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Conserved domains on  [gi|79333554|ref|NP_171671|]
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SIGNAL PEPTIDE PEPTIDASE-LIKE 4 [Arabidopsis thaliana]

Protein Classification

PA and Peptidase_A22B domain-containing protein( domain architecture ID 11978233)

PA and Peptidase_A22B domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
241-527 2.46e-123

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


:

Pssm-ID: 282158  Cd Length: 286  Bit Score: 363.16  E-value: 2.46e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   241 TSSRGVVEVTVISAILFVVVASCFLIMLYKLMSFWFIEVLVVLFCIGGVEGLQTCLVSLLSCFrWFRRFGESYVKVPFL- 319
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSLLVYVLTIYFCILGIIALAFCLSPFLTRL-FFNKCPLKNIKLPFLp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   320 GAVSYLTLAICPFCIAFAVFWAVKRQYsyaWIGQDILGISLIITVLQIVRVPNLKVGFVLLSCAFMYDIFWVFVSKWWFR 399
Cdd:pfam04258  80 GRFSYSELVALLLCIVFAVWWALKRHE---WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYIFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   400 ESVMIVVARGDRSGEDGIPMLLKIPR---MFDPWGGYSIIGFGDIILPGLLVTFALRYDWLANKRLKSGYFLGTMSAYGL 476
Cdd:pfam04258 157 TSVMVTVATGPSSTGEDIPMKLVFPRlsnMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHDIYFISTMIAYGL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 79333554   477 GLLITYIALNLMDgHGQPALLYIVPFILGTLFVLGHKRGDLKTLWTTGEPD 527
Cdd:pfam04258 237 GLLITFVALNLFK-AAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA super family cl28883
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
46-183 1.30e-56

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 cd02132:

Pssm-ID: 333703 [Multi-domain]  Cd Length: 139  Bit Score: 185.71  E-value: 1.30e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  46 FVLVKVPTRVNGSEYTEYVGVGARFGPTLESKEKHATLIKLAIADPPDCCSTPKNKLTGEVILVHRGKCSFTTKTKVAEA 125
Cdd:cd02132   2 FQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNANKTRAVLANPLDCCSPSTSKLSGSIALVERGECAFTEKAKIAEA 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79333554 126 AGASAILIINNSTDLFKMVCEKGENVLDITIPVVMLPVDAGRSLENIVKSNAIVTLQL 183
Cdd:cd02132  82 GGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
241-527 2.46e-123

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


Pssm-ID: 282158  Cd Length: 286  Bit Score: 363.16  E-value: 2.46e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   241 TSSRGVVEVTVISAILFVVVASCFLIMLYKLMSFWFIEVLVVLFCIGGVEGLQTCLVSLLSCFrWFRRFGESYVKVPFL- 319
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSLLVYVLTIYFCILGIIALAFCLSPFLTRL-FFNKCPLKNIKLPFLp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   320 GAVSYLTLAICPFCIAFAVFWAVKRQYsyaWIGQDILGISLIITVLQIVRVPNLKVGFVLLSCAFMYDIFWVFVSKWWFR 399
Cdd:pfam04258  80 GRFSYSELVALLLCIVFAVWWALKRHE---WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYIFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   400 ESVMIVVARGDRSGEDGIPMLLKIPR---MFDPWGGYSIIGFGDIILPGLLVTFALRYDWLANKRLKSGYFLGTMSAYGL 476
Cdd:pfam04258 157 TSVMVTVATGPSSTGEDIPMKLVFPRlsnMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHDIYFISTMIAYGL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 79333554   477 GLLITYIALNLMDgHGQPALLYIVPFILGTLFVLGHKRGDLKTLWTTGEPD 527
Cdd:pfam04258 237 GLLITFVALNLFK-AAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
247-514 2.22e-68

