NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|86577810|gb|AAI13159|]
View 

4833403I15Rik protein [Mus musculus]

Protein Classification

M1 family metallopeptidase( domain architecture ID 10176152)

M1 family metallopeptidase is a zinc-dependent metallopeptidase that functions as an aminopeptidase and contains an HEXXH motif as part of its active site

CATH:  1.10.390.10|2.60.40.1840|1.25.50.10
EC:  3.4.11.-
Gene Ontology:  GO:0008270|GO:0008237|GO:0004177|GO:0006508
MEROPS:  M1
PubMed:  31351924|7674922|37216842|21258033|10493853

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
M1_APN-Q_like cd09601
Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), ...
 102-549 8.20e-175

Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1); This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


:

Pssm-ID: 341064 [Multi-domain]  Cd Length: 442  Bit Score: 501.34  E-value: 8.20e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 102 LHYDLELWPWLQpdklsppNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVwgplaqdtRNATVGRVQVEKVWFAPD 181
Cdd:cd09601   1 LHYDLTLTPDLE-------NFTFSGSVTITLEVLEPTDTIVLHAKDLTITSASL--------TLKGGSGIIEVTVVTDEE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 182 MQFVVLDLGQSLEPGSRYELSFHFSGQvLQVGLEGLFLNLYHDED-ELRALVATQMEPTFARHVFPCFDEPALKATFNIT 260
Cdd:cd09601  66 TEFLTITLDETLPPGENYTLSIEFTGK-LNDDLRGFYRSSYTDEDgETRYLAATQFEPTDARRAFPCFDEPAFKATFDIT 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 261 VIHHPGYAALSNMPQLGQSEridvNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISR-TERGKEIRVWARKDDIanGYLD 339
Cdd:cd09601 145 ITHPKGYTALSNMPPVESTE----LEDGWKTTTFETTPPMSTYLVAFVVGDFEYIEStTKSGVPVRVYARPGKI--EQGD 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 340 FAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWF 419
Cdd:cd09601 219 FALEVAPKILDFYEDYFGIPYPLPKLDLVAIPDFAAGAMENWGLITYRETALLYDPKTSSASDKQRVAEVIAHELAHQWF 298

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 420 GNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENfteTSEINRLFDLY 499
Cdd:cd09601 299 GNLVTMKWWDDLWLNEGFATYMEYLAVDKLFPEWNMWDQFVVDELQSALELDSLASSHPIEVPVES---PSEISEIFDAI 375

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 86577810 500 TYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVI 549
Cdd:cd09601 376 SYSKGASVLRMLENFLGEEVFRKGLRKYLKKHAYGNATTDDLWEALQEAS 425
 
Name Accession Description Interval E-value
M1_APN-Q_like cd09601
Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), ...
 102-549 8.20e-175

Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1); This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341064 [Multi-domain]  Cd Length: 442  Bit Score: 501.34  E-value: 8.20e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 102 LHYDLELWPWLQpdklsppNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVwgplaqdtRNATVGRVQVEKVWFAPD 181
Cdd:cd09601   1 LHYDLTLTPDLE-------NFTFSGSVTITLEVLEPTDTIVLHAKDLTITSASL--------TLKGGSGIIEVTVVTDEE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 182 MQFVVLDLGQSLEPGSRYELSFHFSGQvLQVGLEGLFLNLYHDED-ELRALVATQMEPTFARHVFPCFDEPALKATFNIT 260
Cdd:cd09601  66 TEFLTITLDETLPPGENYTLSIEFTGK-LNDDLRGFYRSSYTDEDgETRYLAATQFEPTDARRAFPCFDEPAFKATFDIT 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 261 VIHHPGYAALSNMPQLGQSEridvNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISR-TERGKEIRVWARKDDIanGYLD 339
Cdd:cd09601 145 ITHPKGYTALSNMPPVESTE----LEDGWKTTTFETTPPMSTYLVAFVVGDFEYIEStTKSGVPVRVYARPGKI--EQGD 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 340 FAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWF 419
Cdd:cd09601 219 FALEVAPKILDFYEDYFGIPYPLPKLDLVAIPDFAAGAMENWGLITYRETALLYDPKTSSASDKQRVAEVIAHELAHQWF 298

