PlantCAZyme

Basic Information
Species	Physcomitrella patens
Cazyme ID	Pp1s85_169V6.1
Family	AA7
Protein Properties	Length: 518 Molecular Weight: 57611.5 Isoelectric Point: 6.1891
Chromosome	Chromosome/Scaffold: 85 Start: 1263682 End: 1272963
Description	tubulin beta chain 3
View CDS

External Links
NCBI Taxonomy
Plaza
CAZyDB

Signature Domain Download full data set without filtering

Family	Start	End	Evalue
AA7	406	503	4.9e-24
GRAVGGGWGFSSTKFGIVSDNILGALAIANGTLVTATANQNSNLFFALCGASANSFDIVTQFTFRVHDVSFPVTHFKYTWIMKNQQFQSFKAFQTWGV

Full Sequence
Protein Sequence Length: 518 Download
MREILHIQGG QCGNQIGSKF WEVVCEEHGI DPTGSYKGVT DLQLERINVY FDEASGGRYV 60 PRAVLMDLEP GTMDSVRTGP YGQIFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV 120 RKEVESCDCL QGFQFCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV 180 EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLITP SFGDLNHLIS ATMSGITCCL 240 RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF APLTSRGSQQ YRSLTVPELT QQMWDSKNMM 300 CAADPRHGRY LTASAVFRGK VSTKEVDEQM INVQNKNSSY FVEWIPNNVK SSVCDIPPTG 360 LKMSSTFIGN STSIQEMFRR VVIHEHHQNS YTNKCDPWAM EATRFGRAVG GGWGFSSTKF 420 GIVSDNILGA LAIANGTLVT ATANQNSNLF FALCGASANS FDIVTQFTFR VHDVSFPVTH 480 FKYTWIMKNQ QFQSFKAFQT WGVEISDYIL ASLYMDP* 540

Full Sequence

Protein Sequence Length: 518 Download

MREILHIQGG QCGNQIGSKF WEVVCEEHGI DPTGSYKGVT DLQLERINVY FDEASGGRYV    60
PRAVLMDLEP GTMDSVRTGP YGQIFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV    120
RKEVESCDCL QGFQFCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV    180
EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLITP SFGDLNHLIS ATMSGITCCL    240
RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF APLTSRGSQQ YRSLTVPELT QQMWDSKNMM    300
CAADPRHGRY LTASAVFRGK VSTKEVDEQM INVQNKNSSY FVEWIPNNVK SSVCDIPPTG    360
LKMSSTFIGN STSIQEMFRR VVIHEHHQNS YTNKCDPWAM EATRFGRAVG GGWGFSSTKF    420
GIVSDNILGA LAIANGTLVT ATANQNSNLF FALCGASANS FDIVTQFTFR VHDVSFPVTH    480
FKYTWIMKNQ QFQSFKAFQT WGVEISDYIL ASLYMDP*                            540

Functional Domains Download unfiltered results here

Cdd ID	Domain	E-Value	Start	End	Length	Domain Description
cd06059	Tubulin	6.0e-130	3	380	379	+ The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins. Also included in this group is the mitochondrial Misato/DML1 protein family, involved in mitochondrial fusion and in mitochondrial distribution and morphology.
PLN00220	PLN00220	0	1	381	381	+ tubulin beta chain; Provisional
cd02187	beta_tubulin	0	2	381	380	+ The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.
PTZ00010	PTZ00010	0	1	384	384	+ tubulin beta chain; Provisional
COG5023	COG5023	0	1	381	384	+ Tubulin [Cytoskeleton]

Gene Ontology
GO Term	Description
GO:0003924	GTPase activity
GO:0005525	GTP binding
GO:0005874	microtubule
GO:0006184	GTP catabolic process
GO:0007017	microtubule-based process

Annotations - NR Download unfiltered results here
Source	Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
RefSeq	XP_001766554.1	0	1	381	1	381	predicted protein [Physcomitrella patens subsp. patens]
RefSeq	XP_001766602.1	0	1	381	1	381	predicted protein [Physcomitrella patens subsp. patens]
RefSeq	XP_001767462.1	0	1	381	1	381	predicted protein [Physcomitrella patens subsp. patens]
RefSeq	XP_001777263.1	0	1	381	1	381	predicted protein [Physcomitrella patens subsp. patens]
RefSeq	XP_001779193.1	0	1	381	1	381	predicted protein [Physcomitrella patens subsp. patens]

Annotations - PDB Download unfiltered results here
Source	Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
PDB	3n2k_D	0	1	381	1	381	A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond
PDB	3n2k_B	0	1	381	1	381	A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond
PDB	3n2g_D	0	1	381	1	381	A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond
PDB	3n2g_B	0	1	381	1	381	A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond
PDB	3hke_D	0	1	381	1	381	A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond

Orthologous Group
Species	ID
Physcomitrella patens	Pp1s128_133V6.1

CAZyme Information