CAZyme Information: PHYCI_71361T0-p1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: PHYCI_71361T0-p1
• CAZy Family: GT1
• CAZyme Description: Cdc2-related protein kinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1778		196971.02	7.5724

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcinnamomiCBS144-22	26201	1048749	70	26131

Full Sequence      

MTFSRRVRNVCAIATLFAAVIIPQVDAWLPPIIAKGNKFFDSDTGLEFRMKGMAYYPRPN
SGELASVSNYDWAADEHEAVWKPHLEIMKDLGVNTIRLYSVDPSVSHDKFMCACSEAGIY
VLVGISAPCENCSIQDLEPPNCYPDELFTRGQMVYNAFSVYDNTLGFSVGNENNLQVKYG
ASGTTTAPCVKAFLRDMRSYAASCSGSVRQVPMGLDIADIPPRWQWISYYDCAVNDDENT
RAEWMGFNPYVECDPATHTKYSQSSGLVTLMAEYANVKYARPLMFGEFGCNKGANTIDGY
ENQREFYDAKWMNEEKDMTTEIVGGNVFEFSTELANLVDKTALTKTADAGKYGVGYFQPD
DCDHDKVACEFTPYPEYDNLKKAYTTTANSTVTHDSFNPSRTKILTCPTTMSINLPPTPT
NVTLLACTALQPVCNGSSANSYKHTDSSTSMGEKRTPSNGEGASALASSSSSGSSKKSAA
TTATPAASVAALLFSAAIAVLLDIVRSVGASTFVIPCCSHGEELLALSQPQPQPQPLGRA
RGAGRQQHELRPAAGAAPRAAHRAQRVPAAAPGARQGYETDENDAEEDQEVGEKQYVQLK
ENGWQLYCPPEEREGDTVFAIPKKRLLPTSSGRSSAAGSREPSPKREVMSQSPVDTPSPV
AMAKLESSFTTAKKNQYGEPLDRDGKIVSKTLLVKFLPKEYDARGLRSLFVSRKHPNALV
DADVFHFLDGTGWALVELESNELAASFRRTLDRRNLLDKMLRVYQAGAKELENYRYQKGK
VQVMRQQASTDKNNTSPSEEKENVQVVERQDPYCFGRKLNWLVTEEELKNLSVQQVLSAS
LEETLRVKYVKSIFHIAKGLRLDREDATSAIIALNRFFTFHAMPMEVDIYAATMLHLFLK
AHARNVPWTAFVKEVYKAKHGAAAAERLTAASPELGVLKRHLVKAEGELLEGLHYDVTGE
DPYALLDLLTTRKSSKKLVTMSQDGFTQQVTPFLSSLPPPEVQKEAKHLVAEALPLPIWT
RTPVECVMLSVVYVSAAVTEALSPSSATPMTRIPDFLPQLDLQANTSEARMLLDCSLSIC
TQLKDRWLRLEKQSKASQQQKQKQKQNQTKNADSSEFDLEQFAVSKDKKDVEISERITRL
LKHWINLPTPTVPSVLSVASAVSSVPMGMRNFGVTAPTQSGVKNFITFKAMGSSVPVPSS
STGQINEAEAVISALSIFPQKSAASDTIVGDTRLHTDEITKVESIRKRAFLGIISSEVNL
DLAGQSVYLQSWPYLEQEVFFTEERGINEACLRELSAATTLSSLLPDRFMKLYGIIFPAD
RKDRQANESGATSNKPSSTATTVDELDLLAATIDDDGNPLPEGIDRLTRQKHYLAFEQPL
HMFSGIFEAHVSLTPELRKKAIFDMLQSLSAVHDQGYVHRFVAPSHLLVFKNGIKLGGFH
AMRKIANIKPKDGEGSSMAAYEMTDGERKEHCYGAWLYVTAPEVLLGETKYSWRADVWSA
GCVALAILLEKVPFLQGPDIKVQLDLIYRLCGTPSSSWEGAHKLPLYSTFRPKHEYKMRL
RKTLLEQRSKFPEFPEDAVEVLEAMLQLDPSRRCTVKKLLEMRYFDSVRSNGRTFDFSGL
PSTFPVQKKKLVQHLLKSKAKKHRSAGSSSRSSGSARPSHHHSSHRHSNSDHHRHKRSAS
SAHDGSSSGGDKSSHHDRHRPRTDKRKSRSLSTSRREVKHAMEDVEMQDASEYVPLPASF
TASAGYSPSQPMVDTDDSLPRREKRVKLGWGMGLNSES