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 220.59  E-value: 2.22e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    247 VEVTVISAILFVVVASCFLIMLYKLMSFWFIeVLVVLFCIGGVEGLQTCLvSLLSCFRwfrrfgesyvkvpflgaVSYLT 326
Cdd:smart00730   3 SLLNSLVAIVFPIVATFVLVLLYKFFKYLVI-VLVIYFSSLGVLFLYSLL-YPLEVFR-----------------VDYPT 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    327 LAICPFCIAFAVFWAVKRQYsyAWIGQDILGISLIITVLQIVRVPNLKVGFVLLSCAFMYDIFWVFVSKWwfRESVMIVV 406
Cdd:smart00730  64 LLILLLNFAVVGFWCIHRKG--AWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG--PLRVMVEV 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    407 ARGDRSGEDGIPMLLKIPRM-----FDPWGGYSIIGFGDIILPGLLVTFALRYDWLanKRLKSGYFLGTMSAYGLGLLIT 481
Cdd:smart00730 140 ATGRDEPIKVFPALLYVPRLvvsfeDDEEERFSMLGLGDIVFPGILVASAARFDVS--VRSDSNYFLACFVAYGIGLILT 217
                          250       260       270
                   ....*....|....*....|....*....|...
gi 79333554    482 YIALNLMDgHGQPALLYIVPFILGTLFVLGHKR 514
Cdd:smart00730 218 LVLLALFK-KAQPALPYLVPFTLVFYLLTALLR 249
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
46-183 1.30e-56

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: 185.71  E-value: 1.30e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  46 FVLVKVPTRVNGSEYTEYVGVGARFGPTLESKEKHATLIKLAIADPPDCCSTPKNKLTGEVILVHRGKCSFTTKTKVAEA 125
Cdd:cd02132   2 FQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNANKTRAVLANPLDCCSPSTSKLSGSIALVERGECAFTEKAKIAEA 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79333554 126 AGASAILIINNSTDLFKMVCEKGENVLDITIPVVMLPVDAGRSLENIVKSNAIVTLQL 183
Cdd:cd02132  82 GGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
44-183 5.36e-15

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: 78.16  E-value: 5.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   44 NNFVLVKVPTRVNGSeyteYVGVGARFGPTLESKEKHATL--IKLAIADPPDCCSTPKN--KLTGEVILVHRGKCSFTTK 119
Cdd:NF038113 409 GNLLQVNAPGSLAGR----YPGVRAGFGPRLPDAPITGDLalATDSSPDPNDGCDPILNaaALAGKIAVIRRGSCEFAVK 484
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79333554  120 TKVAEAAGASAILIINNSTDLfKMVCEKGENVLDITIPVVMLPVDAGRSLENIVKSNAIVTLQL 183
Cdd:NF038113 485 VLNAQNAGAIAVIIVNNVPGE-PIVMGGGDTGPPITIPSIMISQADGEAIITALNNGETVNVTL 547
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
40-192 4.70e-13

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: 72.38  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    40 PGCNNNFVLVKVPTRVNGSeyteYVGVGARFGPTLESKEKHATLIKLAIADPPDCCS--TPKNKLTGEVILVHRGKCSFT 117
Cdd:NF038112  484 DGTPEQTLTVTAPASLAGV----YEAGSASFGPQAFDVTGDVVLAPDGTGSDTDGCTpfTNAAEVAGKIALIDRGTCDFT 559
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79333554   118 TKTKVAEAAGASAILIINNSTdlfKMVCEKGENVLDITIPVVMLPVDAGRSLENIVkSNAIVTLQLYspKRPAVD 192
Cdd:NF038112  560 VKALNAQNAGAIGVIIANNAA---GAAPGLGGTDPAVTIPALSITQADGNAWKAAL-ANGPVTVRLR--REPALD 628
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
85-169 4.13e-08

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: 50.98  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    85 KLAIADPPDCC--STPKNKLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTDLF--KMVCEKGENVLDITIPVVM 160
Cdd:pfam02225   3 PLVLAPGCYAGdgIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGgpPGAGGNELYPDGIYIPAVG 82

                  ....*....
gi 79333554   161 LPVDAGRSL 169
Cdd:pfam02225  83 VSRADGEAL 91
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
241-527 2.46e-123

