CAZyme Information: EPrPIT00000016819-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000016819-p1
• CAZy Family: CBM38
• CAZyme Description: Regulator of chromosome condensation (RCC1)

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1943		215054.60	6.1624

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC0181:10364-19072(-)

Full Sequence      

MGLFGRSRRSFSSKIAEGGPDLPSGADGSGTGSSAAAAAAGKYQPQPEETKTPKSKKKED
SLDLFGADSDDSDDDATIDRYANGDVDEPLNEQQALAAESKKVSTLLSKLSPEELFRKYD
TDSSGNISVQEFLAMLPDLGINMSDAKAMRIFRKCDSDGGGEIDLNEFKMAMFAVDPVSG
NTLGFSPSSLLSPQDAFELFDTDGTGQIDELEFADVLEYFDMDVSDGKQEAIFKKYDKDK
SGFIDYKEFRAMWVRLANVREELTKRGIEIPKYATPWKLQQMLEKVLDEEEAREALVFAE
AQKFLRKQREKQRRELLGKKATVRAQDELAAALDAAGQVYIFGSGKYNQFAGEPAIRDEE
LFPGFKEVSEIWSFRVDPKPQALQESCGTVKADATADENLENQKKAKQMKSKPTGGIDEK
LVQKKKKLRKLEESKPRERDLSKFVRRRPENKRWKFQSPPKLNRQTLHTLKMKLGSNRDE
DDGDSTSGNKAESNGGNAEDRTEEPEVEHLESVCQDDIEEDNEDATKNEELAKLFFEDRE
FVRSLRFRLTKLMTNTGLLWGRGVVHATISENVALVVTSSGTILTWGGKDNSMSWDSIVK
KSAIDDVGASDSGEDEPPKVTDSLDGEILSEIVRSKVTARSAMQKMATPNQLRGMKDPEV
EAREEELIEAQLREQEENERYERLKYVMMYYNIWELPPSNATRFLFMEQVLVPKLDFEVM
LQSARLRGLELELITKMDLILTLGECFELESELRGDEGHQAFKASEERIKARCLDKHNKL
LQPEKEKLLKDDHAFEIQAARRKVQMEDTTPEYTTRGGNLSIQLSGITSRGPPLHSPRGG
TSVAGISAGGSHAALLLHDGSMYTWGNGAAGRLALQQNEAGALCYDSDHPQYVQAFQDVN
IRLVSCAHSHSAAISSDGLLYAWGSAISGKLGVGIVEDKYEQLSAIPLLVKFPGKRQIRS
VSCGAAHTGAVSTAGELFMWGCANGGRLGLGPNVTDAVVVPTLVRELSAKKKVKVWQVSC
GSAHSAVCTEIVSEFESGSKKLLGGQVLVCGGAAPLGRFVNTWELVLELDGVGIRQVSCG
TNHTAAVSAYGELYTWGRNQNGCTGHAVTLLKCLHVEPYNLAFGKPCRQISVYNEQDAQM
AVNGEISGKLAACIHTHLEDKPWWEVDLGQPAVIERIQVWNRTDEPLNPSKGRDEFTARL
FPFWILVSEFPFKDLEGKEGLRAAKVQSGAFELFKDNKRMTEWVLPTANTIGQYVRIQLQ
SRNFLHLAEVEIFGVYSAFKTVGRVGSVHCTHDATMVVVPPTSHESMLEDYYLRAIQADA
DNATILRQFTAFERSHSKFGRGDAHEVLGGTCRLCRVFRQCEICELYAETALLSKFKGED
GELPSRVVGDRKGLRGCAEAEEKGANGLESLTMMGMLNDKKRPKAQQQTGRALRAECITK
ARQAAAASQEKAPIVASAHAVPAPPATTKKQRSIHDFFAQDIVRETARKKREPAAASRIA
SADVEPVMKRIDYDSSSSGGMDDESSEANSASQTSEVAFDNSHQPKPKKIDFSSQRSEPD
GEPNEIPGSGFGSGGGAFGGRSVVSSQQGLFLENLSAPHFSRMYSQDEMDFLTPLDQPVM
HLSHPTTPSPLKKRQRRNDDEYDGDGNAVGFGVDRIREEEVQNLTQDMTHMDVCHRMGVQ
PPPSFSSDSMPSPRHFLQPTPHKFTETPAKSFLPGKRRSRPNSNEGTSSKTSFLVMESFV
NPFAPTPASDLKKKRSNRKRQSFPTTWGSGLNTAPLSKYLADFSELELIGSGSFSKVFKC
MKKIDGWMYAVKKSKRHFRGKADTERALREVQALAALSSSRHVVRYFDAWIEDDLLYIQL
ESCSGCSLGGFLNKFKPHHIPEAVLCKVLCHITQALHDMHSKKMVHMDVKIQNVLVADGE
IYKLGDLGTVAHMDGSMEITEGN

