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Conserved domains on  [gi|442627723|ref|NP_001260434|]
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ER degradation enhancer, mannosidase alpha-like 2, isoform B [Drosophila melanogaster]

Protein Classification

glycoside hydrolase family 47 protein( domain architecture ID 10479226)

glycoside hydrolase family 47 protein such as ER class I alpha1,2-mannosidase, which is a critical enzyme in the maturation of N-linked oligosaccharides and ER-associated degradation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
57-494 1.16e-155

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


:

Pssm-ID: 460241  Cd Length: 453  Bit Score: 460.87  E-value: 1.16e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723   57 MFYHAYNAYMQNAYPADELMPLSCKGRyrgvtpsrgdmdDILGNFSMTLVDTLDTLVLLGDFTEFDHAVKLVIRDVQFDS 136
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGN------------DTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  137 D-IIVSVFETNIRMVGGLLSAHILAEylqkhadtmhWYKGELLEMSRELGYRLLPAFNTSTGIPHARVNLRLGMKDPMLK 215
Cdd:pfam01532  69 DsTEVSVFETTIRYLGGLLSAYDLSG----------DGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  216 KSRETCTACAGTILLEFAALSRLTGDPIFEVRAHAAMDALWK--LRHRGSDLMGTVLNVHSGDWVRRDSGVGAGIDSYYE 293
Cdd:pfam01532 139 AGGASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqSRTPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYE 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  294 YLFKSYVLLG--DDKYLARFNRHYNAVMKYVSEGPMLLDVLM---HRPHAKSKNF---MDSLLAFWPGLQVL-------- 357
Cdd:pfam01532 219 YLLKQYLLTGgtDPEYRDMYEEAMDAIKKHLLFRPSTPSDLLfigELDSGGGGKLspkMDHLSCFAGGMLALgatlglpr 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  358 SGDLKPAVQTHEM---LYQVMQMHTfIPEAFTV--------------DFQIHW--GQHPLRPEFIESTYFLYRATGDHHY 418
Cdd:pfam01532 299 EGDLELAEKLTEGcykTYDSTPTGL-GPEIFYFdpcdedcpwdedkwDFYVKIedPHYLLRPETIESLFYLYRATGDPKY 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627723  419 LQVGKKALKTLQQHAKVSCGYAAVNDVR--TGKHEDRMDSFVLSETIKYLFLLFSDPQdlIINVDEFVFTTEAHLLPL 494
Cdd:pfam01532 378 REWGWEIFQAIEKYTRTECGYSGLQDVTspPGEKEDNMESFWLAETLKYLYLLFSDDD--LLSLDEWVFNTEAHPLPV 453
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
636-761 1.42e-62

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: 205.67  E-value: 1.42e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 636 MAGPSHFSPELTGDQFVEGDVILAKPLRACDEsLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSG 715
Cdd:cd02126    1 TAGPAQFGMDLTGDKAGVGRVVKAKPYRACSE-ITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNEGSSS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 442627723 716 ETQPMFAMSGDG--KDDVLIPVVFMYSMEFGKLSAVMQrRKQPLRVRV 761
Cdd:cd02126   80 DTAPMFAMSGDGdsTDDVTIPVVFLFSKEGSKLLAAIK-EHQNVEVLL 126
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
57-494 1.16e-155

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 460.87  E-value: 1.16e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723   57 MFYHAYNAYMQNAYPADELMPLSCKGRyrgvtpsrgdmdDILGNFSMTLVDTLDTLVLLGDFTEFDHAVKLVIRDVQFDS 136
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGN------------DTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  137 D-IIVSVFETNIRMVGGLLSAHILAEylqkhadtmhWYKGELLEMSRELGYRLLPAFNTSTGIPHARVNLRLGMKDPMLK 215
Cdd:pfam01532  69 DsTEVSVFETTIRYLGGLLSAYDLSG----------DGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  216 KSRETCTACAGTILLEFAALSRLTGDPIFEVRAHAAMDALWK--LRHRGSDLMGTVLNVHSGDWVRRDSGVGAGIDSYYE 293
Cdd:pfam01532 139 AGGASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqSRTPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYE 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  294 YLFKSYVLLG--DDKYLARFNRHYNAVMKYVSEGPMLLDVLM---HRPHAKSKNF---MDSLLAFWPGLQVL-------- 357
Cdd:pfam01532 219 YLLKQYLLTGgtDPEYRDMYEEAMDAIKKHLLFRPSTPSDLLfigELDSGGGGKLspkMDHLSCFAGGMLALgatlglpr 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  358 SGDLKPAVQTHEM---LYQVMQMHTfIPEAFTV--------------DFQIHW--GQHPLRPEFIESTYFLYRATGDHHY 418
Cdd:pfam01532 299 EGDLELAEKLTEGcykTYDSTPTGL-GPEIFYFdpcdedcpwdedkwDFYVKIedPHYLLRPETIESLFYLYRATGDPKY 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627723  419 LQVGKKALKTLQQHAKVSCGYAAVNDVR--TGKHEDRMDSFVLSETIKYLFLLFSDPQdlIINVDEFVFTTEAHLLPL 494
Cdd:pfam01532 378 REWGWEIFQAIEKYTRTECGYSGLQDVTspPGEKEDNMESFWLAETLKYLYLLFSDDD--LLSLDEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
43-497 3.34e-83