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


Pssm-ID: 282158  Cd Length: 286  Bit Score: 363.16  E-value: 2.46e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   241 TSSRGVVEVTVISAILFVVVASCFLIMLYKLMSFWFIEVLVVLFCIGGVEGLQTCLVSLLSCFrWFRRFGESYVKVPFL- 319
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSLLVYVLTIYFCILGIIALAFCLSPFLTRL-FFNKCPLKNIKLPFLp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   320 GAVSYLTLAICPFCIAFAVFWAVKRQYsyaWIGQDILGISLIITVLQIVRVPNLKVGFVLLSCAFMYDIFWVFVSKWWFR 399
Cdd:pfam04258  80 GRFSYSELVALLLCIVFAVWWALKRHE---WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYIFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   400 ESVMIVVARGDRSGEDGIPMLLKIPR---MFDPWGGYSIIGFGDIILPGLLVTFALRYDWLANKRLKSGYFLGTMSAYGL 476
Cdd:pfam04258 157 TSVMVTVATGPSSTGEDIPMKLVFPRlsnMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHDIYFISTMIAYGL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 79333554   477 GLLITYIALNLMDgHGQPALLYIVPFILGTLFVLGHKRGDLKTLWTTGEPD 527
Cdd:pfam04258 237 GLLITFVALNLFK-AAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
247-514 2.22e-68

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 220.59  E-value: 2.22e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    247 VEVTVISAILFVVVASCFLIMLYKLMSFWFIeVLVVLFCIGGVEGLQTCLvSLLSCFRwfrrfgesyvkvpflgaVSYLT 326
Cdd:smart00730   3 SLLNSLVAIVFPIVATFVLVLLYKFFKYLVI-VLVIYFSSLGVLFLYSLL-YPLEVFR-----------------VDYPT 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    327 LAICPFCIAFAVFWAVKRQYsyAWIGQDILGISLIITVLQIVRVPNLKVGFVLLSCAFMYDIFWVFVSKWwfRESVMIVV 406
Cdd:smart00730  64 LLILLLNFAVVGFWCIHRKG--AWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG--PLRVMVEV 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    407 ARGDRSGEDGIPMLLKIPRM-----FDPWGGYSIIGFGDIILPGLLVTFALRYDWLanKRLKSGYFLGTMSAYGLGLLIT 481
Cdd:smart00730 140 ATGRDEPIKVFPALLYVPRLvvsfeDDEEERFSMLGLGDIVFPGILVASAARFDVS--VRSDSNYFLACFVAYGIGLILT 217
                          250       260       270
                   ....*....|....*....|....*....|...
gi 79333554    482 YIALNLMDgHGQPALLYIVPFILGTLFVLGHKR 514
Cdd:smart00730 218 LVLLALFK-KAQPALPYLVPFTLVFYLLTALLR 249
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
46-183 1.30e-56

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: 185.71  E-value: 1.30e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  46 FVLVKVPTRVNGSEYTEYVGVGARFGPTLESKEKHATLIKLAIADPPDCCSTPKNKLTGEVILVHRGKCSFTTKTKVAEA 125
Cdd:cd02132   2 FQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNANKTRAVLANPLDCCSPSTSKLSGSIALVERGECAFTEKAKIAEA 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79333554 126 AGASAILIINNSTDLFKMVCEKGENVLDITIPVVMLPVDAGRSLENIVKSNAIVTLQL 183
Cdd:cd02132  82 GGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
66-183 3.53e-16

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: 74.67  E-value: 3.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  66 VGARFGPTLESKEKHATLIKLAIADPPDCCS--TPKNKLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTD--LF 141
Cdd:cd04818   1 VSAGFGPALTNVTADVVLAGAAPASNTDGCTafTNAAAFAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVANNVAGgaPI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 79333554 142 KMvcekGENVLDITIPVVMLPVDAGRSLENIVKSNAIVTLQL 183
Cdd:cd04818  81 TM----GGDDPDITIPAVMISQADGDALKAALAAGGTVTVTL 118
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
44-183 5.36e-15

