CAZyme Information: PHYBL_186111T0-p1

Basic Information

• Species: Phycomyces blakesleeanus
• Lineage: Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
• CAZyme ID: PHYBL_186111T0-p1
• CAZy Family: GT15
• CAZyme Description: Phosphorylase kinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1436		161472.93	5.8367

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555	16528	763407	0	16528

• Gene Location: location=PblaNRRL1555-_SC06:986819-991688(-)

Full Sequence      

MAHFNRKHSLERLDYYYQVINATVLSKQSAASGLIPASVAITNHGDYTDAWVRDNVYSIY
CVYGLALAYRRLDDSSGRTFELEHSVVKLMRGLLFSMMRQADKVEKFKKTQDKLDSLHAK
YKTETGATVVKDNEWGHLQIDATSIFVLAMADMTTGGLNIIFTQDEVDFVQNLVFYIERA
YRTPDFGIWERGNKSNHGQPELNTSSIGMAVAALRAINGVNLFGARGGPSSTIYVLPDEL
TRNATTLQSVLPRESNSKEIDGSVLSVIGFPAFACTDPELVKRTREDAKMKLEGKYGWKR
FLRDGHQTVVEDTSRLHYNDNELKAFEDIESEWPLFFTYMVLDGLFTGDMEQVEEYRKKL
EPTIIDSAHWDPNNKIFNEDREPCADGDTGKLHIPLLPELYYVPCELIEAEKANPHSQKR
LPNDNTPLVWALSLYLLGSLIYENLLSPSEMDPLGRRFNINAQKRETITQIVLLSESPEL
QNKLAMYGLETQSVDQISSSITVLPPKALADVYHALGQNSKLGLTGRPKRPVGVLGTSRL
YRIEGHIYVFTPHFMDSETFYLNSDPDFLISAFENELAFCSDNWLYAGRPTIVVVLSEAM
LGNLQSSSMATPGGSGFDSSRKNLLNFFMNLRSGDCNGTRVRLSRLSETINTSNIESLDF
LIDKPELDWESILLVNKSAHYGSSSHRKLGYNESKTQASTPGGFTPGNKTPKRRNTAFQG
KSLGTPLDKLHDEGYFQDIATALSNLNSSEPKFRLKDHEDSPLLSATRKGAVADGAVLSK
LPETGGTVHLGGQEEIHERSQSPLSTDVSPTTTEMLSLTLGDRSQFGQAVASLASSVNLY
DQIDLLQYMASCDHLDSYISELQASLKELLEEVYLKAVRLQYWSIARQATGLLHKIVPAL
TINITDLVIRQKQISIGSGHKEILITTPVGPETLAKMFVEQCSDDVREGPVVQEIIIYLG
SFVRTTPYMFDGILRLRTHYIIIALREEISRMNNCDEEEAIEHLMQLSPYELQSLLGTIL
SGPTLCDSGSSIMIRDKPGGFLMLSRFTDHWRRSSLGSEHQSFIPILPPPSDGHADRTQL
IIRAQSGGYMAGNFARVEINGNTMFANSRGIHVWAIDRPQKIILEHASFDTHISSEESDA
FAKFIGWLKPGMIVVIASRDDFSEHLTSDAIKALENLGSKRIRDVKYRDSYVFIGEKGGP
VEKITEAHKAAHEGPTDTIELSVKLDEKPERDQEVTQDNIISFFPNASGRWLRRRKNDGA
LNRVPAHFFPQTWKVLDRSRGIQIFSHCLPRDPTVLEMTPEEYNFALAVEGFLGWFTDPA
ERQIAVEVLALIYRFQTSNPKTRTADTVMDIPVIMKKAREIFWYKWVESNKAQFEKSKLF
SKGFDYEEHKDLVRRLFYDLPIEGTESTSAYLRKAIVSVLPFETDNIDNQNSEKCS

Enzyme Prediction     

No EC number prediction in PHYBL_186111T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	16	314	7.2e-18	0.7728531855955678

