y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30170.m013878 |
Family | GH13 |
Protein Properties | Length: 1113 Molecular Weight: 124439 Isoelectric Point: 6.3526 |
Chromosome | Chromosome/Scaffold: 30170 Start: 1515948 End: 1520962 |
Description | Tetratricopeptide repeat (TPR)-like superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 36 | 345 | 6.30584e-44 |
SCNKGGGWYNLLKNSILDIANAGITHVWLPPPSQSVSPQGYMPGRLYDLNASRYGTQDELKSLIRAFHHKGIKCLADIVINHRTAEKKDERGIWCIFEGG TDDDRLDWGPSFICCDDTVFSDGTGNPDTGEDYPPAPDIDHLNPRVQKELSDWMNWLKLEIGFGGWRFDFAKGYSPTIMKIYMEQIPPGFAVGEKWDSLS YGQDWKPDYNQDAHRNALKDWIQASGGVITAFDFTTKGILQAAVQGELWRLIDSNGNPPGLIGIMPQNAVTFIDNHDTGSTQQLWPFPSDKVMQGYAYIL THPGIPTIFY |
Full Sequence |
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Protein Sequence Length: 1113 Download |
MNRRKSIEIL FWLFLLSIFP LSTSSALLFQ GFNWESCNKG GGWYNLLKNS ILDIANAGIT 60 HVWLPPPSQS VSPQGYMPGR LYDLNASRYG TQDELKSLIR AFHHKGIKCL ADIVINHRTA 120 EKKDERGIWC IFEGGTDDDR LDWGPSFICC DDTVFSDGTG NPDTGEDYPP APDIDHLNPR 180 VQKELSDWMN WLKLEIGFGG WRFDFAKGYS PTIMKIYMEQ IPPGFAVGEK WDSLSYGQDW 240 KPDYNQDAHR NALKDWIQAS GGVITAFDFT TKGILQAAVQ GELWRLIDSN GNPPGLIGIM 300 PQNAVTFIDN HDTGSTQQLW PFPSDKVMQG YAYILTHPGI PTIFYDHFFD WGLKEQISKL 360 ASIRKNYGID SRSGMKILAA ESDLYMAAIN DNVIMKIGPR MDLGNLLPSK EFQVATSGES 420 YAVWVKNGWM NFLEERSYSM KSQRPNLAPK GSNSLDANTE AIQIQNHLIK RGIDQFVYVS 480 TALLDLYMKL GRVSYAHNAF DYMPIRDVVS WNALICGYSR NGYDFSALEL FVQMLKLGFC 540 PRQTTLVGLL PSCGQLELVF QGKSIHGFGI KSGLHLDPQV KNALTSMYAK CGDLEAAEYL 600 FEEMMDKSVV SWNTMIGAYG QNGFFDEAMF VFKRMIGAGV EVSQVTIMSL PSANANPESI 660 HCYTIKVGLA DDASVVTSLI CMYARYGSTD HAELLYWSLP QKNLVSLTAI ITSYAEAGNL 720 GLVMESFSQM HQLNMKPDSV AMLSILHGIA DPVHICIGHV FHGYAIKSGL DTFNLVTNGL 780 ISMYSKFNNV EALFGLFSGM HEKPLISWNS VISGCVQAGR ASHAIELFCQ MKMHGCNPDA 840 ITIASLLSGC SQLGYLQFGE RLHSYILRNK LEMEDFVGTA LIHMYTKCGS IVHAERVFKS 900 IGKPCLATWN AMISGYSCYG FEHKALTCYS EMQEQGVEPD KITFLGVLAA CTHGGLIHEG 960 RRYFQIMTKV YDMVPTLQHC ACMVGLLARV GLFEEALLFI KNMEKEPDSA VWGAFLSACC 1020 IHQEVKLGEY LAKKLYLLDC RNGGLYVLMS NLYAVTGRWD DVARVREMMK DAGGDGNSGW 1080 KLLMSNDEIR GHNNWVLINF STKTEIRESK FTF 1140 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN03077 | PLN03077 | 1.0e-140 | 477 | 1079 | 609 | + Protein ECB2; Provisional | ||
PLN02784 | PLN02784 | 5.0e-142 | 27 | 424 | 402 | + alpha-amylase | ||
PLN02361 | PLN02361 | 2.0e-151 | 27 | 426 | 404 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-160 | 28 | 373 | 349 | + Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. | ||
PLN00196 | PLN00196 | 0 | 5 | 427 | 426 | + alpha-amylase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004556 | alpha-amylase activity |
GO:0005509 | calcium ion binding |
GO:0005975 | carbohydrate metabolic process |
GO:0043169 | cation binding |
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_002327138.1 | 4e-27 | 424 | 862 | 117 | 529 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002327138.1 | 0 | 469 | 931 | 68 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002327138.1 | 0 | 506 | 1079 | 4 | 577 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002327138.1 | 5.00264e-43 | 604 | 1017 | 1 | 412 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510219.1 | 0 | 1 | 1113 | 1 | 1113 | pentatricopeptide repeat-containing protein, putative [Ricinus communis] |
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 | 1bg9_A | 0 | 27 | 426 | 2 | 402 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 1ava_B | 0 | 27 | 426 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 27 | 426 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 27 | 426 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 27 | 428 | 3 | 406 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |