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Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | g4372.t2 |
Family | GH3 |
Protein Properties | Length: 1425 Molecular Weight: 144556 Isoelectric Point: 6.4575 |
Chromosome | Chromosome/Scaffold: 3 Start: 8484877 End: 8497878 |
Description | DegP protease 9 |
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 |
GH3 | 417 | 524 | 6e-23 |
HFTPYRRPVPPHSPPATPDLRESYLPAFRACVVEGRAHSVMCAYNKVNGVPACAHPHLLRATLNDSWGFGSDPANFVVSDCGAVSDLALTHGWNTSLAAA AAEALTAG |
Full Sequence |
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Protein Sequence Length: 1425 Download |
MTSLLSALGR RASAGTPLGR PAPGGSTLPA VAPAAAASPA LPRRTCCPTA ALSTTASSAC 60 GAAPGISAEP LPQLASCPSR ISSSRSGGRR SRVLLAAPPR STGNGQVGPP QHRKGVVAPG 120 AGAGAAAASA AAPAAAVAAA VDEEVADDDE DVLMDEDEAG QQLAPFMDAV VKVYCMHTEP 180 NYSLPWQRKR QYSSSSSGFV VSHGGRNWLL TNAHSVDYHT QVKVKRRGDD RKFLARVISV 240 GVDCDIAALQ VDDPDFWAPQ SPDSPPPPVL ELGPLPRLQD GVAVVGYPIG GDTISVTAGV 300 VSRIEVTDYS HGSTDLLAIQ IDAAINGGNS GGPVFNRACQ CVGIAFQALV GSDVENVGYV 360 IPTPVVAHFL DDYTRTGGFS GFPQLGIQWQ RMESEALRRA YGMTAAAAGA PHALLPHFTP 420 YRRPVPPHSP PATPDLRESY LPAFRACVVE GRAHSVMCAY NKVNGVPACA HPHLLRATLN 480 DSWGFGSDPA NFVVSDCGAV SDLALTHGWN TSLAAAAAEA LTAGGLSLFC DNAAAAAVPQ 540 AVASGLLAPA VLRAAVRRML LARCRLGILG AAQPNTTNTT DSSSSTQLDT SEAPAGASST 600 SADGTLSQAE AAVDRSGNSG SGGGSGSGSG GGSGSSSGSG SGSGGGSGSS SGSGSGSGSG 660 RPDVQALSRS HAHTRLAYEA ALRSITLLVN RPPPGGSGGR PLLPLQLPPP PPAPANTTDN 720 TTAAPGPLLA LLGPHADGAL YYLGTYYGTP SHPVVTPLAA LREALGPAAV SHTPCLTGVG 780 LEPSDGLHTC TQAAAAAQVA AVVFVGGSSR NFACGDQQCT TITPVSESEG LDRGSLRLPG 840 LQEELVRAVA RSGVPVVVVA VAGGPLDLSP LLGLQGVAAV LAAPYGGQQA GYALASVLLG 900 TSSPSGRLPA TWLYDWYTHL SDPTSMAMRA WPGRTYRYLQ EELVRAVARS GVPVVVVAVA 960 GGPLDLSPLL GLQGVAAVLA APYGGQQGGY PLASVLLGTS SPSGRLPATW LYTHLSDPTS 1020 MAMRAWPGRT YRYLQVPVLF PFGFGLSYTH FHTTDMRASP WDCRTRGDTG AGTAAEGRRR 1080 RQAAPRGAGG GGGEEELCFR VEVDVVNAGR RASGHAVLLS LRRSPQPPGA APAAGGTRTG 1140 AGGGSGSGGG GARSDSGDAG GGGASGGAGG RVLAAAGVGG VAAAAASGGE PGAGRAHSGC 1200 RPCAEVLQQQ QPWRAQRQQE QGQRDGPQDG EEESEEEEEG GEFAEWGGER YGHPDTLAAH 1260 TAAYHRIMAD RLERPQGQQR PQAQQGQQGR GARGGSGARG SASAAGAGSH SDGGGGDELD 1320 GQVDGVDDDP PPVRELVAFG RLEDVSPGEV RTLVLQVRLP AAGLEVEVEA EAEVEAEAEV 1380 EAEEEQQAGR QGGGPRRRAH RRYVAHLQAG ALCCPLPRPA ASRR* 1440 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN03080 | PLN03080 | 3.0e-11 | 983 | 1125 | 159 | + Probable beta-xylosidase; Provisional | ||
PLN03080 | PLN03080 | 7.0e-14 | 435 | 501 | 67 | + Probable beta-xylosidase; Provisional | ||
TIGR02037 | degP_htrA_DO | 2.0e-16 | 187 | 395 | 217 | + periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]. | ||
pfam00933 | Glyco_hydro_3 | 3.0e-17 | 435 | 504 | 71 | + Glycosyl hydrolase family 3 N terminal domain. | ||
COG0265 | DegQ | 2.0e-19 | 198 | 395 | 199 | + Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones] |
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 | NP_568577.1 | 0 | 158 | 410 | 116 | 358 | DegP9 (DegP protease 9); catalytic/ protein binding / serine-type endopeptidase/ serine-type peptidase [Arabidopsis thaliana] |
RefSeq | XP_002280249.1 | 0 | 158 | 410 | 103 | 345 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002321577.1 | 0 | 162 | 410 | 16 | 254 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002511437.1 | 0 | 162 | 410 | 59 | 297 | serine endopeptidase degp2, putative [Ricinus communis] |
RefSeq | XP_002511438.1 | 0 | 162 | 410 | 101 | 339 | serine endopeptidase degp2, 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 | 4fln_C | 0 | 157 | 400 | 37 | 270 | E Chain E, Crystal Structure Of Plant Protease Deg2 |
PDB | 4fln_B | 0 | 157 | 400 | 37 | 270 | E Chain E, Crystal Structure Of Plant Protease Deg2 |
PDB | 4fln_A | 0 | 157 | 400 | 37 | 270 | E Chain E, Crystal Structure Of Plant Protease Deg2 |
PDB | 3ac0_D | 0.00000000000003 | 915 | 1073 | 586 | 753 | A Chain A, Crystal Structure Of Beta-Glucosidase From Kluyveromyces Marxianus In Complex With Glucose |
PDB | 3ac0_D | 0.0000000009 | 827 | 948 | 588 | 711 | A Chain A, Crystal Structure Of Beta-Glucosidase From Kluyveromyces Marxianus In Complex With Glucose |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
(1,4)-β-xylan degradation | 3.2.1.37-RXN | EC-3.2.1.37 | xylan 1,4-β-xylosidase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CD448928 | 233 | 162 | 394 | 0 |
FC432284 | 231 | 164 | 394 | 0 |
GE580922 | 234 | 161 | 394 | 0 |
JK792833 | 235 | 160 | 394 | 0 |
BU004489 | 227 | 168 | 394 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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