Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna26581.1-v1.0-hybrid |
Family | PL4 |
Protein Properties | Length: 1429 Molecular Weight: 162698 Isoelectric Point: 5.5961 |
Chromosome | Chromosome/Scaffold: 1 Start: 3928096 End: 3943257 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 167 | 770 | 0 |
HVVMNNDILQVNLSKPQGMVTGIQYKGIDNLLEVLEDETNRGYWDLVWSAPGITRKKGAFDRIEGTNFTVIVETEDQIELSFTRMWDPSLEGKVVPLNID KRFVLLRNSSGFYTYAIYEHLNEWPAFNLTNTRTVFKLRKDKFHYMAISDTRQRHMPLPDDRSAERGQALAYPEAVLLVNPVEPEFKGEVDDKYQYSIEN MYNRVHGWIANDSQVGFWQITPSEEFKTGGPFKQCLTSHVGPTTLAIFHSTHYSGEELILQFGTNEPWKKVLGPVFFYLNSLVNGTTNPIQRLWEDAKQE MNDEVERWPYDFPASKDFLSPKQRGAVRGSLLVRERYVTDDKDVPGNGTWVGLAAPGVVGSWQLECKGYQFWTKADSNGYFSIHGVRPGTYNLYAWVPGF IGDYRDVSEVVVTPDGDVDVGTLVYEPPRTGPTLWEIGIPDRTAAEFYVPDPNPKYINKLYVNHTDRFRQYGLWERYAELYPDNDLVYTIGVSDYTKDFF FAQVTRKMGNNTYKGSTWQIKFNLGNVDKNTTYTLRISLATAHVSELQVRINDPETKNPPLFTTGEIGNDNTIARHGIHGLYRLYSVDIPSALLVEGNNT IFLT | |||
PL4 | 814 | 1406 | 0 |
SSLQVIMDNGIVQVTLSNPGGIVTGIQYKGIDNLLEVLNEEANRGYWDLVWSETGSIGTTGTYDRIVGTKFTVIVESEEQVEISFTREWNHDDMNVPLNI DKRFVMLRNSSGFYSYAIYEHLKEWPAFNLPQTRITFKLRKEMFQYMAIADNRQRNMPLPDDRLPERSQILNSDFPEAVLLVNPIEPQYKGEVDDKYQYS CENQNLRVHGWICKDPHVGFWQITPSDEFRSGGPLKQNLTSHVGPICLAMFLSAHYSGEDLVLKLKPDEPWKKVFGPVFIYLNSSSDEKDSSPLWEDAKK QMMTEVQSWPYEFPASSDFPTSKQRGNVSGGILVRDGDHHILGDGAYVGLAPPGDVGSWQRDCKGYQFWTRVDENGYYSIKNIREGNYNLYAWVPGFIGD YRYGVAINITPGCDIQLGDLVYEPPRDGPTLWEIGFPDRTATGFYVPDPNPKFRQWGLWERYAELYPKEDLVYTIGTSDYSKDWFFAQVTRKKDDGTYQG TSWKINFQIDNVNQTKTHKLRVALATANIAELQIRVNDSNADTPLFTTGVIGHDNAICRHGIHGLYRLYSINVPGTLLAKGDNTVFLTQAMST |
Full Sequence |
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Protein Sequence Length: 1429 Download |
MSFSGYEPVQ LCLISDDGPR PICTLVLSDE IVVMKNIRFW RQDAEMMRML EIWSRKDSCG 60 GNACKYTTVF KNWGAIEAPR GGNRNLDVVA VAASGRMTLS SNAKPIGLAC SFWAGDKILR 120 PYLEPENEQR TNPPHFFAFH DNMDFCKAGY HDSSSPLLQP FISGWEHVVM NNDILQVNLS 180 KPQGMVTGIQ YKGIDNLLEV LEDETNRGYW DLVWSAPGIT RKKGAFDRIE GTNFTVIVET 240 EDQIELSFTR MWDPSLEGKV VPLNIDKRFV LLRNSSGFYT YAIYEHLNEW PAFNLTNTRT 300 VFKLRKDKFH YMAISDTRQR HMPLPDDRSA ERGQALAYPE AVLLVNPVEP EFKGEVDDKY 360 QYSIENMYNR VHGWIANDSQ VGFWQITPSE EFKTGGPFKQ CLTSHVGPTT LAIFHSTHYS 420 GEELILQFGT NEPWKKVLGP VFFYLNSLVN GTTNPIQRLW EDAKQEMNDE VERWPYDFPA 480 SKDFLSPKQR GAVRGSLLVR ERYVTDDKDV PGNGTWVGLA APGVVGSWQL ECKGYQFWTK 540 ADSNGYFSIH GVRPGTYNLY AWVPGFIGDY RDVSEVVVTP DGDVDVGTLV YEPPRTGPTL 600 WEIGIPDRTA AEFYVPDPNP KYINKLYVNH TDRFRQYGLW ERYAELYPDN DLVYTIGVSD 660 YTKDFFFAQV TRKMGNNTYK GSTWQIKFNL GNVDKNTTYT LRISLATAHV SELQVRINDP 720 ETKNPPLFTT GEIGNDNTIA