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 275.06  E-value: 3.34e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  43 SNKERaelREEARDMFYHAYNAYMQNAYPADELMPLSckGRYRGvtpsrgdmddiLGNFSMTLVDTLDTLVLLGDFTEFD 122
Cdd:PTZ00470  68 LNIKR---RESVREAMKHAWEGYKEYAWGHDELRPLT--KRHHE-----------WFGLGLTIIDSLDTLKIMGLKKEYK 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 123 HAVKLVIRDVQFDSDI--IVSVFETNIRMVGGLLSAHILAEylqkhaDTMHWYKGellemsRELGYRLLPAFNTSTGIPH 200
Cdd:PTZ00470 132 EGRDWVANNLKQSKDTglGVSVFETTIRVLGGLLSAYDLTG------DEMYLEKA------REIADRLLPAFNEDTGFPA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 201 ARVNLRLGMKDPMLKKSRETCTACAGTILLEFAALSRLTGDPIFEVRAHAAMDALWKLRHRGSDLMGTVLNVHSGDWVRR 280
Cdd:PTZ00470 200 SEINLATGRKSYPGWAGGCSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGLYPIFLNPDAGRFCGN 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 281 DSGVGAGIDSYYEYLFKSYVLL--GDDKYLarfnRHYNAVMK---------------YVSEgpMLLDVLMHRphaksknf 343
Cdd:PTZ00470 280 HISLGALGDSYYEYLLKQWLYTngREERYR----RLFVESAKgiiehlykrspkgltYIAE--MDGGSLTNK-------- 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 344 MDSLLAFWPGLQVLSGDLKpAVQTHEMLYQVM---------------QMHTFI-PEAFTVD-------FQIHWGQHPLRP 400
Cdd:PTZ00470 346 MEHLACFAGGMFALGAAIN-ITPDDEKSARYMevgeevtktcyetyaTSPTGLgPEIFHFDpnsgdisPNVHDSHYILRP 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 401 EFIESTYFLYRATGDHHYLQVGKKALKTLQQHAKVSCGYAAVNDVRT--GKHEDRMDSFVLSETIKYLFLLFSDpqDLII 478
Cdd:PTZ00470 425 ETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTvhPQQDDFQESFFLAETLKYLYLLFQP--DHVI 502
                        490
                 ....*....|....*....
gi 442627723 479 NVDEFVFTTEAHllPLSIA 497
Cdd:PTZ00470 503 PLDKYVFNTEAH--PIPIQ 519
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
636-761 1.42e-62

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: 205.67  E-value: 1.42e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 636 MAGPSHFSPELTGDQFVEGDVILAKPLRACDEsLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSG 715
Cdd:cd02126    1 TAGPAQFGMDLTGDKAGVGRVVKAKPYRACSE-ITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNEGSSS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 442627723 716 ETQPMFAMSGDG--KDDVLIPVVFMYSMEFGKLSAVMQrRKQPLRVRV 761
Cdd:cd02126   80 DTAPMFAMSGDGdsTDDVTIPVVFLFSKEGSKLLAAIK-EHQNVEVLL 126
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
639-739 2.43e-12

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: 70.84  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 639 PSHFSPELTGDQfVEGDVILAK-----PLRACDeSLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGS 713
Cdd:NF038113 428 RAGFGPRLPDAP-ITGDLALATdsspdPNDGCD-PILNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGE 505
                         90       100
                 ....*....|....*....|....*..
gi 442627723 714 SgetqpmFAMSGDGKDD-VLIPVVFMY 739
Cdd:NF038113 506 P------IVMGGGDTGPpITIPSIMIS 526
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
653-745 3.23e-11

