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Conserved domains on  [gi|19922788|ref|NP_611740|]
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uncharacterized protein Dmel_CG9849, isoform A [Drosophila melanogaster]

Protein Classification

protease-associated domain-containing protein; M28 family metallopeptidase( domain architecture ID 10114766)

protease-associated (PA) domain-containing protein which may participate in substrate binding and/or promote conformational changes| M28 family metallopeptidase contains aminopeptidases as well as carboxypeptidases that have co-catalytic zinc ions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
 57-176 3.06e-59

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: 181.03  E-value: 3.06e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788  57 DFGSAFSERLEGVPLVITDPPGACQEIRNARDLNGGVALIDRGECSFLTKTLRAEAAGALAAIITEYNPssPEFEHYIEM 136
Cdd:cd02127   1 DFGTIFNTRYKHVPLVPADPLEACEELRNIHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNN--DSDEYYVEM 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19922788 137 IHDNSQQDANIPAGFLLGKNGVIIRSTLQRLKRVHALINI 176
Cdd:cd02127  79 IQDDSSRRADIPAAFLLGKNGYMIRKTLERLGLPYAIINI 118
 
Name Accession Description Interval E-value
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
 57-176 3.06e-59

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: 181.03  E-value: 3.06e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788  57 DFGSAFSERLEGVPLVITDPPGACQEIRNARDLNGGVALIDRGECSFLTKTLRAEAAGALAAIITEYNPssPEFEHYIEM 136
Cdd:cd02127   1 DFGTIFNTRYKHVPLVPADPLEACEELRNIHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNN--DSDEYYVEM 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19922788 137 IHDNSQQDANIPAGFLLGKNGVIIRSTLQRLKRVHALINI 176
Cdd:cd02127  79 IQDDSSRRADIPAAFLLGKNGYMIRKTLERLGLPYAIINI 118
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 37-181 1.73e-06

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 47.72  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788   37 FFEILSPSELEYTYrlrpaKDFGSAFSERLEGVPL---------VITDPPGACQEIRNARDLNGGVALIDRGECSFLTKT 107
Cdd:NF038113 411 LLQVNAPGSLAGRY-----PGVRAGFGPRLPDAPItgdlalatdSSPDPNDGCDPILNAAALAGKIAVIRRGSCEFAVKV 485

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922788  108 LRAEAAGALAAIITEYNPSSPefehyIEMIHDNSQQDANIPAGFLLGKNGVIIRSTLQRlkrvhaliNIPVNLT 181
Cdd:NF038113 486 LNAQNAGAIAVIIVNNVPGEP-----IVMGGGDTGPPITIPSIMISQADGEAIITALNN--------GETVNVT 546
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 38-108 3.38e-04

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: 40.80  E-value: 3.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922788    38 FEILSPSELEYTYRLRPAkDFG-SAFSerLEGvPLVI-----TDPPGACQEIRNARDLNGGVALIDRGECSFLTKTL 108
Cdd:NF038112  491 LTVTAPASLAGVYEAGSA-SFGpQAFD--VTG-DVVLapdgtGSDTDGCTPFTNAAEVAGKIALIDRGTCDFTVKAL 563
 
Name Accession Description Interval E-value
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
 57-176 3.06e-59

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: 181.03  E-value: 3.06e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788  57 DFGSAFSERLEGVPLVITDPPGACQEIRNARDLNGGVALIDRGECSFLTKTLRAEAAGALAAIITEYNPssPEFEHYIEM 136
Cdd:cd02127   1 DFGTIFNTRYKHVPLVPADPLEACEELRNIHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNN--DSDEYYVEM 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19922788 137 IHDNSQQDANIPAGFLLGKNGVIIRSTLQRLKRVHALINI 176
Cdd:cd02127  79 IQDDSSRRADIPAAFLLGKNGYMIRKTLERLGLPYAIINI 118
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
 54-174 2.36e-11

