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Conserved domains on  [gi|15221538|ref|NP_174375|]
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VACUOLAR SORTING RECEPTOR 6 [Arabidopsis thaliana]

Protein Classification

M28 family metallopeptidase( domain architecture ID 11978250)

M28 family metallopeptidase is a zinc-dependent peptidase that may be an aminopeptidase or a carboxypeptidase with co-catalytic zinc ions; contains a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PA super family cl28883
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
52-175 2.35e-58

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


The actual alignment was detected with superfamily member cd02125:

Pssm-ID: 333703 [Multi-domain]  Cd Length: 127  Bit Score: 191.93  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  52 NFGVPNYGGYMIGSVVYAGQGAYGCDSFDKTFKPK----FPRPTILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPL 127
Cdd:cd02125   1 NFGLPQYGGTLTGVVVYPKENRTGCKEFDVFFKPKksepGRRPVILLLDRGGCFFTLKAWNAQQAGAAAVLVADNVDEPL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15221538 128 ITMDSPEESKEAdDFIEKLNIPSALIDFSFANTLKQALKKGEEVVLKI 175
Cdd:cd02125  81 LTMDTPEESGSA-DYIEKITIPSALITKAFGEKLKKAISNGEMVVIKL 127
EGF_CA smart00179
Calcium-binding EGF-like domain;
513-541 3.92e-04

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 3.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 15221538    513 DIDECKEQSACQCDGcNCKNKWGGFECKC 541
Cdd:smart00179   1 DIDECASGNPCQNGG-TCVNTVGSYRCEC 28
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
308-394 2.45e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 38.83  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538 308 IRCSMKEKKY--------------SKECAERVVESLGLPLDKIKKCIGDPDanVENEVlkaEQALQVGQGDRGDVTilPT 373
Cdd:COG1651  55 ALCAADQGKFwafhdalfanqpalTDDDLREIAKEAGLDAAKFDACLNSGA--VAAKV---EADTALAQALGVTGT--PT 127
                        90       100
                ....*....|....*....|.
gi 15221538 374 LIVNNAQYRGKLERNAVLKAI 394
Cdd:COG1651 128 FVVNGKLVSGAVPYEELEAAL 148
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
498-516 7.06e-03

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.


:

Pssm-ID: 463661  Cd Length: 22  Bit Score: 34.31  E-value: 7.06e-03
                          10        20
                  ....*....|....*....|.
gi 15221538   498 CRCPPGFKG--DGLKCEDIDE 516
Cdd:pfam12662   2 CSCPPGYQLdpDGRTCVDIDE 22
 
Name Accession Description Interval E-value
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
52-175 2.35e-58

PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239040 [Multi-domain]  Cd Length: 127  Bit Score: 191.93  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  52 NFGVPNYGGYMIGSVVYAGQGAYGCDSFDKTFKPK----FPRPTILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPL 127
Cdd:cd02125   1 NFGLPQYGGTLTGVVVYPKENRTGCKEFDVFFKPKksepGRRPVILLLDRGGCFFTLKAWNAQQAGAAAVLVADNVDEPL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15221538 128 ITMDSPEESKEAdDFIEKLNIPSALIDFSFANTLKQALKKGEEVVLKI 175
Cdd:cd02125  81 LTMDTPEESGSA-DYIEKITIPSALITKAFGEKLKKAISNGEMVVIKL 127
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
32-168 3.35e-11

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 66.60  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538    32 SSVTILNPLAMRSKHDAAIANFGVPNYGgyMIGSVVYAGQGAY----GCDSFD--KTFKPKfprptILIIDRGECYFALK 105
Cdd:NF038112  489 QTLTVTAPASLAGVYEAGSASFGPQAFD--VTGDVVLAPDGTGsdtdGCTPFTnaAEVAGK-----IALIDRGTCDFTVK 561
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221538   106 VWNGQQSGVAAVLVADNVDEPLITM--DSPeeskeaddfieKLNIPSALIDFSFANTLKQALKKG 168
Cdd:NF038112  562 ALNAQNAGAIGVIIANNAAGAAPGLggTDP-----------AVTIPALSITQADGNAWKAALANG 615
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
64-161 1.37e-07