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	2.25e-63	12	459	3	294	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
406202	ILEI	5.18e-29	1109	1198	1	89	Interleukin-like EMT inducer. ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fibrosis. ILEI is upregulated exclusively at the level of translation, and abnormal ILEI expression, ie cytoplasmic over-expression instead of vesicular localization, is associated with EMT in human cancerous tissue. In order to induce and maintain the EMT of hepatocytes in a TGF-beta-independent fashion ILEI needs the cooperation of oncogenic Ras.
260110	PANDER_like	7.52e-27	1082	1225	3	149	Domains similar to the Pancreatic-derived factor. FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a regulator of glucose homeostasis and beta cell function. The protein is expressed in the endocrine pancreas and co-secreted with insulin in response to glucose, particularly under conditions of insulin resistance. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3B designation. This wider family contains FAM3B and FAM4C, N-terminal domains of N-acetylglucosaminyltransferases, and domains in poorly characterized proteins that have been associated with deafness and the progression of cancer.
260112	PANDER_like_TMEM2	1.62e-23	1078	1208	22	150	PANDER-like domain of the transmembrane protein TMEM2. TMEM2 has been characterized as a transmembrane protein that maps to the DFNB7-DFNB11 deafness locus on human chromosome 9. It contains a domain similar to the Pancreatic-derived factor PANDER, C-terminal to a glycine rich G8-domain. The function of the PANDER-like domain in TMEM2 has not been characterized.
260111	PANDER_GnT-1_2_like	8.08e-15	1089	1202	6	123	PANDER-like domain of N-acetylglucosaminyltransferases. O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 participates in O-mannosyl glycosylation and may be responsible for creating GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moieties on alpha dystroglycan and other O-mannosylated proteins. The domain characterized by this model lies N-terminal to the catalytic domain. Its function has not been determined.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS03190.1|GH0	0.0	10	1198	15	1235
ULP73450.1|GH0	2.74e-249	12	1053	10	906
BAY93985.1|GH0	8.39e-248	12	1021	10	861
BAZ72317.1|GH0	2.34e-247	12	1021	10	861
BAY97175.1|GH0	2.34e-247	12	1021	10	861

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GGJ_A	5.63e-11	1097	1201	26	134	Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Man-alpha-pNP [Homo sapiens],5GGJ_B Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Man-alpha-pNP [Homo sapiens],5GGK_A Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Man-beta-pNP [Homo sapiens],5GGK_B Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Man-beta-pNP [Homo sapiens],5GGL_A Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-alpha-pNP [Homo sapiens],5GGL_B Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-alpha-pNP [Homo sapiens],5GGN_A Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta-pNP [Homo sapiens],5GGN_B Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta-pNP [Homo sapiens],5GGO_A Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GalNac-beta1,3-GlcNAc-beta-pNP [Homo sapiens],5GGO_B Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GalNac-beta1,3-GlcNAc-beta-pNP [Homo sapiens],5GGP_A Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta1,2-Man-peptide [Homo sapiens],5GGP_B Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta1,2-Man-peptide [Homo sapiens]
5XFC_A	1.92e-10	1097	1201	26	134	Serial femtosecond X-ray structure of a stem domain of human O-mannose beta-1,2-N-acetylglucosaminyltransferase solved by Se-SAD using XFEL (refined against 13,000 patterns) [Homo sapiens],5XFC_B Serial femtosecond X-ray structure of a stem domain of human O-mannose beta-1,2-N-acetylglucosaminyltransferase solved by Se-SAD using XFEL (refined against 13,000 patterns) [Homo sapiens]
5GGF_A	1.11e-09	1097	1301	21	201	Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form II [Homo sapiens],5GGF_B Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form II [Homo sapiens],5GGF_C Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form II [Homo sapiens],5GGG_A Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form I [Homo sapiens],5GGI_A Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Mn, UDP and Mannosyl-peptide [Homo sapiens],5GGI_B Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Mn, UDP and Mannosyl-peptide [Homo sapiens]
7ECQ_A	1.98e-07	1109	1221	48	164	Chain A, Protein FAM3A [Mus musculus]
2YOP_A	2.16e-07	1108	1212	61	164	Long wavelength S-SAD structure of FAM3B PANDER [Mus musculus],2YOP_B Long wavelength S-SAD structure of FAM3B PANDER [Mus musculus],2YOP_C Long wavelength S-SAD structure of FAM3B PANDER [Mus musculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8BWJ3|KPB2_MOUSE	6.43e-219	5	1420	3	1223	Phosphorylase b kinase regulatory subunit alpha, liver isoform OS=Mus musculus OX=10090 GN=Phka2 PE=1 SV=1
sp|P46018|KPB2_RABIT	9.01e-219	5	1420	3	1223	Phosphorylase b kinase regulatory subunit alpha, liver isoform OS=Oryctolagus cuniculus OX=9986 GN=PHKA2 PE=2 SV=1
sp|P46019|KPB2_HUMAN	2.49e-218	5	1420	3	1223	Phosphorylase b kinase regulatory subunit alpha, liver isoform OS=Homo sapiens OX=9606 GN=PHKA2 PE=1 SV=1
sp|P18688|KPB1_RABIT	7.26e-218	5	1415	3	1220	Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform OS=Oryctolagus cuniculus OX=9986 GN=PHKA1 PE=1 SV=1
sp|P18826|KPB1_MOUSE	8.10e-218	5	1415	3	1224	Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform OS=Mus musculus OX=10090 GN=Phka1 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999233	0.000764

TMHMM  Annotations     

There is no transmembrane helices in PHYBL_186111T0-p1.