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: 58.53  E-value: 2.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788  54 PAKdFGSAFSERLEGV-PLVITDPPGACQEIRNARDLNGGVALIDRGECSFLTKTLRAEAAGALAAIITEYNPSS----- 127
Cdd:cd02126   4 PAQ-FGMDLTGDKAGVgRVVKAKPYRACSEITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNEGSssdta 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19922788 128 PEFehyiEMIHD-NSQQDANIPAGFLLGKNGVIIRSTLQRLKRVHALI 174
Cdd:cd02126  83 PMF----AMSGDgDSTDDVTIPVVFLFSKEGSKLLAAIKEHQNVEVLL 126
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
 54-180 1.06e-08

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: 51.96  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788  54 PAKdFG-SAFSERLEGVpLVITDPPGACQEIRNARDLNGG----VALIDRGECSFLTKTLRAEAAGALAAIIteYNPSSp 128
Cdd:cd02123  28 PAN-FGpIPPGSGLKGV-LVVAEPLNACSPIENPPLNSNAsgsfIVLIRRGNCSFETKVRNAQRAGYKAAIV--YNDES- 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19922788 129 efEHYIEMIHDNS-QQDANIPAGFLLGKNGVIIRSTLQRLKRVHALINIPVNL 180
Cdd:cd02123 103 --NDLISMSGNDQeIKGIDIPSVFVGKSTGEILKKYASYEKGVILIPDLPLKI 153
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
 57-108 5.25e-07

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: 46.55  E-value: 5.25e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19922788  57 DFGSAFSERLEGVPLVITDPPG---ACQEIRNARDLNGGVALIDRGECSFLTKTL 108
Cdd:cd04818   4 GFGPALTNVTADVVLAGAAPASntdGCTAFTNAAAFAGKIALIDRGTCNFTVKVL 58
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 37-181 1.73e-06

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 47.72  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788   37 FFEILSPSELEYTYrlrpaKDFGSAFSERLEGVPL---------VITDPPGACQEIRNARDLNGGVALIDRGECSFLTKT 107
Cdd:NF038113 411 LLQVNAPGSLAGRY-----PGVRAGFGPRLPDAPItgdlalatdSSPDPNDGCDPILNAAALAGKIAVIRRGSCEFAVKV 485

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922788  108 LRAEAAGALAAIITEYNPSSPefehyIEMIHDNSQQDANIPAGFLLGKNGVIIRSTLQRlkrvhaliNIPVNLT 181
Cdd:NF038113 486 LNAQNAGAIAVIIVNNVPGEP-----IVMGGGDTGPPITIPSIMISQADGEAIITALNN--------GETVNVT 546
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 38-108 3.38e-04

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: 40.80  E-value: 3.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922788    38 FEILSPSELEYTYRLRPAkDFG-SAFSerLEGvPLVI-----TDPPGACQEIRNARDLNGGVALIDRGECSFLTKTL 108
Cdd:NF038112  491 LTVTAPASLAGVYEAGSA-SFGpQAFD--VTG-DVVLapdgtGSDTDGCTPFTNAAEVAGKIALIDRGTCDFTVKAL 563
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
 85-174 1.49e-03

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: 37.11  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922788  85 NARDLNGGVALIDRGECSFLTKTLRAEAAGALAAIIteYNpssPEFEHYIEMIHDN-SQQDANIPAGFLLGKNGVIIRST 163
Cdd:cd00538  41 SGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVII--YN---NGDDPGPQMGSVGlESTDPSIPTVGISYADGEALLSL 115

                        90
                ....*....|.
gi 19922788 164 LQRLKRVHALI 174
Cdd:cd00538 116 LEAGKTVTVDL 126
PA_PoS1_like cd02124
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ...
 54-106 7.83e-03

PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 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: 239039  Cd Length: 129  Bit Score: 35.00  E-value: 7.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922788  54 PAKDFGSAFSERLEGV---PLV-----ITDPPGACQEI-RNARDLNGGVALIDRGECSFLTK 106
Cdd:cd02124  10 GTTDFGYLPGFPALWNdtlPLWalsldTSVADDACQPLpDDTPDLSGYIVLVRRGTCTFATK 71
 
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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