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: 60.22  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  653 EGDVILAKPLRACDESlENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSGETQPMFAMSGDgkDDVL 732
Cdd:pfam02225   1 TGPLVLAPGCYAGDGI-PADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPPGAGGNELYP--DGIY 77
                          90
                  ....*....|...
gi 442627723  733 IPVVFMySMEFGK 745
Cdd:pfam02225  78 IPAVGV-SRADGE 89
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
638-736 3.19e-10

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: 63.91  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  638 GPSHFSpeltgdqfVEGDVILAK-----PLRACDEsLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPG 712
Cdd:NF038112  511 GPQAFD--------VTGDVVLAPdgtgsDTDGCTP-FTNAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVIIANNAAG 581
                          90       100
                  ....*....|....*....|....*
gi 442627723  713 SsgetqpmfAMSGDGKD-DVLIPVV 736
Cdd:NF038112  582 A--------APGLGGTDpAVTIPAL 598
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
57-494 1.16e-155

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 460.87  E-value: 1.16e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723   57 MFYHAYNAYMQNAYPADELMPLSCKGRyrgvtpsrgdmdDILGNFSMTLVDTLDTLVLLGDFTEFDHAVKLVIRDVQFDS 136
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGN------------DTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  137 D-IIVSVFETNIRMVGGLLSAHILAEylqkhadtmhWYKGELLEMSRELGYRLLPAFNTSTGIPHARVNLRLGMKDPMLK 215
Cdd:pfam01532  69 DsTEVSVFETTIRYLGGLLSAYDLSG----------DGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  216 KSRETCTACAGTILLEFAALSRLTGDPIFEVRAHAAMDALWK--LRHRGSDLMGTVLNVHSGDWVRRDSGVGAGIDSYYE 293
Cdd:pfam01532 139 AGGASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqSRTPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYE 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  294 YLFKSYVLLG--DDKYLARFNRHYNAVMKYVSEGPMLLDVLM---HRPHAKSKNF---MDSLLAFWPGLQVL-------- 357
Cdd:pfam01532 219 YLLKQYLLTGgtDPEYRDMYEEAMDAIKKHLLFRPSTPSDLLfigELDSGGGGKLspkMDHLSCFAGGMLALgatlglpr 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  358 SGDLKPAVQTHEM---LYQVMQMHTfIPEAFTV--------------DFQIHW--GQHPLRPEFIESTYFLYRATGDHHY 418
Cdd:pfam01532 299 EGDLELAEKLTEGcykTYDSTPTGL-GPEIFYFdpcdedcpwdedkwDFYVKIedPHYLLRPETIESLFYLYRATGDPKY 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627723  419 LQVGKKALKTLQQHAKVSCGYAAVNDVR--TGKHEDRMDSFVLSETIKYLFLLFSDPQdlIINVDEFVFTTEAHLLPL 494
Cdd:pfam01532 378 REWGWEIFQAIEKYTRTECGYSGLQDVTspPGEKEDNMESFWLAETLKYLYLLFSDDD--LLSLDEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
43-497 3.34e-83

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 275.06  E-value: 3.34e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  43 SNKERaelREEARDMFYHAYNAYMQNAYPADELMPLSckGRYRGvtpsrgdmddiLGNFSMTLVDTLDTLVLLGDFTEFD 122
Cdd:PTZ00470  68 LNIKR---RESVREAMKHAWEGYKEYAWGHDELRPLT--KRHHE-----------WFGLGLTIIDSLDTLKIMGLKKEYK 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 123 HAVKLVIRDVQFDSDI--IVSVFETNIRMVGGLLSAHILAEylqkhaDTMHWYKGellemsRELGYRLLPAFNTSTGIPH 200
Cdd:PTZ00470 132 EGRDWVANNLKQSKDTglGVSVFETTIRVLGGLLSAYDLTG------DEMYLEKA------REIADRLLPAFNEDTGFPA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 201 ARVNLRLGMKDPMLKKSRETCTACAGTILLEFAALSRLTGDPIFEVRAHAAMDALWKLRHRGSDLMGTVLNVHSGDWVRR 280
Cdd:PTZ00470 200 SEINLATGRKSYPGWAGGCSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGLYPIFLNPDAGRFCGN 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 281 DSGVGAGIDSYYEYLFKSYVLL--GDDKYLarfnRHYNAVMK---------------YVSEgpMLLDVLMHRphaksknf 343
Cdd:PTZ00470 280 HISLGALGDSYYEYLLKQWLYTngREERYR----RLFVESAKgiiehlykrspkgltYIAE--MDGGSLTNK-------- 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 344 MDSLLAFWPGLQVLSGDLKpAVQTHEMLYQVM---------------QMHTFI-PEAFTVD-------FQIHWGQHPLRP 400
Cdd:PTZ00470 346 MEHLACFAGGMFALGAAIN-ITPDDEKSARYMevgeevtktcyetyaTSPTGLgPEIFHFDpnsgdisPNVHDSHYILRP 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 401 EFIESTYFLYRATGDHHYLQVGKKALKTLQQHAKVSCGYAAVNDVRT--GKHEDRMDSFVLSETIKYLFLLFSDpqDLII 478
Cdd:PTZ00470 425 ETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTvhPQQDDFQESFFLAETLKYLYLLFQP--DHVI 502
                        490
                 ....*....|....*....
gi 442627723 479 NVDEFVFTTEAHllPLSIA 497
Cdd:PTZ00470 503 PLDKYVFNTEAH--PIPIQ 519
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
636-761 1.42e-62