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: 78.16  E-value: 5.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554   44 NNFVLVKVPTRVNGSeyteYVGVGARFGPTLESKEKHATL--IKLAIADPPDCCSTPKN--KLTGEVILVHRGKCSFTTK 119
Cdd:NF038113 409 GNLLQVNAPGSLAGR----YPGVRAGFGPRLPDAPITGDLalATDSSPDPNDGCDPILNaaALAGKIAVIRRGSCEFAVK 484
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79333554  120 TKVAEAAGASAILIINNSTDLfKMVCEKGENVLDITIPVVMLPVDAGRSLENIVKSNAIVTLQL 183
Cdd:NF038113 485 VLNAQNAGAIAVIIVNNVPGE-PIVMGGGDTGPPITIPSIMISQADGEAIITALNNGETVNVTL 547
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
70-181 7.50e-15

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: 70.87  E-value: 7.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  70 FGPTLESKEKHatlIKLAIADPPDCCSTPKN--KLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTD----LFKM 143
Cdd:cd02127   2 FGTIFNTRYKH---VPLVPADPLEACEELRNihDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNNDsdeyYVEM 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 79333554 144 VCEKGENvlDITIPVVMLPVDAG----RSLENIVKSNAIVTL 181
Cdd:cd02127  79 IQDDSSR--RADIPAAFLLGKNGymirKTLERLGLPYAIINI 118
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
98-183 7.88e-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: 71.01  E-value: 7.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  98 PKNKLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNS-TDLFKMVCEkGENVLDITIPVVMLPVDAGRSLENIVKSN 176
Cdd:cd00538  41 SGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGdDPGPQMGSV-GLESTDPSIPTVGISYADGEALLSLLEAG 119

                ....*..
gi 79333554 177 AIVTLQL 183
Cdd:cd00538 120 KTVTVDL 126
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
68-182 3.47e-13

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: 67.36  E-value: 3.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  68 ARFGPTLESKEKHATLIklaIADPPDCCS------TPKNKLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINN-STDL 140
Cdd:cd02123  29 ANFGPIPPGSGLKGVLV---VAEPLNACSpienppLNSNASGSFIVLIRRGNCSFETKVRNAQRAGYKAAIVYNDeSNDL 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 79333554 141 FKMVCEKGEnVLDITIPVVMLPVDAGRSLENIVKSNAIVTLQ 182
Cdd:cd02123 106 ISMSGNDQE-IKGIDIPSVFVGKSTGEILKKYASYEKGVILI 146
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
40-192 4.70e-13

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: 72.38  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    40 PGCNNNFVLVKVPTRVNGSeyteYVGVGARFGPTLESKEKHATLIKLAIADPPDCCS--TPKNKLTGEVILVHRGKCSFT 117
Cdd:NF038112  484 DGTPEQTLTVTAPASLAGV----YEAGSASFGPQAFDVTGDVVLAPDGTGSDTDGCTpfTNAAEVAGKIALIDRGTCDFT 559
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79333554   118 TKTKVAEAAGASAILIINNSTdlfKMVCEKGENVLDITIPVVMLPVDAGRSLENIVkSNAIVTLQLYspKRPAVD 192
Cdd:NF038112  560 VKALNAQNAGAIGVIIANNAA---GAAPGLGGTDPAVTIPALSITQADGNAWKAAL-ANGPVTVRLR--REPALD 628
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
68-161 2.66e-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: 60.84  E-value: 2.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  68 ARFGPTLeSKEKHATLiKLAIADPPDCCSTPKN--KLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINN-------ST 138
Cdd:cd02126   5 AQFGMDL-TGDKAGVG-RVVKAKPYRACSEITNaeEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNnegsssdTA 82
                        90       100
                ....*....|....*....|...
gi 79333554 139 DLFKMVCEkGENVLDITIPVVML 161
Cdd:cd02126  83 PMFAMSGD-GDSTDDVTIPVVFL 104
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
81-184 1.32e-09

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: 56.18  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  81 ATLIKLAIADPPDCCSTPKNKL--TGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTDLFkMVCEKGENVLDITIPV 158
Cdd:cd04816  19 APLVPLDPERPAGCDASDYDGLdvKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSDGGG-TAGTLGAPNIDLKVPV 97
                        90       100
                ....*....|....*....|....*.
gi 79333554 159 VMLPVDAGRSLENivKSNAIVTLQLY 184
Cdd:cd04816  98 GVITKAAGAALRR--RLGAGETLELD 121
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
85-169 4.13e-08