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 420 GNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENfteTSEINRLFDLY 499
Cdd:cd09601 299 GNLVTMKWWDDLWLNEGFATYMEYLAVDKLFPEWNMWDQFVVDELQSALELDSLASSHPIEVPVES---PSEISEIFDAI 375

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 86577810 500 TYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVI 549
Cdd:cd09601 376 SYSKGASVLRMLENFLGEEVFRKGLRKYLKKHAYGNATTDDLWEALQEAS 425
PepN COG0308
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];
94-546 1.54e-103

Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];


Pssm-ID: 440077 [Multi-domain]  Cd Length: 609  Bit Score: 324.29  E-value: 1.54e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810  94 RLPPWLVPLHYDLELwpwlqpdKLSPPNLTFTGRVNITVRCTVASsrllLHSFLLnykqvevwgplaqDTRNATVGRVQV 173
Cdd:COG0308  10 YRPPGYDVTHYDLDL-------DLDPATTRLSGTATITFTATEAP----LDSLVL-------------DLKGLEVTSVTV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 174 --EKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGqVLQVGLEGLFLnlYHDEDELRALVATQMEPTFARHVFPCFDEP 251
Cdd:COG0308  66 dgKPLDFTRDGERLTITLPKPLAPGETFTLEIEYSG-KPSNGGEGLYR--SGDPPDGPPYLYTQCEPEGARRWFPCFDHP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 252 ALKATFNITVIHHPGYAALSNMPQLGQSEridvNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRT-ERGKEIRVWARK 330
Cdd:COG0308 143 DDKATFTLTVTVPAGWVAVSNGNLVSETE----LGDGRTTWHWADTQPIPTYLFALAAGDYAVVEDTfASGVPLRVYVRP 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 331 DDIAngYLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRamILSII 410
Cdd:COG0308 219 GLAD--KAKEAFESTKRMLDFFEELFGVPYPFDKYDQVAVPDFNFGAMENQGLVTFGEKVLADETATDADYER--RESVI 294

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 411 AHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTavenfTETS 490
Cdd:COG0308 295 AHELAHQWFGNLVTCADWDDLWLNEGFATYMEQLFSEDLYGKDAADRIFVGALRSYAFAEDAGPNAHPIRP-----DDYP 369

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 86577810 491 EINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQ 546
Cdd:COG0308 370 EIENFFDGIVYEKGALVLHMLRTLLGDEAFRAGLRLYFARHAGGNATTEDFLAALE 425
Peptidase_M1 pfam01433
Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ ...
 340-546 6.34e-68

Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase, this enzyme also has an aminopeptidase activity.


Pssm-ID: 426262 [Multi-domain]  Cd Length: 219  Bit Score: 218.70  E-value: 6.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   340 FAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWF 419
Cdd:pfam01433   1 YALEITVKLLEFYEDYFNIPYPLPKYDLVALPDFSAGAMENWGLITYRETLLLYDPGNSSTSDKQRVASVIAHELAHQWF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   420 GNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENFTETSEInrlFDLY 499
Cdd:pfam01433  81 GNLVTMKWWDDLWLNEGFATYMEYLGTDALFPEWNIWEQFLLDEVQNAMARDALDSSHPITQNVNDPSEIDDI---FDAI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 86577810   500 TYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQ 546
Cdd:pfam01433 158 PYEKGASVLRMLETLLGEEVFQKGLRSYLKKFQYGNATTEDLWDALS 204
pepN_strep_liv TIGR02412
aminopeptidase N, Streptomyces lividans type; This family is a subset of the members of the ...
 234-545 3.09e-46

aminopeptidase N, Streptomyces lividans type; This family is a subset of the members of the zinc metallopeptidase family M1 (pfam01433), with a single member characterized in Streptomyces lividans 66 and designated aminopeptidase N. The spectrum of activity may differ somewhat from the aminopeptidase N clade of E. coli and most other Proteobacteria, well separated phylogenetically within the M1 family. The M1 family also includes leukotriene A-4 hydrolase/aminopeptidase (with a bifunctional active site).