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: 205.67  E-value: 1.42e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 636 MAGPSHFSPELTGDQFVEGDVILAKPLRACDEsLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSG 715
Cdd:cd02126    1 TAGPAQFGMDLTGDKAGVGRVVKAKPYRACSE-ITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNEGSSS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 442627723 716 ETQPMFAMSGDG--KDDVLIPVVFMYSMEFGKLSAVMQrRKQPLRVRV 761
Cdd:cd02126   80 DTAPMFAMSGDGdsTDDVTIPVVFLFSKEGSKLLAAIK-EHQNVEVLL 126
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
651-738 7.78e-16

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: 74.33  E-value: 7.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 651 FVEGDVILAKPLRACDEsLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSGETQPMfaMSGDGKDD 730
Cdd:cd02127   10 YKHVPLVPADPLEACEE-LRNIHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNNDSDEYYVEM--IQDDSSRR 86

                 ....*...
gi 442627723 731 VLIPVVFM 738
Cdd:cd02127   87 ADIPAAFL 94
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
638-738 1.42e-14

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: 70.82  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 638 GPSHFSPELTG--DQFVEGDVILAKPLRACDeSLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSsg 715
Cdd:cd04818    1 VSAGFGPALTNvtADVVLAGAAPASNTDGCT-AFTNAAAFAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVANNVAGG-- 77
                         90       100
                 ....*....|....*....|...
gi 442627723 716 etqPMFAMSGDGkDDVLIPVVFM 738
Cdd:cd04818   78 ---APITMGGDD-PDITIPAVMI 96
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
611-737 3.22e-14

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: 70.83  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 611 SINQLAQLQAVAYATDENSQDWIALmagPSHFSPELTGDQFvEGDVILAKPLRACdESLENAEEAKGK-----VLVaERG 685
Cdd:cd02123    3 VVSPLATADKLALADSNLTDEFDDL---PANFGPIPPGSGL-KGVLVVAEPLNAC-SPIENPPLNSNAsgsfiVLI-RRG 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442627723 686 DCTFVSKARLAQKVGAAALIVCDNVpgsSGETQPMFAMSGDGKdDVLIPVVF 737
Cdd:cd02123   77 NCSFETKVRNAQRAGYKAAIVYNDE---SNDLISMSGNDQEIK-GIDIPSVF 124
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
659-738 4.25e-13

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: 66.77  E-value: 4.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 659 AKPLRACDESLE--NAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSgetqPMFAMSGDGKDDVLIPVV 736
Cdd:cd00538   27 AGPLVGCGYGTTddSGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGDDPG----PQMGSVGLESTDPSIPTV 102

                 ..
gi 442627723 737 FM 738
Cdd:cd00538  103 GI 104
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
639-739 2.43e-12

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: 70.84  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 639 PSHFSPELTGDQfVEGDVILAK-----PLRACDeSLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGS 713
Cdd:NF038113 428 RAGFGPRLPDAP-ITGDLALATdsspdPNDGCD-PILNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGE 505
                         90       100
                 ....*....|....*....|....*..
gi 442627723 714 SgetqpmFAMSGDGKDD-VLIPVVFMY 739
Cdd:NF038113 506 P------IVMGGGDTGPpITIPSIMIS 526
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
661-750 1.59e-11

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: 62.02  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 661 PLRACDeSLENAEEaKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSGETqpMFAMSGDgkDDVLIPVVFMYS 740
Cdd:cd04813   26 PTDACS-LQEHAEI-DGKVALVLRGGCGFLDKVMWAQRRGAKAVIVGDDEPGRGLIT--MFSNGDT--DNVTIPAMFTSR 99
                         90
                 ....*....|
gi 442627723 741 MEFGKLSAVM 750
Cdd:cd04813  100 TSYHLLSSLL 109
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
653-745 3.23e-11

