Basic Information | |
---|---|
Species | Selaginella moellendorffii |
Cazyme ID | 448592 |
Family | GT2 |
Protein Properties | Length: 2500 Molecular Weight: 382460 Isoelectric Point: 7.9343 |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GT2 | 2202 | 2376 | 3.1e-27 |
IFLPCCKEPTDVPEDSIQAALAMDYPKHQYRVLVLDDGGDDQLKQYCEVLEHVEPPSASVRYLRREKIPGVPHNFKCGNLNYGLEHSDAEFVVMMDADMI LHPSFLKTLLPHIVKDPKVSFVQIPQSFYNLPVGDPLNDASGFGYDRAMVHRDTLGAAPCVGTGAIFRRKHLDEI | |||
GT2 | 2903 | 3072 | 5e-28 |
IFLPCCKEPTDVPEDSIQAALAMDYPKHQFRVLVLDDGGDDELKRYCEELESACVKYLRRKKIPGVPHNFKCGNLNYGLEHSDAEFVVMMDADMILHPSF LKTLLPHIVKDPKVSFVQIPQSFYNLPVGDPLNDACGFGYERVMIHRDTFGAAPCVGTGAIFRRKHLDEI |
Full Sequence |
---|
Protein Sequence Length: 2500 Download |
MEIREVPEVS PPNGGAKSYS HRSHSSSSRG SIKGAVGARK IKNSGSEEQK APEQQPRISP 60 ERPPRPFLKT SFGQRLSAQC GSVFFDTTSY SHQAPLASTT RNHNDHGGQP LVEGSSLGTG 120 GDRTKLRSTG NSHSASGRGS SGLSEADVRG MALVATATPE VPVFRPGSNS QQQQQALKLW 180 GGAIPKQRAI AMVGQLATSS RVSTDTFSFG GGVRDRSSKR DGSPLGRTAS TSPAPPVHEQ 240 ENEKETKVVN KDAGLQLVPP KLEFCDEEKN KPQAVRSSSE LELEEARKEM MLMASGLGAA 300 LSGRHSQTSL NLAHVKTEVD DQTMILSGAK PGRESSSLPR CSTDILQPAP LSTAADSEAP 360 NLSELGAAQA AKARPSFKND CGFLKLLPSK RKFEVEHDQA SPLQKTASYV LADSENAGLR 420 LSSNSSSGIP PIRKSLLVHL ADKPKQVANG VTRNLSNSKE RRASCSDQFA AAASAQKPVV 480 GSFMKWMIDV GKGLAKKRCF GSEATAAPST ELGSPVGGLC SSVDLRLESS SKAKDHDLVL 540 SPPLMKRFPD EHAVSPQSMD CTDDGAHHKE ASEMQTSGDE QQQRVQQRQR QEQQDGGEHE 600 KSERRRDFSS REEPQASGDG NEGGGNSTNA TEGTTRSSGP PEQLKDGKRT KEHASKSLEQ 660 QQHQLLKQDQ DQDQAQAPAQ AQDLLEDRAH ASQEEQHLKQ EQQDASKSKS GGGEEASFGM 720 WQAASCLIPS QGQQEKSSKL QRSSTGNRSK ARNLAAALDG SGDPECSQGM AEFVASMATV 780 KNWVNSSFKP KDKAAISSAS RSCSFCGLKG HSVMDCSETL ECELKELERR ALVLEDMSSE 840 VLDFPCLRCL GMGHLGAQCR FSVTEAASRA RENSEMRNWR FMRRNSSNVV NTTIVVKPSV 900 TSVTVPANPS LVLVDHAKAS PAASIPPVVW TQSTSLVPQS GNLSIAPLHE PDHKVARAKD 960 QRKNEESPKD NTHKKVGLQR TGTPAKKAAA PQTSETLPSV PKDMLAAIES VRLSRSELWR 1020 SMDSPDFNTN VRGFFLRLRF GRWEKDLGGT GYRMARIRGA IRKLGGDDKN MSVSVDLGDM 1080 ECTVDSQYVS NHSFTERLGR VAWLKEDLTP PAQEEIEQKE KYGDVQWCLT VPAIWSDQAK 1140 GSMQVYAERA NRGAKNDTVS ETMGSLALCD TPLPKVVVGL DFGTTYSGFA FAHRSDPEDV 1200 HLFIDWPGAP RSYCKTQTSL FYAPGKEGAF RLEDWSWSAL DNFKLLLADE GEKMAREKAA 1260 NGFSGKLEVE RLVVDYLASI FGFITRHLGE KYGESFSKRD VQWCLTVPAI WSDEAKQRME 1320 VYAEKAGLIA GKFCSVPDAS IYPLRIILEP EAASFSCQRQ LRGVLSFAQG DKFLVADVGG 1380 GTIDIIVHER EGAQDWITHK VHEACASSGA LGGGTYVDSN FLEFLRKKIG CFDTFKQQEP 1440 DVVHRILSWW LGPKGNCTFN GSGSKFLEIP AKLSKAWKKH DKAELGFPES GDYYDEIEIS 1500 CEQMKAIFDT EVDKTIKLID EKLRKVDNVK YILLVGGFSE SRYLFNRIKK RFEDSVEDVL 1560 SPPNSGAAVC RGAVALGVGT GVVLSRISKN SYGIATSRYA RWDDPPASKF IDNYGIERCS 1620 VFSLYVKKDE SVSENQEITH SFFPISKIPE YTVDEGCAVL DSYSIDINED LELGTSRQVA 1680 VTMYFGRSSI EVSAQRVNFG RNRGLERLYS VEFDAAQTSI LYKEGGDWSW NAQDKFVVVS 1740 KAFRSEWAEE HPDDPPCPED IERRVGVFKI NFKLLLTEGN