Enzyme Prediction     

No EC number prediction in EPrPIT00000016819-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM47	1129	1270	2.8e-20	0.9765625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
270899	PKc_Wee1_like	1.12e-47	1782	1943	1	163	Catalytic domain of the Wee1-like Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
270953	PTKc_Wee1	2.21e-41	1782	1930	1	175	Catalytic domain of the Protein Tyrosine Kinase, Wee1. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
271040	PTKc_Wee1a	4.17e-39	1777	1943	1	187	Catalytic domain of the Protein Tyrosine Kinase, Wee1a. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
270952	PKc_Myt1	5.30e-36	1783	1942	3	161	Catalytic domain of the Dual-specificity protein kinase, Myt1. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
270898	STKc_EIF2AK	8.71e-35	1777	1940	2	165	Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTD39109.1|CBM47	5.86e-16	1120	1276	1352	1495
ARF14915.1|CBM48	7.98e-15	818	1109	66	335
AMX03783.1|CBM32|CBM47|CBM6	8.81e-15	1061	1275	85	290
AZM48749.1|CBM47|GH29	1.73e-14	1107	1272	605	761
QOX79078.1|CBM47	2.47e-14	1120	1281	131	279

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7N3U_A	1.18e-31	1777	1943	3	189	Chain A, Wee1-like protein kinase [Homo sapiens]
2Z2W_A	1.18e-31	1777	1943	3	189	Human Wee1 kinase complexed with inhibitor PF0335770 [Homo sapiens]
2IN6_A	1.24e-31	1777	1943	5	191	Wee1 kinase complex with inhibitor PD311839 [Homo sapiens],2IO6_A Wee1 kinase complexed with inhibitor PD330961 [Homo sapiens]
3BI6_A	1.24e-31	1777	1943	5	191	Wee1 kinase complex with inhibitor PD352396 [Homo sapiens],3BIZ_A Wee1 kinase complex with inhibitor PD331618 [Homo sapiens],3CQE_A Wee1 kinase complex with inhibitor PD074291 [Homo sapiens],3CR0_A Wee1 kinase complex with inhibitor PD259_809 [Homo sapiens]
1X8B_A	1.30e-31	1777	1943	7	193	Structure of human Wee1A kinase: kinase domain complexed with inhibitor PD0407824 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A4QNA8|WEE2_XENTR	2.01e-30	1773	1930	207	385	Wee1-like protein kinase 2 OS=Xenopus tropicalis OX=8364 GN=wee2 PE=2 SV=1
sp|O57473|WEE2B_XENLA	1.05e-29	1700	1930	153	381	Wee1-like protein kinase 2-B OS=Xenopus laevis OX=8355 GN=wee2-b PE=1 SV=1
sp|Q8QGV2|WEE1B_XENLA	1.56e-29	1777	1943	242	428	Wee1-like protein kinase 1-B OS=Xenopus laevis OX=8355 GN=wee1-b PE=1 SV=1
sp|Q6DFE0|WEE2C_XENLA	1.87e-29	1700	1930	153	381	Wee1-like protein kinase 2-C OS=Xenopus laevis OX=8355 GN=wee2-c PE=2 SV=1
sp|E1BTE1|WEE2_CHICK	2.09e-29	1776	1943	210	399	Wee1-like protein kinase 2 OS=Gallus gallus OX=9031 GN=WEE2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EPrPIT00000016819-p1.