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: 60.22  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  653 EGDVILAKPLRACDESlENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSSGETQPMFAMSGDgkDDVL 732
Cdd:pfam02225   1 TGPLVLAPGCYAGDGI-PADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPPGAGGNELYP--DGIY 77
                          90
                  ....*....|...
gi 442627723  733 IPVVFMySMEFGK 745
Cdd:pfam02225  78 IPAVGV-SRADGE 89
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
671-755 5.97e-11

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: 61.15  E-value: 5.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 671 NAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGSsgetqpmFAMSGDGKDDvlIPVVFMySMEFG-KLSAV 749
Cdd:cd02133   42 EGKDVKGKIALIQRGEITFVEKIANAKAAGAVGVIIYNNVDGL-------IPGTLGEAVF--IPVVFI-SKEDGeALKAA 111

                 ....*.
gi 442627723 750 MQRRKQ 755
Cdd:cd02133  112 LESSKK 117
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
638-736 3.19e-10

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: 63.91  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723  638 GPSHFSpeltgdqfVEGDVILAK-----PLRACDEsLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPG 712
Cdd:NF038112  511 GPQAFD--------VTGDVVLAPdgtgsDTDGCTP-FTNAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVIIANNAAG 581
                          90       100
                  ....*....|....*....|....*
gi 442627723  713 SsgetqpmfAMSGDGKD-DVLIPVV 736
Cdd:NF038112  582 A--------APGLGGTDpAVTIPAL 598
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
634-728 7.50e-10

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: 57.27  E-value: 7.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 634 ALMAGPSHFSPelTGDqfVEGDVILAKPLrACDESlENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVP-- 711
Cdd:cd02130    8 AIPTTAFTYSP--AGE--VTGPLVVVPNL-GCDAA-DYPASVAGNIALIERGECPFGDKSALAGAAGAAAAIIYNNVPag 81
                         90       100
                 ....*....|....*....|....*
gi 442627723 712 ---GSSGE----TQPMFAMSG-DGK 728
Cdd:cd02130   82 glsGTLGEpsgpYVPTVGISQeDGK 106
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
647-750 1.52e-09

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: 57.05  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 647 TGDQFVEGDVILAKPLRACDESlenAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPgssgETQPMFAMSGD 726
Cdd:cd02132   33 KEDNANKTRAVLANPLDCCSPS---TSKLSGSIALVERGECAFTEKAKIAEAGGASALLIINDQE----ELYKMVCEDND 105
                         90       100
                 ....*....|....*....|....*
gi 442627723 727 GKDDVLIPVVfMYSMEFG-KLSAVM 750
Cdd:cd02132  106 TSLNISIPVV-MIPQSAGdALNKSL 129
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
647-737 1.98e-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: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 647 TGDQFVEGDVILAKPLR--ACDESLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDNVPGssGETQPMFams 724
Cdd:cd04816   12 TPPGGVTAPLVPLDPERpaGCDASDYDGLDVKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSDG--GGTAGTL--- 86
                         90
                 ....*....|...
gi 442627723 725 GDGKDDVLIPVVF 737
Cdd:cd04816   87 GAPNIDLKVPVGV 99
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
665-738 2.20e-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: 53.16  E-value: 2.20e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627723 665 CDESLENAEEAKGKVLVAERGDCTFVSKARLAQKVGAAALIVCDN---VPGSSGETQPmfamsgdgkDDVLIPVVFM 738
Cdd:cd02129   33 CSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRerlVPPSGNRSEY---------EKIDIPVALL 100
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
679-736 8.91e-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: 42.85  E-value: 8.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627723 679 VLVAERGDCTFVSKARLAQKVGAAALIVCDNVpgssgeTQPMFAM-----SGDGK--DDVLIPVV 736
Cdd:cd02125   45 ILLLDRGGCFFTLKAWNAQQAGAAAVLVADNV------DEPLLTMdtpeeSGSADyiEKITIPSA 103
PA_GRAIL_like cd02122
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ...
660-755 2.41e-04

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: 41.90  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627723 660 KPLRACDESLENAEEAKGKVLVA--ERGDCTFVSKARLAQKVGAAALIVCdNVPGSSGETqpmFAMSGDGKDDVlipVVF 737
Cdd:cd02122   42 NDHYGCDPDTRFPIPPNGEPWIAliQRGNCTFEEKIKLAAERNASAVVIY-NNPGTGNET---VKMSHPGTGDI---VAI 114
                         90
                 ....*....|....*....
gi 442627723 738 MYSMEFGK-LSAVMQRRKQ 755
Cdd:cd02122  115 MITNPKGMeILELLERGIS 133
 
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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