Enzyme Prediction     

No EC number prediction in PHYCI_71361T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH72	29	336	4.6e-72	0.8942307692307693

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397351	Glyco_hydro_72	5.33e-57	26	388	6	315	Glucanosyltransferase. This is a family of glycosylphosphatidylinositol-anchored beta(1-3)glucanosyltransferases. The active site residues in the Aspergillus fumigatus example are the two glutamate residues at 160 and 261.
270832	STKc_CDK9_like	2.46e-35	1373	1605	80	291	Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like 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.
270823	STKc_CDK_like	8.15e-34	1367	1605	68	282	Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like 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.
270833	STKc_CDK7	5.88e-31	1405	1605	111	285	Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 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.
270847	STKc_CDK12	3.26e-30	1373	1600	92	297	Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ24052.1|GH72	UIZ24052.1|GH72	0.0	1	1778	494	2516
AIG55825.1|GH72	AIG55825.1|GH72	1.76e-161	26	444	24	444
AIG56180.1|GH72	AIG56180.1|GH72	1.16e-159	28	464	42	482
CCA15748.1|GH72	CCA15748.1|GH72	2.87e-139	27	459	2186	2612
AIG55538.1|GH72	AIG55538.1|GH72	7.36e-137	17	419	15	432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6B3E_A	6B3E_A	1.77e-26	1373	1608	94	307	Crystal structure of human CDK12/CyclinK in complex with an inhibitor [Homo sapiens],6B3E_C Crystal structure of human CDK12/CyclinK in complex with an inhibitor [Homo sapiens]
4UN0_C	4UN0_C	2.00e-26	1373	1608	98	311	Crystal structure of the human CDK12-cyclinK complex [Homo sapiens],4UN0_D Crystal structure of the human CDK12-cyclinK complex [Homo sapiens]
5FIH_A	5FIH_A	2.42e-26	30	291	34	279	SACCHAROMYCES CEREVISIAE GAS2P (E176Q MUTANT) IN COMPLEX WITH LAMINARITETRAOSE AND LAMINARIPENTAOSE [Saccharomyces cerevisiae]
2W62_A	2W62_A	2.42e-26	30	291	34	279	Saccharomyces cerevisiae Gas2p in complex with laminaripentaose [Saccharomyces cerevisiae],2W63_A Saccharomyces Cerevisiae Gas2p In Complex With Laminaritriose And Laminaritetraose [Saccharomyces cerevisiae],5O9O_A Crystal structure of ScGas2 in complex with compound 7. [Saccharomyces cerevisiae S288C],5O9P_A Crystal structure of Gas2 in complex with compound 10 [Saccharomyces cerevisiae S288C],5O9Q_A Crystal structure of ScGas2 in complex with compound 6 [Saccharomyces cerevisiae S288C],5O9R_A Crystal structure of ScGas2 in complex with compound 9 [Saccharomyces cerevisiae S288C],5O9Y_A Crystal structure of ScGas2 in complex with compound 11 [Saccharomyces cerevisiae S288C],5OA2_A Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_B Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_C Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA6_A Crystal structure of ScGas2 in complex with compound 12 [Saccharomyces cerevisiae S288C]
2W61_A	2W61_A	2.42e-26	30	291	34	279	Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant) [Saccharomyces cerevisiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9Y7Y7|GAS4_SCHPO	sp|Q9Y7Y7|GAS4_SCHPO	3.34e-35	7	333	3	301	1,3-beta-glucanosyltransferase gas4 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gas4 PE=1 SV=1
sp|B0XT72|GEL1_ASPFC	sp|B0XT72|GEL1_ASPFC	1.50e-33	14	336	15	300	1,3-beta-glucanosyltransferase gel1 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=gel1 PE=1 SV=1
sp|B0Y8H9|GEL2_ASPFC	sp|B0Y8H9|GEL2_ASPFC	2.18e-33	2	348	4	319	1,3-beta-glucanosyltransferase gel2 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=gel2 PE=1 SV=1
sp|P0C954|GEL2_ASPFU	sp|P0C954|GEL2_ASPFU	2.18e-33	2	348	4	319	1,3-beta-glucanosyltransferase gel2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=gel2 PE=3 SV=1
sp|P0C7S9|GEL1_ASPFU	sp|P0C7S9|GEL1_ASPFU	1.61e-32	14	336	15	300	1,3-beta-glucanosyltransferase gel1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=gel1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000458	0.999519	CS pos: 27-28. Pr: 0.9745

TMHMM  Annotations     

Start	End
7	29