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CAZyme Information: GAQ06282.1

You are here: Home > Sequence: GAQ06282.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aspergillus lentulus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
CAZyme ID GAQ06282.1
CAZy Family GH16
CAZyme Description serine/threonine-protein kinase cds1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1515 171086.71 6.9154
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AlentulusIFM54703 9916 N/A 259 9657
Gene Location Start: 1033083; End:1039127  Strand: +

Full Sequence      Download help

MEATQESTQP  CTDPRRIGRN  NSGLLEEDVS  DIICILHPTS  LAAHEAVAAT  ASLAPQHILQ60
KDELEYEDPD  TAALDIALRL  SSNVRNINLG  FCFGRNRSRC  DLLLAPDDNA  KRISNTHFRI120
HLTGDGILML  EDLSTNGTVV  DDCRLRKNQK  ENSRMLTNGS  VIQVLRGNNA  SDEVRFVVRI180
PSRDGYAMRY  TENMLRYLER  VQRQPAGAMQ  KNRQGSVRPS  LEWTVANAYG  MHWTGGSMYN240
VTGQIGKGAF  ATVYKLATKQ  HGAVYAAKEL  DKRRFMKNGI  LDQKVDNEMK  IMKDLKHPNI300
VQYIDHHEHD  RWIYIIMEYV  PGGELSTYLS  THGKIPEDMV  KMLARQLLHA  LQYLHKRRIT360
HRDIKPDNIL  IASLEPLRVK  LSDFGLSKVV  QEETFLKTFC  GTLLYCAPEV  YPEYENYRRG420
EVRKRRRLGD  PPPKTSPYDQ  SVDMWSFGAV  LFHILSGTPP  YTGRGDDRGS  QMLRNIMTTD480
PDYDVLRREG  VSEAGVDFVR  RLLNRDPHSR  PKESECFQHS  WIRDVPDVDE  YDDNDIQPAD540
FGALSDIGED  LENELDASQI  SLNDNPEPVL  TGDESHDSND  LAQSKRPRID  HLPADIHYPS600
LPNIESFPAA  RPIPETTPRR  LFGEITSSAL  RSSNVFGASM  NAFGGDDLSV  HDFVSSTGES660
IISDGNSLNS  VLSLPDNPFA  GSAPSLMGAE  NLVGQLNMNS  WHPGTSAHGP  PAATELPALK720
TSVDEGVGGS  PGPELNKETH  PSTSTPKGAK  FSRRIELPLP  DTASERSSRE  ITRENSKAPS780
DKPEASAGEV  FDIELAVTID  ARTGRQISHP  PEGIVSDTTS  AALRHEMPTE  IPPTISLHRH840
EQPRPLLGKL  TTLPGSIFDL  TIRLEDRMTS  WGRGPLATIC  HPDPMDTRIP  AYALEVTFWA900
PAIEAQIAAG  RNWMEVPGVM  AILSTKTRKC  IWVNDTELRR  GSEGSSTREG  FHFGKLYTGD960
IITIYRHRNK  FLKFQCEFYH  GDSARSRPEE  EKGFVVRKVL  MSKEGVAANR  LPVRKDNDGG1020
KKQGINPKTS  AIYENLRADL  FTIFNLPDGL  DTPMSLSRSP  SPHPGGGWSS  PGLTPGSGTS1080
TPRSGFLSPN  SLGPSGISWA  AARAKSDEVR  GYPSFSTRNN  GFFSRSKRKI  TSSLPRFRMN1140
GSARNGYVDK  DEYWRGHNSS  EAGLRFGFAR  GLMRRRRSRA  FLALIVLVLG  YLFFWTAIVQ1200
SYRRSSFGGG  RKFVIILPSN  VEGGVMEWKG  AREWAIERNS  ISNKEEYAKR  WGYELEIVNM1260
LAKKRYSHEW  RESWEKVDII  RDAMRKYPNA  EWFWWLDLNT  WIMEYSYSLQ  DHIFDRLGEL1320
TYRDINLYNP  LNISHPPTAP  YLDELSRSAE  GDGNPSSIEL  LLSQDCGGFN  LGSFFIKRSL1380
WSDRLMDLWW  DPVMYEQKHM  DWEHKEQDAL  EYLYQSQPWI  RSNVAFTPQR  YINSFPPGAC1440
GEGGDPDVHY  SVKDRDFMVN  MAGCQFGRDC  WGEMYLYREL  SKKLNRTRWQ  RLKDGLGELY1500
SRLLPKEDKP  QEQQQ1515

Enzyme Prediction      help

No EC number prediction in GAQ06282.1.

CAZyme Signature Domains help

Created with Snap751512273033784545306066817578339099841060113612121287136314393245GT34
Family Start End Evalue family coverage
GT34 1212 1472 1.7e-85 0.983739837398374

CDD Domains      download full data without filtering help

Created with Snap75151227303378454530606681757833909984106011361212128713631439239522S_TKc239521STKc_CAMK12121470Glyco_transf_34239521STKc_Rad53_Cds1244522STKc_MAPKKK
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
214567 S_TKc 4.33e-86 239 522 1 254
Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily.
270687 STKc_CAMK 2.30e-83 239 521 2 258
The catalytic domain of CAMK family Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
368535 Glyco_transf_34 2.68e-80 1212 1470 4 238
galactosyl transferase GMA12/MNN10 family. This family contains a number of glycosyltransferase enzymes that contain a DXD motif. This family includes a number of C. elegans homologs where the DXD is replaced by DXH. Some members of this family are included in glycosyltransferase family 34.
271000 STKc_Rad53_Cds1 3.11e-74 239 521 2 265
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
270783 STKc_MAPKKK 5.75e-70 244 522 7 258
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