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 49.43  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538    64 GSVVYAGQ---GAYGCDSFDktFKPKfprptILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPLITMDSPEESKEAD 140
Cdd:pfam02225   2 GPLVLAPGcyaGDGIPADFD--VKGK-----IVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPPGAGGNELYPD 74
                          90       100
                  ....*....|....*....|.
gi 15221538   141 DFieklNIPSALIDFSFANTL 161
Cdd:pfam02225  75 GI----YIPAVGVSRADGEAL 91
EGF_CA smart00179
Calcium-binding EGF-like domain;
513-541 3.92e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 3.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 15221538    513 DIDECKEQSACQCDGcNCKNKWGGFECKC 541
Cdd:smart00179   1 DIDECASGNPCQNGG-TCVNTVGSYRCEC 28
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
513-541 4.89e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 4.89e-04
                        10        20
                ....*....|....*....|....*....
gi 15221538 513 DIDECKEQSACQCDGcNCKNKWGGFECKC 541
Cdd:cd00054   1 DIDECASGNPCQNGG-TCVNTVGSYRCSC 28
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
308-394 2.45e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 38.83  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538 308 IRCSMKEKKY--------------SKECAERVVESLGLPLDKIKKCIGDPDanVENEVlkaEQALQVGQGDRGDVTilPT 373
Cdd:COG1651  55 ALCAADQGKFwafhdalfanqpalTDDDLREIAKEAGLDAAKFDACLNSGA--VAAKV---EADTALAQALGVTGT--PT 127
                        90       100
                ....*....|....*....|.
gi 15221538 374 LIVNNAQYRGKLERNAVLKAI 394
Cdd:COG1651 128 FVVNGKLVSGAVPYEELEAAL 148
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
498-516 7.06e-03

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 34.31  E-value: 7.06e-03
                          10        20
                  ....*....|....*....|.
gi 15221538   498 CRCPPGFKG--DGLKCEDIDE 516
Cdd:pfam12662   2 CSCPPGYQLdpDGRTCVDIDE 22
 
Name Accession Description Interval E-value
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
52-175 2.35e-58

PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239040 [Multi-domain]  Cd Length: 127  Bit Score: 191.93  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  52 NFGVPNYGGYMIGSVVYAGQGAYGCDSFDKTFKPK----FPRPTILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPL 127
Cdd:cd02125   1 NFGLPQYGGTLTGVVVYPKENRTGCKEFDVFFKPKksepGRRPVILLLDRGGCFFTLKAWNAQQAGAAAVLVADNVDEPL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15221538 128 ITMDSPEESKEAdDFIEKLNIPSALIDFSFANTLKQALKKGEEVVLKI 175
Cdd:cd02125  81 LTMDTPEESGSA-DYIEKITIPSALITKAFGEKLKKAISNGEMVVIKL 127
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
47-176 1.84e-16

PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239038 [Multi-domain]  Cd Length: 153  Bit Score: 76.99  E-value: 1.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  47 DAAIANFGVPNYGGYMIGSVVYAgQGAYGCDS-FDKTFKPKFPRPTILIIDRGECYFALKVWNGQQSGVAAVLVADNVDE 125
Cdd:cd02123  25 DDLPANFGPIPPGSGLKGVLVVA-EPLNACSPiENPPLNSNASGSFIVLIRRGNCSFETKVRNAQRAGYKAAIVYNDESN 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15221538 126 PLITMDSpeeskeADDFIEKLNIPSALIDFSFANTLKQALkKGEEVVLKID 176
Cdd:cd02123 104 DLISMSG------NDQEIKGIDIPSVFVGKSTGEILKKYA-SYEKGVILIP 147
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
75-175 5.63e-15

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


Pssm-ID: 238300 [Multi-domain]  Cd Length: 126  Bit Score: 71.78  E-value: 5.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  75 GCDSFDKTFKPKFPRPTILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPLITMDSPEESKeaddfiEKLNIPSALID 154
Cdd:cd00538  32 GCGYGTTDDSGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGDDPGPQMGSVGLES------TDPSIPTVGIS 105
                        90       100
                ....*....|....*....|.
gi 15221538 155 FSFANTLKQALKKGEEVVLKI 175
Cdd:cd00538 106 YADGEALLSLLEAGKTVTVDL 126
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
51-175 1.03e-13

PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.