Pssm-ID: 274121 [Multi-domain]  Cd Length: 831  Bit Score: 173.82  E-value: 3.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   234 TQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNmpQLGQSERIDVNGSRWTvttFHTTPRMPTYLVALVVCDLD 313
Cdd:TIGR02412 122 TQFEPADARRVFAVFDQPDLKANFKFSVKAPEDWTVISN--SRETDVTPEPADRRWE---FPETPKLSTYLTAVAAGPYH 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   314 HISRTERGKEIRVWARKDdiANGYLDFAA--NITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSL 391
Cdd:TIGR02412 197 SVQDESRSYPLGIYARRS--LAQYLDADAifTITRQGLAFFHRKFGYPYPFKKYDQIFVPEFNAGAMENAGCVTFAENFL 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   392 LL-EPEDELTEKRAMIlsiIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFEL-------ELTNYFypkvpmnmiffftV 463
Cdd:TIGR02412 275 HRaEATRAEKENRAGV---ILHEMAHMWFGDLVTMRWWNDLWLNESFAEYMGTlasaeatEYTDAW-------------T 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   464 LHGILGEDHALESRAVSTA---VENFTETSEINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDD 540
Cdd:TIGR02412 339 TFAAQGKQWAYEADQLPTThpiVADVADLADALSNFDGITYAKGASVLKQLVAWVGEEAFFAGVNAYFKRHAFGNATLDD 418


                  ....*
gi 86577810   541 LWRHI 545
Cdd:TIGR02412 419 LIDSL 423
pepN PRK14015
aminopeptidase N; Provisional
 301-437 6.52e-10

aminopeptidase N; Provisional


Pssm-ID: 237585 [Multi-domain]  Cd Length: 875  Bit Score: 62.07  E-value: 6.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810  301 PTYLVALVVCDLDHIS---RTERGKE--IRVWARKDDIanGYLDFAANitgpifSfL-------EDLFNISYRLPKTDIV 368
Cdd:PRK14015 188 PSYLFALVAGDLDVLEdtfTTRSGREvaLEIYVEPGNL--DKCDHAMD------S-LkksmkwdEERFGLEYDLDIFMIV 258

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86577810  369 ALPIFASGAMENWGLLIFDESSLLLEPE----DELtekrAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGF 437
Cdd:PRK14015 259 AVDDFNMGAMENKGLNIFNSKYVLADPEtatdADY----ERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGL 327
 
Name Accession Description Interval E-value
M1_APN-Q_like cd09601
Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), ...
 102-549 8.20e-175

Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1); This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341064 [Multi-domain]  Cd Length: 442  Bit Score: 501.34  E-value: 8.20e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 102 LHYDLELWPWLQpdklsppNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVwgplaqdtRNATVGRVQVEKVWFAPD 181
Cdd:cd09601   1 LHYDLTLTPDLE-------NFTFSGSVTITLEVLEPTDTIVLHAKDLTITSASL--------TLKGGSGIIEVTVVTDEE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 182 MQFVVLDLGQSLEPGSRYELSFHFSGQvLQVGLEGLFLNLYHDED-ELRALVATQMEPTFARHVFPCFDEPALKATFNIT 260
Cdd:cd09601  66 TEFLTITLDETLPPGENYTLSIEFTGK-LNDDLRGFYRSSYTDEDgETRYLAATQFEPTDARRAFPCFDEPAFKATFDIT 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 261 VIHHPGYAALSNMPQLGQSEridvNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISR-TERGKEIRVWARKDDIanGYLD 339
Cdd:cd09601 145 ITHPKGYTALSNMPPVESTE----LEDGWKTTTFETTPPMSTYLVAFVVGDFEYIEStTKSGVPVRVYARPGKI--EQGD 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 340 FAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWF 419
Cdd:cd09601 219 FALEVAPKILDFYEDYFGIPYPLPKLDLVAIPDFAAGAMENWGLITYRETALLYDPKTSSASDKQRVAEVIAHELAHQWF 298

