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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 412258 |
Family | GT2 |
Protein Properties | Length: 1631 Molecular Weight: 184557 Isoelectric Point: 7.181 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT2 | 1113 | 1287 | 4.8e-27 |
IFLPCCKEPTDVPEDSIQAALAMDYPKHQFRVLVLDDGGDDQLKQYCEVLEHVEPPSASVRYLRRVKIPGVPHNFKCGNLNYGLEHSDAEFVVMMDADMI LHPSFLKTLLPHIVKDPKVSFVQIPQSFYNLPVGDPLNDACGFCYERLMIHRDTFGAAPCVGTGAIFRRKHLDEI |
Full Sequence |
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Protein Sequence Length: 1631 Download |
MATVKNWVNA SLKPKDKEAI SSASRSCSFC GLKGHSVMDC SETLECELKE LERRALILED 60 MSSEVLDFPC LRCLGMDTWE LSVDSRSPRW RLELERTQRL KPSVTSVTVP ANPSLVLVDH 120 AKAIPAASIP PVVWTQSTSL VPQSGNLSIA LLHEPDHKVA RAKDQRKNEE SPKGNTHKKV 180 GLQRTGTPAK KAAAPQTSET LPSVPKDMLA AIESVRLSRS ELWRWMDSPD FNTNVRGFFL 240 RLRFGRWEKD LGGTGYRMAR IRGAIRKLGG DDKNMSVSVD LGDMECTVDS QYVSNHSFTE 300 RLRRVAWLKE DLTPPAQEEI EQKWCLTVPA IWSDQAKGSM QVYAERANRG AKNDTVSERE 360 AVTRTFVPLN KSDIIMGISL LGSSKSRLRG VLEKFLVADV GGIIDIIVHE KESAQDWIIH 420 KVHEACASSG ALGGGTYVDS NFLEFLRKKI GCFDTFKQQE PDVVHRILSW WLGPKGKCTF 480 DGSGSKFLEI PAKLSKAWKK HDKAELGFPE SSDYYDEIEI RCEQMKAIFD TEADKTIKLI 540 DEKLRKVDNV KYILLVGGFS ESRYLFNRIR FEDLVSPPNP GSAVCRGAVA LGVGTGVDDP 600 PASKSIDNYG IERCSVFSLY VKKDESVSEN QEITHSFFPI YTDQKALRID LLISSSSNIP 660 DYSMDINEDL ELGTSRQVAV TMYFGRSNIE VSAQRVNFGM NRGLERLYSV EFDAAQTYVN 720 KVHEARASSG ALGGVPPKLP KAWKEHDREF DTGNWDLLQR DDECYHEIEI DCEEMCAIFD 780 TEINKTIQLI EENFDKVDGI KYIYLVGGFS ESPYVVKRIK VQFEEAVEAV HCPFNPTAAI 840 CRGAVALGTG TGVVLSRISR KSYGISTSHI FRWDVDPPEY KFLDFFEIER YQNVFFKVFV 900 KKDEPVTEDQ LVTHSFFPLN HYSFDIDEDL HLDTDPEVAV TIFSGRSSIE VSARRINFGS 960 NCESRGSIGR FSKDLELQQQ PSDNLSDQSD SNAPHESSSS SSSPSSSPSS STSLSAAPQA 1020 SPWGKLIWHT IICLLVSAHM ATFVNYLGYR FYVYSKHPGE FVRRPWLIIL TICEVIYFLN 1080 SVIGAVDLVL PPRIWRPRQS LSLNWEDLPT VDIFLPCCKE PTDVPEDSIQ AALAMDYPKH 1140 QFRVLVLDDG GDDQLKQYCE VLEHVEPPSA SVRYLRRVKI PGVPHNFKCG NLNYGLEHSD 1200 AEFVVMMDAD MILHPSFLKT LLPHIVKDPK VSFVQIPQSF YNLPVGDPLN DACGFCYERL 1260 MIHRDTFGAA PCVGTGAIFR RKHLDEIGGF QPMSITEDTT TAFKLFNQGF KSVYLNRNLQ 1320 IGLIPWTFEG YIKQRQRWCQ GAIQQFSATW REMLGPKSKL SLVLKVSFFW HTGYYFIAIV 1380 NLVMLLLFIV CLALHLDLMI GTSHEAWRVI IQLAIFLIFW RLSWMSVWLS LPQSIRSRNR 1440 DESHFWWMTP FFLQTIYKSI FSYSSTFTFT PTSSIDRVAA QAKLTKQPAL IKIFLVKLKH 1500 VKVHIIYILL VLAVVAYRIS WVAKQRGRNC SHDFYVIAMS FFLLSTWTHM LVPIVYILCP 1560 PSYKPGQRKG LLHYREKVPH FVEGDHLPKW HWSAMFYEAI ANVVVVIFWV AALVIAVTKA 1620 VCQWCKTGAI * 1680 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10229 | HSPA12_like_NBD | 3.0e-18 | 723 | 842 | 123 | + Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins. Human HSPA12A (also known as 70-kDa heat shock protein-12A) and HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2) belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A or HSPA12B. The gene encoding HSPA12A maps to 10q26.12, a cytogenetic region that might represent a common susceptibility locus for both schizophrenia and bipolar affective disorder; reduced expression of HSPA12A has been shown in the prefrontal cortex of subjects with schizophrenia. HSPA12A is also a candidate gene for forelimb-girdle muscular anomaly, an autosomal recessive disorder of Japanese black cattle. HSPA12A is predominantly expressed in neuronal cells. It may also play a role in the atherosclerotic process. The gene encoding HSPA12B maps to 20p13. HSPA12B is predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway. | ||