RHGIHGLYRL YSVDIPSALL VEGNNTIFLT RELSVSPFQG 780 IISRQRGRSY KVENTYAMKI SSHKQRLMQH QNFSSLQVIM DNGIVQVTLS NPGGIVTGIQ 840 YKGIDNLLEV LNEEANRGYW DLVWSETGSI GTTGTYDRIV GTKFTVIVES EEQVEISFTR 900 EWNHDDMNVP LNIDKRFVML RNSSGFYSYA IYEHLKEWPA FNLPQTRITF KLRKEMFQYM 960 AIADNRQRNM PLPDDRLPER SQILNSDFPE AVLLVNPIEP QYKGEVDDKY QYSCENQNLR 1020 VHGWICKDPH VGFWQITPSD EFRSGGPLKQ NLTSHVGPIC LAMFLSAHYS GEDLVLKLKP 1080 DEPWKKVFGP VFIYLNSSSD EKDSSPLWED AKKQMMTEVQ SWPYEFPASS DFPTSKQRGN 1140 VSGGILVRDG DHHILGDGAY VGLAPPGDVG SWQRDCKGYQ FWTRVDENGY YSIKNIREGN 1200 YNLYAWVPGF IGDYRYGVAI NITPGCDIQL GDLVYEPPRD GPTLWEIGFP DRTATGFYVP 1260 DPNPKFRQWG LWERYAELYP KEDLVYTIGT SDYSKDWFFA QVTRKKDDGT YQGTSWKINF 1320 QIDNVNQTKT HKLRVALATA NIAELQIRVN DSNADTPLFT TGVIGHDNAI CRHGIHGLYR 1380 LYSINVPGTL LAKGDNTVFL TQAMSTSPFV GIMYDYIRLE APSSSTSA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10317 | RGL4_C | 2.0e-51 | 1245 | 1420 | 178 | + C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
cd10320 | RGL4_N | 3.0e-65 | 814 | 1104 | 292 | + N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
cd10320 | RGL4_N | 2.0e-68 | 167 | 447 | 284 | + N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
pfam06045 | Rhamnogal_lyase | 2.0e-79 | 817 | 1006 | 191 | + Rhamnogalacturonate lyase family. Rhamnogalacturonate lyase (EC:4.2.2.-) degrades the rhamnogalacturonan I (RG-I) backbone of pectin. This family contains mainly members from plants, but also contains the plant pathogen Erwinia chrysanthemi. | ||
pfam06045 | Rhamnogal_lyase | 3.0e-90 | 164 | 356 | 193 | + Rhamnogalacturonate lyase family. Rhamnogalacturonate lyase (EC:4.2.2.-) degrades the rhamnogalacturonan I (RG-I) backbone of pectin. This family contains mainly members from plants, but also contains the plant pathogen Erwinia chrysanthemi. |
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 | 3njx_A | 0.001 | 536 | 769 | 283 | 483 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210a |
PDB | 3njv_A | 0.001 | 536 | 769 | 283 | 483 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210a |
PDB | 2xhn_B | 0.001 | 536 | 769 | 283 | 483 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150a Active Site Mutant |
PDB | 2xhn_A | 0.001 | 536 | 769 | 283 | 483 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150a Active Site Mutant |
PDB | 1nkg_A | 0.001 | 536 | 769 | 283 | 483 | A Chain A, Rhamnogalacturonan Lyase From Aspergillus Aculeatus |
Sequence Alignments (This image is cropped. Click for full image.) |
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