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 420 GNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENfteTSEINRLFDLY 499
Cdd:cd09601 299 GNLVTMKWWDDLWLNEGFATYMEYLAVDKLFPEWNMWDQFVVDELQSALELDSLASSHPIEVPVES---PSEISEIFDAI 375

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 86577810 500 TYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVI 549
Cdd:cd09601 376 SYSKGASVLRMLENFLGEEVFRKGLRKYLKKHAYGNATTDDLWEALQEAS 425
PepN COG0308
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];
94-546 1.54e-103

Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];


Pssm-ID: 440077 [Multi-domain]  Cd Length: 609  Bit Score: 324.29  E-value: 1.54e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810  94 RLPPWLVPLHYDLELwpwlqpdKLSPPNLTFTGRVNITVRCTVASsrllLHSFLLnykqvevwgplaqDTRNATVGRVQV 173
Cdd:COG0308  10 YRPPGYDVTHYDLDL-------DLDPATTRLSGTATITFTATEAP----LDSLVL-------------DLKGLEVTSVTV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 174 --EKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGqVLQVGLEGLFLnlYHDEDELRALVATQMEPTFARHVFPCFDEP 251
Cdd:COG0308  66 dgKPLDFTRDGERLTITLPKPLAPGETFTLEIEYSG-KPSNGGEGLYR--SGDPPDGPPYLYTQCEPEGARRWFPCFDHP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 252 ALKATFNITVIHHPGYAALSNMPQLGQSEridvNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRT-ERGKEIRVWARK 330
Cdd:COG0308 143 DDKATFTLTVTVPAGWVAVSNGNLVSETE----LGDGRTTWHWADTQPIPTYLFALAAGDYAVVEDTfASGVPLRVYVRP 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 331 DDIAngYLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRamILSII 410
Cdd:COG0308 219 GLAD--KAKEAFESTKRMLDFFEELFGVPYPFDKYDQVAVPDFNFGAMENQGLVTFGEKVLADETATDADYER--RESVI 294

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 411 AHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTavenfTETS 490
Cdd:COG0308 295 AHELAHQWFGNLVTCADWDDLWLNEGFATYMEQLFSEDLYGKDAADRIFVGALRSYAFAEDAGPNAHPIRP-----DDYP 369

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 86577810 491 EINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQ 546
Cdd:COG0308 370 EIENFFDGIVYEKGALVLHMLRTLLGDEAFRAGLRLYFARHAGGNATTEDFLAALE 425
M1 cd09595
Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 ...
 103-542 6.95e-74

Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 hydrolase; The model represents the catalytic domains of M1 peptidase family members including aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile upon activation during catalysis. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. APN expression is dysregulated in many inflammatory diseases and is enhanced in numerous tumor cells, making it a lead target in the development of anti-cancer and anti-inflammatory drugs. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase in LTA4H is as yet unknown, while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals.