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: 50.98  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554    85 KLAIADPPDCC--STPKNKLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTDLF--KMVCEKGENVLDITIPVVM 160
Cdd:pfam02225   3 PLVLAPGCYAGdgIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGgpPGAGGNELYPDGIYIPAVG 82

                  ....*....
gi 79333554   161 LPVDAGRSL 169
Cdd:pfam02225  83 VSRADGEAL 91
PA_PoS1_like cd02124
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ...
92-181 4.18e-08

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: 51.95  E-value: 4.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  92 PDccSTPKnkLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTDLFKMVcekGENVLDItipVVMLPVDAGRSLEN 171
Cdd:cd02124  48 PD--DTPD--LSGYIVLVRRGTCTFATKAANAAAKGAKYVLIYNNGSGPTDQV---GSDADSI---IAAVTPEDGEAWID 117
                        90
                ....*....|
gi 79333554 172 IVKSNAIVTL 181
Cdd:cd02124 118 ALAAGSNVTV 127
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
73-161 4.38e-08

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: 51.62  E-value: 4.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  73 TLESKEKHATLIKLAIADPPDCCST---PKNKLTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTDLfkmvcEKGE 149
Cdd:cd02129  11 SLPSDLDKATLLPLRNLTSSVLCSAsdvPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERLV-----PPSG 85
                        90
                ....*....|....*
gi 79333554 150 NVL---DITIPVVML 161
Cdd:cd02129  86 NRSeyeKIDIPVALL 100
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
102-195 4.54e-08

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: 52.29  E-value: 4.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554 102 LTGEVILVHRGKCSFTTKTKVAEAAGASAILIINNSTDLFKMVCEkgenvLDITIPVVMLPVDAGRSLENIVKSNAIVTL 181
Cdd:cd02133  46 VKGKIALIQRGEITFVEKIANAKAAGAVGVIIYNNVDGLIPGTLG-----EAVFIPVVFISKEDGEALKAALESSKKLTF 120
                        90
                ....*....|....
gi 79333554 182 QLYSPKRPAVDVAE 195
Cdd:cd02133 121 NTKKEKATNPDLAD 134
PA_GRAIL_like cd02122
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ...
59-181 2.19e-07

PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. 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: 239037 [Multi-domain]  Cd Length: 138  Bit Score: 49.99  E-value: 2.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554  59 EYTEYVGVGaRFGptLESKEKHATLIKLAIADPPD--CCS------TPKNKlTGEVILVHRGKCSFTTKTKVAEAAGASA 130
Cdd:cd02122  12 LTTEKTESG-RYG--EHSPKEEAKGLVVVPDPPNDhyGCDpdtrfpIPPNG-EPWIALIQRGNCTFEEKIKLAAERNASA 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 79333554 131 ILIINN---STDLFKM-VCEKGENVlditipVVMLPVDAGRSLENIVKSNAIVTL 181
Cdd:cd02122  88 VVIYNNpgtGNETVKMsHPGTGDIV------AIMITNPKGMEILELLERGISVTM 136
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
106-183 1.12e-05

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: 44.78  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79333554 106 VILVHRGKCSFTTKTKVAEAAGASAILIINNSTD-LFKMVC--EKGEN--VLDITIPVVMLPVDAGRSLENIVKSNAIVT 180
Cdd:cd02125  45 ILLLDRGGCFFTLKAWNAQQAGAAAVLVADNVDEpLLTMDTpeESGSAdyIEKITIPSALITKAFGEKLKKAISNGEMVV 124

                ...
gi 79333554 181 LQL 183
Cdd:cd02125 125 IKL 127
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
104-136 4.23e-05

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: 43.01  E-value: 4.23e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 79333554 104 GEVILVHRGKCSFTTKTKVAEAAGASAILIINN 136
Cdd:cd02130  45 GNIALIERGECPFGDKSALAGAAGAAAAIIYNN 77
 
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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