQI DSLVEKGYLD
EAISLASMLE DALLRDKQGR LRQIKLEKAE GLFKMRKYTD SMDLFTEISA PPETVIRLYP
KIIAGELSSI VEEPEESEDG TTDSQPKTQE NNNPTDAPAT EETPAPKTLS HAPSVMSLLR
TRTDDGSDAG SIRGKVVEEA KNDKALEGAD LKLAVRDLQR YLADVRRRFQ RFLNPDGTLK
VIDATTDGAN DALTDSVMKL LSIDPEGEYD LGEKLREKAR LVDTTLFRAY MYAIPALAGS
LFRIANFCDP DVVMEKLEET GRHNDLIDFL YGKKLHRQAL ELLQKFGQAD DEEETAPQLH
GPKRTVNYLQ NLSPDHIDLI LEFAEWPVRQ DPELGMEIFL ADTENAETLP RERVLDFLQG
IDVNLAVRYL EHIIGELNDM TPDLHQKLLI LYLNRLKKHQ AKEWEFSSLD DYVNWQSKFL
NMLRSSSQYS PAKILDRLDR DDPEFFEARA IVFSKMGQHR QALEIYVFKL EDYVKAEEYC
NHLHKVEDTT AADGSVSRCV ALLPYEDDKP SIYLTLLSLY LSPPHGYKPR YGPALEVLAK
HGSRLPPNSA LDLIPESLPV KELEFYFKGR MRAANTILNE SRIVANLQKA EDIKTQAQLL
VGEGTDGRST RSRHVTITEE RVCGICHKRI GGSVINVFPE FFCLRFLVVF SFEVPDLPFR
ISWPCLVQRK HTGVADISYT MIPRDSGIQG SNAYDLFSRD SFLVSLVVST LSTVSLVGAT
GSSILFHNLL SVVLLFLGFL VRDLATLCLG GLLVLFHTLG QEYVDVVLQS GLRSHLFAHT
MLRSPVSPER SSSRSPLPPP PLSQPPRRSF DDFSYARPAS SGSDASSITS NVTTISPRHS
AFNPGAVSVT SSPRPPRTSS ITANTTAPPP ISTATTNTNT SSSSSSTIRS PVSFMPHGEI
LSRKPSGRGG PPELQRRSRH HSQGFFEPSL PTASSSEATI SASRIAAQAA MLQQQQTAPQ
NPPKRPPPVR GVSEDGSRSR RGGSASPPPP PPPAPLFAPP TSSGSASGAS YQSGSTSGNT
HAATTAANVV FPRNPALQPP GLEMPVEREH KHKGEKSKMK LFSKPKHIGI SRDKDGISKD
RGLPSPSKMG FPSGGLSRIV SASTTSLADT FPSNNSSLYN LSNASASTVV PADKPVGSEK
EKEKDKDKHK HHFLSRQKLK LKDRDDHYNL PLSSASSNSK PSDPNAPQSL YSFTPASPGA
VTTTFGKSVS GLDLLHGLRD KKKEEKALES EQLDWVANSS GPAPGTFAGP SSLGSSTGVL
AEAALRETLQ GFGLNNMTPE DAWDFLKAKL MVIFDGEDVR IAIEDLNKLV LIHIQRCVQK
RMPTAVVDDL RELLETGCAS LNHTLNGIPD EKLVPHLVQV WMLFKGCGSV MNRREASEFW
ASAFNGEYAG CDLDVRNLVL IAFRDMVILY RYDVLKATFS RLSLDSIKLG TAALSVTTKS
SSNSGRPTTS ASLDGGFGSY SSQSSTLLNA ANSYSSDSLD CNRSRAASNT SNPDQLIFQS
ISSPTQRPSI IHRSSHTDTS HIITETVGRM LQCVSVLASV QTGDRAQEQI EILSKELKHN
WLGRGRTGRD RRGFVGTKIR PAIVARTDSD DYMRDGMEDY GRRELSVL
//