SNETKVIDKQ SKRDVQWCLT 1800 VLAIWTDQPK HAMQVYAEMW EDHLGARGGV ILLFLARRRI ASPTGSMKLV LAPAHLEVVL 1860 TSTLTFWSCF DTFKRQEPDV VHRILSWHGR EFDTGSWDLL QSDDDDEIEI DCEEMCAIFD 1920 TEINKTIQLI EENVDKVDGI EYIFLVGEKD QGAVALGNGT GVVLARISKK SYGISTSHIF 1980 RWDVDPLEYK FLDCFGIERC QMFSSSSKSN DVPRYTETGC EKLDNYSFDI DEDREVALTI 2040 FFGRSCLPCA STLGATARPR GSTRWNSTLL KMIPPPTTSC LVWGILSCSS NQVIISPSSS 2100 TSVLAAPQAS PWGKLIWHTI ICLLVSAHIA AFVNYLGYRF YVYSKQPREL VRRPWLIILS 2160 ICEVIYFLNS VIAAVDLVLP PRMWRPRQSL SLNWEELPTV DIFLPCCKEP TDVPEDSIQA 2220 ALAMDYPKHQ YRVLVLDDGG DDQLKQYCEV LEHVEPPSAS VRYLRREKIP GVPHNFKCGN 2280 LNYGLEHSDA EFVVMMDADM ILHPSFLKTL LPHIVKDPKV SFVQIPQSFY NLPVGDPLND 2340 ASGFGYDRAM VHRDTLGAAP CVGTGAIFRR KHLDEIGGFQ PMSITEDTMT AFKLFNQGFK 2400 SVYLNRKLQI GLTPWTFEGY IKQRQRWCQG AIQQFSATWR EMLGPKSRLS FLLKVCYFWH 2460 TGYYFISVFN IVMVLLFIVL LALNLDLIVG TFDESRRILI |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10229 | HSPA12_like_NBD | 0.006 | 1915 | 1947 | 36 | + 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. | ||
cd10229 | HSPA12_like_NBD | 2.0e-5 | 1112 | 1150 | 46 | + 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. | ||
cd06421 | CESA_CelA_like | 1.0e-81 | 2899 | 3131 | 239 | + 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. | ||
cd10229 | HSPA12_like_NBD | 2.0e-111 | 1176 | 1571 | 421 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001768999.1 | 0 | 1175 | 1713 | 10 | 587 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001783660.1 | 0 | 2112 | 2678 | 64 | 631 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001783660.1 | 0 | 2808 | 3375 | 59 | 631 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001785652.1 | 0 | 1163 | 1716 | 1 | 581 | 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 | 4hg6_A | 3e-40 | 2165 | 2494 | 114 | 447 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
PDB | 4hg6_A | 3e-38 | 2824 | 3190 | 68 | 447 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
PDB | 2db9_A | 0.0004 | 999 | 1120 | 11 | 137 | A Chain A, Solution Structure Of The Plus-3 Domain Of Human Kiaa0252 Protein |
PDB | 3u1u_B | 0.0004 | 999 | 1120 | 5 | 131 | A Chain A, Crystal Structure Of Rna Polymerase-Associated Protein Rtf1 Homolog Plus-3 Domain |
PDB | 3u1u_A | 0.0004 | 999 | 1120 | 5 | 131 | A Chain A, Crystal Structure Of Rna Polymerase-Associated Protein Rtf1 Homolog Plus-3 Domain |
Metabolic Pathways | |||
---|---|---|---|
Pathway Name | Reaction | EC | Protein Name |
cellulose biosynthesis | CELLULOSE-SYNTHASE-UDP-FORMING-RXN | EC-2.4.1.12 | cellulose synthase (UDP-forming) |
Transmembrane Domains | |
---|---|
Start | End |
2115 | 2137 |
2157 | 2179 |
2463 | 2485 |
2498 | 2520 |
2591 | 2610 |
2623 | 2645 |
2682 | 2704 |
2717 | 2736 |
2817 | 2839 |
2856 | 2878 |
3159 | 3181 |
3194 | 3216 |
3288 | 3307 |
3320 | 3342 |
3380 | 3402 |