CAZyme Hits      help

Created with Snap7515122730337845453060668175783390998410601136121212871363143910541508QRD89754.1|GT3410541508QMW42907.1|GT3410541508QMW30853.1|GT3410541508UDD59694.1|GT3410541508CAK42408.1|GT34
Hit ID E-Value Query Start Query End Hit Start Hit End
QRD89754.1|GT34 9.26e-233 1054 1508 1 458
QMW42907.1|GT34 9.26e-233 1054 1508 1 458
QMW30853.1|GT34 9.26e-233 1054 1508 1 458
UDD59694.1|GT34 9.26e-233 1054 1508 1 458
CAK42408.1|GT34 1.88e-231 1054 1508 1 457

PDB Hits      download full data without filtering help

Created with Snap75151227303378454530606681757833909984106011361212128713631439855245XZV_A2455264PDP_A2395253BHY_A2395231YRP_A2395252J90_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5XZV_A 1.81e-62 85 524 60 468
Crystal structure of Rad53 1-466 in complex with AMP-PNP [Saccharomyces cerevisiae S288C],5XZV_B Crystal structure of Rad53 1-466 in complex with AMP-PNP [Saccharomyces cerevisiae S288C],5XZW_A Crystal structure of Rad53 1-466 [Saccharomyces cerevisiae S288C],5XZW_B Crystal structure of Rad53 1-466 [Saccharomyces cerevisiae S288C]
4PDP_A 5.27e-51 245 526 39 305
Crystal structure of Rad53 kinase domain and SCD2 [Saccharomyces cerevisiae],4PDP_B Crystal structure of Rad53 kinase domain and SCD2 [Saccharomyces cerevisiae],4PDS_A Crystal structure of Rad53 kinase domain and SCD2 in complex with AMPPNP [Saccharomyces cerevisiae],4PDS_B Crystal structure of Rad53 kinase domain and SCD2 in complex with AMPPNP [Saccharomyces cerevisiae]
3BHY_A 2.63e-44 239 525 7 272
Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with a beta-carboline ligand [Homo sapiens],3BQR_A Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with an imidazo-pyridazine ligand [Homo sapiens],5A6N_A Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with compound 2 [Homo sapiens],5A6N_B Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with compound 2 [Homo sapiens],5A6O_A Crystal structure of the apo form of the unphosphorylated human death associated protein kinase 3 (DAPK3) [Homo sapiens],5A6O_B Crystal structure of the apo form of the unphosphorylated human death associated protein kinase 3 (DAPK3) [Homo sapiens],5VJA_A Crystal Structure of human zipper-interacting protein kinase (ZIPK, alias DAPK3) in complex with a pyrazolo[3,4-d]pyrimidinone ligand (HS38) [Homo sapiens],5VJA_B Crystal Structure of human zipper-interacting protein kinase (ZIPK, alias DAPK3) in complex with a pyrazolo[3,4-d]pyrimidinone ligand (HS38) [Homo sapiens],5VJA_C Crystal Structure of human zipper-interacting protein kinase (ZIPK, alias DAPK3) in complex with a pyrazolo[3,4-d]pyrimidinone ligand (HS38) [Homo sapiens],5VJA_D Crystal Structure of human zipper-interacting protein kinase (ZIPK, alias DAPK3) in complex with a pyrazolo[3,4-d]pyrimidinone ligand (HS38) [Homo sapiens]
1YRP_A 3.11e-44 239 523 14 277
Catalytic domain of human ZIP kinase phosphorylated at Thr265 [Homo sapiens],1YRP_B Catalytic domain of human ZIP kinase phosphorylated at Thr265 [Homo sapiens]
2J90_A 4.68e-44 239 525 28 293
Crystal structure of human ZIP kinase in complex with a tetracyclic pyridone inhibitor (Pyridone 6) [Homo sapiens],2J90_B Crystal structure of human ZIP kinase in complex with a tetracyclic pyridone inhibitor (Pyridone 6) [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Created with Snap7515122730337845453060668175783390998410601136121212871363143912031491sp|P50108|MNN10_YEAST12141492sp|P78817|YFE6_SCHPO85526sp|P22216|RAD53_YEAST45525sp|Q09170|CDS1_SCHPO239524sp|Q54MH0|FHKD_DICDI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|P50108|MNN10_YEAST 2.35e-106 1203 1491 112 389
Probable alpha-1,6-mannosyltransferase MNN10 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MNN10 PE=1 SV=1
sp|P78817|YFE6_SCHPO 3.29e-85 1214 1492 76 343
Uncharacterized alpha-1,2-galactosyltransferase C637.06 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC637.06 PE=2 SV=2
sp|P22216|RAD53_YEAST 3.70e-59 85 526 60 470
Serine/threonine-protein kinase RAD53 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=RAD53 PE=1 SV=1
sp|Q09170|CDS1_SCHPO 2.68e-53 45 525 6 436
Serine/threonine-protein kinase cds1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=cds1 PE=1 SV=2
sp|Q54MH0|FHKD_DICDI 2.80e-44 239 524 199 474
Probable serine/threonine-protein kinase fhkD OS=Dictyostelium discoideum OX=44689 GN=fhkD PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000067 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
1180 1202