Pssm-ID: 341058 [Multi-domain]  Cd Length: 413  Bit Score: 241.20  E-value: 6.95e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 103 HYDLELwpwlqpdKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGplaQDTRNATVGRVQVEKVWFAPDm 182
Cdd:cd09595   2 HYDLDL-------DVDFTTKTLNGTETLTVDASQVGRELVLDLVGLTIHSVSVNG---AAVDFGEREHYDGEKLTIPGP- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 183 qfvvldlgqsLEPGSRYELSFHFSGQVLQVGLegLFLNLYHDEDElRALVATQMEPTFARHVFPCFDEPALKATFNITVI 262
Cdd:cd09595  71 ----------KPPGQTFTVRISFEAKPSKNLL--GWLWEQTAGKE-KPYLFTQFEATHARRIFPCIDHPAVKATFTVTIT 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 263 HHPGYAALSNMPQLGqsERIDVNGSRWTvtTFHTTPRMPTYLVALVVCDLDHISRT---ERGKEIRVWARKDDIANgyLD 339
Cdd:cd09595 138 TPKKDLLASNGALVG--EETGANGRKTY--RFEDTPPIPTYLVAVVVGDLEFKYVTvksQPRVGLSVYSEPLQVDQ--AQ 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 340 FAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRamILSIIAHEVGHQWF 419
Cdd:cd09595 212 YAFDATRAALAWFEDYFGGPYPLPKYDLLAVPDFNSGAMENPGLITFRTTYLLRSKVTDTGARS--IENVIAHELAHQWF 289

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 420 GNLVTMSWWNNIWLNEGFASYFELELTNYFYPKvpmnmifFFTVLHGILGEDHALESRAVSTAVENFTET---SEINRLF 496
Cdd:cd09595 290 GNLVTMRWWNDLWLNEGFAVYYENRIMDATFGT-------SSRHLDQLSGSSDLNTEQLLEDSSPTSTPVrspADPDVAY 362

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 86577810 497 DLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLW 542
Cdd:cd09595 363 DGVTYAKGALVLRMLEELVGEEAFDKGVQAYFNRHKFKNATTDDFI 408
M1_APN cd09602
Peptidase M1 family including aminopeptidase N catalytic domain; This model represents the ...
 102-547 1.17e-68

Peptidase M1 family including aminopeptidase N catalytic domain; This model represents the catalytic domain of bacterial and eukaryotic aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341065 [Multi-domain]  Cd Length: 440  Bit Score: 228.17  E-value: 1.17e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 102 LHYDLELwpwlqpdKLSPPNLTFTGRVNITVRCTVASSRLLL-------HSFLLNYKQVevwgplaqDTRNATVGRVQVE 174
Cdd:cd09602  16 VSYDLDL-------DLTEGAETFRGTVTIRFTLREPGASLFLdfrggevKSVTLNGRPL--------DPSAFDGERITLP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 175 KVWFAPDMQFVVldlgqslepgsRYELSFHFSGqvlqvglEGLflNLYHDEDELRALVATQMEPTFARHVFPCFDEPALK 254
Cdd:cd09602  81 GLLKAGENTVVV-----------EFTAPYSSDG-------EGL--HRFVDPADGETYLYTLFEPDDARRVFPCFDQPDLK 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 255 ATFNITVIHHPGYAALSNMPQLGQSERIDVNgsRWTvttFHTTPRMPTYLVALVVCDLDHISRTERGKEIRVWARKDDIA 334
Cdd:cd09602 141 ATFTLTVTAPADWTVISNGPETSTEEAGGRK--RWR---FAETPPLSTYLFAFVAGPYHRVEDEHDGIPLGLYCRESLAE 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 335 NG-YLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEP--EDELtEKRAmilSIIA 411
Cdd:cd09602 216 YErDADEIFEVTKQGLDFYEDYFGIPYPFGKYDQVFVPEFNFGAMENPGAVTFRESYLFREEptRAQR-LRRA---NTIL 291

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 412 HEVGHQWFGNLVTMSWWNNIWLNEGFASYFE----LELTNYFYPKVpmnmIFFFTVLHGILGEDHALESRAVSTAVENfT 487
Cdd:cd09602 292 HEMAHMWFGDLVTMKWWDDLWLNESFADFMAakalAEATPFTDAWL----TFLLRRKPWAYRADQLPTTHPIAQDVPD-L 366

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 488 ETSEINrlFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQM 547
Cdd:cd09602 367 EAAGSN--FDGITYAKGASVLKQLVALVGEEAFRAGLREYFKKHAYGNATLDDLIAALDE 424
Peptidase_M1 pfam01433
Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ ...
 340-546 6.34e-68

Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase, this enzyme also has an aminopeptidase activity.


