| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.001G182200.1 |
| Family | GT47 |
| Protein Properties | Length: 1258 Molecular Weight: 139356 Isoelectric Point: 8.5624 |
| Chromosome | Chromosome/Scaffold: 01 Start: 27866544 End: 27873965 |
| Description | Subtilase family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GT47 | 181 | 403 | 0 |
| QFAVDRPEWGIMGGKDHFLVAGRITWDFRRLSDEESDWGNKLLFLPAARNMSMLVVESSPWNANDFGIPYPTYFHPAKDEEVFIWQDRMRKLERKWLFSF AGAPRPGNPKSIRGQIINQCRNSKVCKLLECDFGESKCHSPSSIMQMFQSSLFCLQPQGDSYTRRSAFDSMLAGCIPVFFHPGSAYTQYTWHLPKNFTTY SVFIPEDDIRKRNVSIEERLSQI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1258 Download |
| RRPVTLGPLE AMEKGSPKNQ QTRLCFLASL SAFFWILLLY FHFVVLGSSP TVEESITLQP 60 VKLESPLVNV ESVPSPVTDA RVEKEKPAPV KPVQDTAGEK VVPYPFMRAL RTVENKSDPC 120 GGRYIYVHKL PPRFNEDMLK ECRSLSLWTN MCKFTSNKGL GPPLENVEGV FENTGWYATN 180 QFAVDRPEWG IMGGKDHFLV AGRITWDFRR LSDEESDWGN KLLFLPAARN MSMLVVESSP 240 WNANDFGIPY PTYFHPAKDE EVFIWQDRMR KLERKWLFSF AGAPRPGNPK SIRGQIINQC 300 RNSKVCKLLE CDFGESKCHS PSSIMQMFQS SLFCLQPQGD SYTRRSAFDS MLAGCIPVFF 360 HPGSAYTQYT WHLPKNFTTY SVFIPEDDIR KRNVSIEERL SQISPEQVKI MRETVINLIP 420 RLIYADPRSK LETLRDAFDV AVQAVIDKVT RLRRNIIQGR TEYDNFVEEN SWKYDLLDEG 480 QREPCLNSLL PLQTTPPPTS SSPSNYLCLY FSMEPKLHLF FSALCFYLVS AYGNTLRTYI 540 VQLHPHGVTS SSFPTKFLWH LSFLDQTLSS EEDSSSRLLY SYGSAMEGFA ALLTETEIEL 600 LRGLPDVVAV RPDQLLQLQT TYSYKFLGLS STTDGAWVKS GFGRGTIIGV LDTGVWPESP 660 SFADQGMPPV PKRWRGMCQE GQNFKATSCN RKLIGARFFI KGHHVSSVPP SENMVDEYIS 720 PRDSSGHGTH TSSTAGGVSV PMASVLVCWF NGCYSSDILA AIDVAIVDGV DVLSLSLGGF 780 PLPLFDDSIA IGSFRAVEHG ISVICAAGNN GPIQSSVANI APWIATIGAS TLDRKFPAIV 840 RMGNGEYVYG ESLFPGKSLP IAEKELELVY VTGGNSGSEF CFRGSLPKEK VKGKMVVCDR 900 GVNGRAEKGV AVKEAGGAAM ILANTEINLE EDSVDAHVLP ATEIGYAEAV RLKTYMDTTS 960 HPRARIVFGG TVIGTSRAPE VAQFSARGPN LYDSTILKPD VIAPGVNIIA AWPQNLGPTG 1020 LPEDTRRVNF TVMSGTSMAC PHVSGIAALI HSAHPGWTPA AIKSAIMTSA DASDHRGKPI 1080 MDGSKPAAVF AIGAGHVNPN RAIDPGLIYD IKPDEYVIHL CTLGYTRSEI FTITHRNVSC 1140 SEKLKMNRGF SLNYPSISVA FKHGVKSKMI TRRLTNVGNP NSVYSVQVKP PEGVKVRVKP 1200 RRLIFKHINQ SLSYRIWVIS RKKTQTKKIS YAEGQLTWMN AHNSFHRVRS PISVTWK* 1260 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd07474 | Peptidases_S8_subtilisin_Vpr-like | 4.0e-33 | 957 | 1102 | 147 | + Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. | ||
| cd04852 | Peptidases_S8_3 | 4.0e-35 | 995 | 1071 | 77 | + Peptidase S8 family domain, uncharacterized subfamily 3. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. | ||
| pfam03016 | Exostosin | 1.0e-43 | 119 | 403 | 331 | + Exostosin family. The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear. | ||
| cd04852 | Peptidases_S8_3 | 3.0e-61 | 616 | 832 | 239 | + Peptidase S8 family domain, uncharacterized subfamily 3. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004252 | serine-type endopeptidase activity |
| GO:0006508 | proteolysis |
| GO:0016020 | membrane |
| GO:0042802 | identical protein binding |
| GO:0043086 | negative regulation of catalytic activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI37197.1 | 0 | 1 | 1256 | 56 | 1316 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_563701.1 | 0 | 513 | 1257 | 1 | 773 | SDD1 (STOMATAL DENSITY AND DISTRIBUTION); serine-type endopeptidase [Arabidopsis thaliana] |
| RefSeq | XP_002269766.1 | 0 | 1 | 1256 | 61 | 1411 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002301847.1 | 0 | 586 | 1257 | 1 | 692 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526537.1 | 0 | 513 | 1257 | 1 | 767 | Cucumisin precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vta_B | 0 | 620 | 1255 | 1 | 618 | A Chain A, Crystal Structure Of Cucumisin, A Subtilisin-Like Endoprotease From Cucumis Melo L |
| PDB | 3vta_A | 0 | 620 | 1255 | 1 | 618 | A Chain A, Crystal Structure Of Cucumisin, A Subtilisin-Like Endoprotease From Cucumis Melo L |
| PDB | 3i74_B | 0 | 620 | 1252 | 1 | 640 | C Chain C, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 In Complex With A Chloromethylketone Inhibitor |
| PDB | 3i74_A | 0 | 620 | 1252 | 1 | 640 | C Chain C, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 In Complex With A Chloromethylketone Inhibitor |
| PDB | 3i6s_B | 0 | 620 | 1252 | 1 | 640 | A Chain A, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 |