COG1215 | COG1215 | 4.0e-41 | 1066 | 1433 | 375 | + Glycosyltransferases, probably involved in cell wall biogenesis [Cell envelope biogenesis, outer membrane] | ||
cd10229 | HSPA12_like_NBD | 3.0e-46 | 291 | 592 | 325 | + Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins. Human HSPA12A (also known as 70-kDa heat shock protein-12A) and HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2) belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A or HSPA12B. The gene encoding HSPA12A maps to 10q26.12, a cytogenetic region that might represent a common susceptibility locus for both schizophrenia and bipolar affective disorder; reduced expression of HSPA12A has been shown in the prefrontal cortex of subjects with schizophrenia. HSPA12A is also a candidate gene for forelimb-girdle muscular anomaly, an autosomal recessive disorder of Japanese black cattle. HSPA12A is predominantly expressed in neuronal cells. It may also play a role in the atherosclerotic process. The gene encoding HSPA12B maps to 20p13. HSPA12B is predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway. | ||
TIGR03030 | CelA | 4.0e-47 | 1075 | 1402 | 358 | + cellulose synthase catalytic subunit (UDP-forming). Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils. | ||
cd06421 | CESA_CelA_like | 2.0e-78 | 1109 | 1346 | 244 | + CESA_CelA_like are involved in the elongation of the glucan chain of cellulose. Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001259116.1 | 0 | 1096 | 1562 | 203 | 682 | glycosyl transferase, putative [Neosartorya fischeri NRRL 181] |
RefSeq | XP_001557767.1 | 0 | 1096 | 1562 | 177 | 659 | hypothetical protein BC1G_03864 [Botryotinia fuckeliana B05.10] |
RefSeq | XP_001783660.1 | 0 | 1029 | 1590 | 69 | 631 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002563258.1 | 0 | 1096 | 1562 | 218 | 697 | Pc20g07350 [Penicillium chrysogenum Wisconsin 54-1255] |
RefSeq | XP_388067.1 | 0 | 1096 | 1562 | 315 | 794 | hypothetical protein FG07891.1 [Gibberella zeae PH-1] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 4hg6_A | 3e-37 | 1034 | 1405 | 68 | 447 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
PDB | 3u1u_B | 0.000007 | 203 | 300 | 5 | 104 | A Chain A, Crystal Structure Of Rna Polymerase-Associated Protein Rtf1 Homolog Plus-3 Domain |
PDB | 3u1u_A | 0.000007 | 203 | 300 | 5 | 104 | A Chain A, Crystal Structure Of Rna Polymerase-Associated Protein Rtf1 Homolog Plus-3 Domain |
PDB | 2db9_A | 0.000008 | 203 | 300 | 11 | 110 | A Chain A, Solution Structure Of The Plus-3 Domain Of Human Kiaa0252 Protein |
PDB | 2bze_A | 0.00004 | 201 | 300 | 21 | 118 | A Chain A, Nmr Structure Of Human Rtf1 Plus3 Domain |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cellulose biosynthesis | CELLULOSE-SYNTHASE-UDP-FORMING-RXN | EC-2.4.1.12 | cellulose synthase (UDP-forming) |