Pssm-ID: 426262 [Multi-domain]  Cd Length: 219  Bit Score: 218.70  E-value: 6.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   340 FAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWF 419
Cdd:pfam01433   1 YALEITVKLLEFYEDYFNIPYPLPKYDLVALPDFSAGAMENWGLITYRETLLLYDPGNSSTSDKQRVASVIAHELAHQWF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   420 GNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENFTETSEInrlFDLY 499
Cdd:pfam01433  81 GNLVTMKWWDDLWLNEGFATYMEYLGTDALFPEWNIWEQFLLDEVQNAMARDALDSSHPITQNVNDPSEIDDI---FDAI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 86577810   500 TYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQ 546
Cdd:pfam01433 158 PYEKGASVLRMLETLLGEEVFQKGLRSYLKKFQYGNATTEDLWDALS 204
M1_APN_like cd09603
Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly ...
 102-546 2.73e-64

Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly bacterial and some archaeal M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341066 [Multi-domain]  Cd Length: 410  Bit Score: 215.53  E-value: 2.73e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 102 LHYDLELwpwlqpdKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVwgplaqDTRNATVGRVQVEKVWfapd 181
Cdd:cd09603   4 LHYDLDL-------DYDPATKSLSGTATITFRATQDLDSLQLDLVGLTVSSVTV------DGVPAAFFTHDGDKLV---- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 182 mqfvvLDLGQSLEPGSRYELSFHFSGQVLQVGLEGLFLNLYHDEDELralVATQMEPTFARHVFPCFDEPALKATFNITV 261
Cdd:cd09603  67 -----ITLPRPLAAGETFTVTVRYSGKPRPAGYPPGDGGGWEEGDDG---VWTAGQPEGASTWFPCNDHPDDKATYDITV 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 262 IHHPGYAALSNmpqlGQSERIDVNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRTE-RGKEIRVWARKDDIANGYLDF 340
Cdd:cd09603 139 TVPAGLTVVSN----GRLVSTTTNGGGTTTWHWKMDYPIATYLVTLAVGRYAVVEDGSgGGIPLRYYVPPGDAAKAKASF 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 341 AanITGPIFSFLEDLFnISYRLPKTDIVALPIFaSGAMENWGLLIFDESSLLLEPEDEltekramilSIIAHEVGHQWFG 420
Cdd:cd09603 215 A--RTPEMLDFFEELF-GPYPFEKYGQVVVPDL-GGGMEHQTATTYGNNFLNGDRGSE---------RLIAHELAHQWFG 281

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 421 NLVTMSWWNNIWLNEGFASYFELELTNYFYpkvpmnmiffftvlhgilGEDHALE-----SRAVSTAVENFTETSEINRL 495
Cdd:cd09603 282 DSVTCADWADIWLNEGFATYAEWLWSEHKG------------------GADAYRAylagqRQDYLNADPGPGRPPDPDDL 343

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 86577810 496 FDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQ 546
Cdd:cd09603 344 FDRDVYQKGALVLHMLRNLLGDEAFFAALRAYLARYAHGNVTTEDFIAAAE 394
Peptidase_M1_N pfam17900
Peptidase M1 N-terminal domain; This domain is found at the N-terminus of aminopeptidases from ...
 100-304 1.59e-50

Peptidase M1 N-terminal domain; This domain is found at the N-terminus of aminopeptidases from the M1 family.