Pssm-ID: 240122 [Multi-domain]  Cd Length: 118  Bit Score: 67.74  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  51 ANFGVPNYggYMIGSVVYAGQG----AYGCDSF--DKTFKPKfprptILIIDRGECYFALKVWNGQQSGVAAVLVADNVD 124
Cdd:cd04818   3 AGFGPALT--NVTADVVLAGAApasnTDGCTAFtnAAAFAGK-----IALIDRGTCNFTVKVLNAQNAGAIAVIVANNVA 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15221538 125 -EPLITMDSPEeskeaddfiEKLNIPSALIDFSFANTLKQALKKGEEVVLKI 175
Cdd:cd04818  76 gGAPITMGGDD---------PDITIPAVMISQADGDALKAALAAGGTVTVTL 118
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
32-168 3.35e-11

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 66.60  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538    32 SSVTILNPLAMRSKHDAAIANFGVPNYGgyMIGSVVYAGQGAY----GCDSFD--KTFKPKfprptILIIDRGECYFALK 105
Cdd:NF038112  489 QTLTVTAPASLAGVYEAGSASFGPQAFD--VTGDVVLAPDGTGsdtdGCTPFTnaAEVAGK-----IALIDRGTCDFTVK 561
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221538   106 VWNGQQSGVAAVLVADNVDEPLITM--DSPeeskeaddfieKLNIPSALIDFSFANTLKQALKKG 168
Cdd:NF038112  562 ALNAQNAGAIGVIIANNAAGAAPGLggTDP-----------AVTIPALSITQADGNAWKAALANG 615
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
92-153 2.81e-08

PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. Proteins in this subgroup contain a RING-finger (Really Interesting New Gene) domain C-terminal to this PA domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup.


Pssm-ID: 240117 [Multi-domain]  Cd Length: 117  Bit Score: 52.39  E-value: 2.81e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221538  92 ILIIDRGECYFALKVWNGQQSGVAAVLVADNV-DEPLITMDSPeeskeadDFIEKLNIPSALI 153
Cdd:cd04813  42 VALVLRGGCGFLDKVMWAQRRGAKAVIVGDDEpGRGLITMFSN-------GDTDNVTIPAMFT 97
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
64-161 1.37e-07

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 49.43  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538    64 GSVVYAGQ---GAYGCDSFDktFKPKfprptILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPLITMDSPEESKEAD 140
Cdd:pfam02225   2 GPLVLAPGcyaGDGIPADFD--VKGK-----IVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPPGAGGNELYPD 74
                          90       100
                  ....*....|....*....|.
gi 15221538   141 DFieklNIPSALIDFSFANTL 161
Cdd:pfam02225  75 GI----YIPAVGVSRADGEAL 91
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
75-155 3.84e-06

PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239042 [Multi-domain]  Cd Length: 118  Bit Score: 46.21  E-value: 3.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  75 GCDSFDKTFkpkFPRPTILIIDRGECYFALKVWNGQQSGVAAVLVADN---VDEPLITMDSPEESKEAD----------- 140
Cdd:cd02127  23 ACEELRNIH---DINGNIALIERGGCSFLTKAINAQKAGALAVIITDVnndSDEYYVEMIQDDSSRRADipaafllgkng 99
                        90
                ....*....|....*....
gi 15221538 141 ----DFIEKLNIPSALIDF 155
Cdd:cd02127 100 ymirKTLERLGLPYAIINI 118
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
92-173 2.01e-05

PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 240120 [Multi-domain]  Cd Length: 122  Bit Score: 44.24  E-value: 2.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  92 ILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPlitMDSPEESKEADDfiekLNIPSALIDFSFANTLKQALKKGEEV 171
Cdd:cd04816  46 IVLVDRGGCPFADKQKVAAARGAVAVIVVNNSDGG---GTAGTLGAPNID----LKVPVGVITKAAGAALRRRLGAGETL 118

                ..
gi 15221538 172 VL 173
Cdd:cd04816 119 EL 120
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
66-179 7.26e-05

PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239048 [Multi-domain]  Cd Length: 143  Bit Score: 43.05  E-value: 7.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  66 VVYAGQGAYGcDSFDKTFKPKfprptILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPL-ITMDspeeskeaddfiE 144
Cdd:cd02133  30 LVDAGLGTPE-DFEGKDVKGK-----IALIQRGEITFVEKIANAKAAGAVGVIIYNNVDGLIpGTLG------------E 91
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15221538 145 KLNIPSALIDFSFANTLKQALKKGEEVVLKIDWSE 179
Cdd:cd02133  92 AVFIPVVFISKEDGEALKAALESSKKLTFNTKKEK 126
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
92-173 2.56e-04

PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239041 [Multi-domain]  Cd Length: 126  Bit Score: 41.19  E-value: 2.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  92 ILIIDRGECYFALKVWNGQQSGVAAVLVADNV------DEPLITMDSpeESKEADDfiekLNIPSAlidFSF---ANTLK 162
Cdd:cd02126  43 IAIMERGDCMFVEKARRVQKAGAIGGIVIDNNegsssdTAPMFAMSG--DGDSTDD----VTIPVV---FLFskeGSKLL 113
                        90
                ....*....|...
gi 15221538 163 QALKKGE--EVVL 173
Cdd:cd02126 114 AAIKEHQnvEVLL 126
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
75-175 3.00e-04

PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239045 [Multi-domain]  Cd Length: 122  Bit Score: 41.09  E-value: 3.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  75 GCDSFDktfkpkFPRPT---ILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEPLI--TMDSPEESkeaddfieklNIP 149
Cdd:cd02130  33 GCDAAD------YPASVagnIALIERGECPFGDKSALAGAAGAAAAIIYNNVPAGGLsgTLGEPSGP----------YVP 96
                        90       100
                ....*....|....*....|....*.
gi 15221538 150 SALIDFSFANTLKQALKKGEEVVLKI 175
Cdd:cd02130  97 TVGISQEDGKALVAALANGGEVSANL 122
EGF_CA smart00179
Calcium-binding EGF-like domain;
513-541 3.92e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 3.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 15221538    513 DIDECKEQSACQCDGcNCKNKWGGFECKC 541
Cdd:smart00179   1 DIDECASGNPCQNGG-TCVNTVGSYRCEC 28
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
513-541 4.89e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 4.89e-04
                        10        20
                ....*....|....*....|....*....
gi 15221538 513 DIDECKEQSACQCDGcNCKNKWGGFECKC 541
Cdd:cd00054   1 DIDECASGNPCQNGG-TCVNTVGSYRCSC 28
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
308-394 2.45e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 38.83  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538 308 IRCSMKEKKY--------------SKECAERVVESLGLPLDKIKKCIGDPDanVENEVlkaEQALQVGQGDRGDVTilPT 373
Cdd:COG1651  55 ALCAADQGKFwafhdalfanqpalTDDDLREIAKEAGLDAAKFDACLNSGA--VAAKV---EADTALAQALGVTGT--PT 127
                        90       100
                ....*....|....*....|.
gi 15221538 374 LIVNNAQYRGKLERNAVLKAI 394
Cdd:COG1651 128 FVVNGKLVSGAVPYEELEAAL 148
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
92-171 4.33e-03

PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239047 [Multi-domain]  Cd Length: 139  Bit Score: 37.79  E-value: 4.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221538  92 ILIIDRGECYFALKVWNGQQSGVAAVLVADNVDEpLITMDSpeeskEADDFIEKLNIPSALIDFSFANTLKQALKKGEEV 171
Cdd:cd02132  62 IALVERGECAFTEKAKIAEAGGASALLIINDQEE-LYKMVC-----EDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKV 135
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
89-156 4.90e-03

PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239044 [Multi-domain]  Cd Length: 120  Bit Score: 37.37  E-value: 4.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221538  89 RPTILIIDRGECYFALKVWNGQQSGVAAVLVADNVdepliTMDSPEESKEAddfIEKLNIPSALIDFS 156
Cdd:cd02129  44 KGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRE-----RLVPPSGNRSE---YEKIDIPVALLSYK 103
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
498-516 7.06e-03

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 34.31  E-value: 7.06e-03
                          10        20
                  ....*....|....*....|.
gi 15221538   498 CRCPPGFKG--DGLKCEDIDE 516
Cdd:pfam12662   2 CSCPPGYQLdpDGRTCVDIDE 22
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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