ID Q0CN10_ASPTN Unreviewed; 1151 AA.
AC Q0CN10;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAU35371.1};
GN ORFNames=ATEG_04924 {ECO:0000313|EMBL:EAU35371.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU35371.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; CH476599; EAU35371.1; -; Genomic_DNA.
DR RefSeq; XP_001214102.1; XM_001214102.1.
DR AlphaFoldDB; Q0CN10; -.
DR STRING; 341663.Q0CN10; -.
DR EnsemblFungi; EAU35371; EAU35371; ATEG_04924.
DR GeneID; 4320060; -.
DR VEuPathDB; FungiDB:ATEG_04924; -.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_2_0_1; -.
DR OMA; QCYEKDY; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd09769; Luminal_IRE1; 1.
DR CDD; cd10422; RNase_Ire1; 1.
DR CDD; cd13982; STKc_IRE1; 1.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 2.
DR SMART; SM00580; PUG; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1151
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004170444"
FT DOMAIN 716..1012
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1015..1149
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 32..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 127919 MW; 88CEA9766B4576B9 CRC64;
MRWRLPGARS TLPASVALLL LPVLVAPQQL QGRQNDRDLP STVSVPLGPT VHHGHHPRSD
PLHVKSNDAS ALATLALAGS GRAVRAPPAQ ASGPSAGLAP QLHARSLQDW EVEDFVLLAT
VDGSIHARDR KTGAARWALE VPSSPTVESI YHRANRSSFD RTQPEDDFIW IVEPNQGGSL
YIYSPGPDAG LQKLGLTVKE LVDETPYSGT DPAVTYTARK ETTLYTIDAR TGTILRVFSS
RGPMPSGQEC RKVDGLDVDA EDCDSPSGTL VLGRIEYAVA IQNTETGDPI CTLKYSEWTA
NNRDMDLQSQ YFRTMDQSHI YSMHDGVVLG FDHSRMERPR YTQRFATPVV RVFDVARPVN
VDSPDAPTPL VLLSQPSQPP DPDYGSLDDR DARVFIDATN AGGWFAMSEE TYPLVTGRAK
MAQCYEKDYF RDGQPLMSLT PSQQRDALAG VHSLNGPRVI RRPIPSISGS SSVDLSNDTP
RDLMRSPSEL ALPPALRHST IIRKGWDNAV DIFVTLLLLF FGTFIYFNSH NIQELAKQKL
DIKNIISAYG QPPLSTPSTP VIDGPQLQRE KSPARPVTNV TVDMDLAEGP AGDVTPKPKK
ARNAPAPDAT PRVRIREPSR GPDGDEDVDD LALDGADDTE KPKKKARRGR RGGKAHKRGK
KPGTEGENKE QADRVVNELS NLRPPSRLET DVQLSRTVSN EIIEMDGLVQ IGRLKVNTDI
VLGHGSHGTV VYRGAFDGRD VAVKRMLVEF YDIASHEVGL LQESDDHNNV IRYYCREQAA
GFLYIALELC PASLQDVVER PFDFPQLVEG GLDMPDVLRQ IVCGVRYLHS LKIVHRDLKP
QNILVAMPRG RSGSKALRLL ISDFGLCKKL EDNQSSFRAT TAHAAGTSGW RAPELLVDDD
KSPAIQSVES QHTESSEPAV VDPQTNRRAT RAIDIFSLGC VFYYVLTRGS HPFDKDGKFM
REANIVKGNY NLDELDRLGE YAFEAHDLIR SMLSLDPRQR PDASAVLTHP FFWSVSDRLA
FLCDVSDHFE FEPRDPPSDA LLLLESVARR VMGPEMDFLR QLPAAFKDNL GKQRKYTGSK
MLDLLRALRN KRNHYNDMPE HLKAHIGGYP EGYLNFWTVK FPSLLMSCHW VIVELGLTRI
DRFKRYFTVP E
//