Pssm-ID: 465557 [Multi-domain]  Cd Length: 186  Bit Score: 171.76  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   100 VPLHYDLELwpwlQPDklsPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGplaqdtrNATVGRVQVEKVWFA 179
Cdd:pfam17900   1 VPEHYDLDL----KID---LKNFTFSGSVTITLQLNNATNVIVLHASDLTIRSISLSD-------EVTSDGVPADFTEDQ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   180 PDMQFVVLDLGQSLEPGSRYELSFHFSGQvLQVGLEGLFLNLYHDEDELRALVATQMEPTFARHVFPCFDEPALKATFNI 259
Cdd:pfam17900  67 KDGEKLTIVLPETLNQTGPYTLEIEYSGE-LNDSMTGFYRSTYTDNGEKKVLVTTQFEPTDARSAFPCFDEPSVKATFTI 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 86577810   260 TVIHHPGYAALSNMPqLGQSERIDvNGsrWTVTTFHTTPRMPTYL 304
Cdd:pfam17900 146 SIIHPKDYTALSNMP-VIASEPLE-NG--WVITTFEQTPKMSTYL 186
pepN_strep_liv TIGR02412
aminopeptidase N, Streptomyces lividans type; This family is a subset of the members of the ...
 234-545 3.09e-46

aminopeptidase N, Streptomyces lividans type; This family is a subset of the members of the zinc metallopeptidase family M1 (pfam01433), with a single member characterized in Streptomyces lividans 66 and designated aminopeptidase N. The spectrum of activity may differ somewhat from the aminopeptidase N clade of E. coli and most other Proteobacteria, well separated phylogenetically within the M1 family. The M1 family also includes leukotriene A-4 hydrolase/aminopeptidase (with a bifunctional active site).


Pssm-ID: 274121 [Multi-domain]  Cd Length: 831  Bit Score: 173.82  E-value: 3.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   234 TQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNmpQLGQSERIDVNGSRWTvttFHTTPRMPTYLVALVVCDLD 313
Cdd:TIGR02412 122 TQFEPADARRVFAVFDQPDLKANFKFSVKAPEDWTVISN--SRETDVTPEPADRRWE---FPETPKLSTYLTAVAAGPYH 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   314 HISRTERGKEIRVWARKDdiANGYLDFAA--NITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSL 391
Cdd:TIGR02412 197 SVQDESRSYPLGIYARRS--LAQYLDADAifTITRQGLAFFHRKFGYPYPFKKYDQIFVPEFNAGAMENAGCVTFAENFL 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   392 LL-EPEDELTEKRAMIlsiIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFEL-------ELTNYFypkvpmnmiffftV 463
Cdd:TIGR02412 275 HRaEATRAEKENRAGV---ILHEMAHMWFGDLVTMRWWNDLWLNESFAEYMGTlasaeatEYTDAW-------------T 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   464 LHGILGEDHALESRAVSTA---VENFTETSEINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDD 540
Cdd:TIGR02412 339 TFAAQGKQWAYEADQLPTThpiVADVADLADALSNFDGITYAKGASVLKQLVAWVGEEAFFAGVNAYFKRHAFGNATLDD 418


                  ....*
gi 86577810   541 LWRHI 545
Cdd:TIGR02412 419 LIDSL 423
M1_LTA4H cd09599
Peptidase M1 family including Leukotriene A4 hydrolase catalytic domain; This model represents ...
 234-533 1.36e-30

Peptidase M1 family including Leukotriene A4 hydrolase catalytic domain; This model represents the N-terminal catalytic domain of leukotriene A4 hydrolase (LTA4H; E.C. 3.3.2.6) and the close homolog cold-active aminopeptidase (Colwellia psychrerythraea-type peptidase; ColAP), both members of the aminopeptidase M1 family. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase is poorly understood while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals. It accepts a variety of substrates, including some opioid, di- and tripeptides, as well as chromogenic aminoacyl-p-nitroanilide derivatives. The aminopeptidase activity of LTA4H is possibly involved in the processing of peptides related to inflammation and host defense. Kinetic analysis shows that LTA4H hydrolyzes arginyl tripeptides with high efficiency and specificity, indicating its function as an arginyl aminopeptidase. Thermodynamic characterization using different biophysical methods shows that structurally distinct inhibitors of the LTA4H occupy different regions of the binding site; while some (RB202, ARM1 and SC57461A) bind to the hydrophobic hydrolase side, both bestatin and captopril are located at the hydrophilic peptidase side. LTB4H overexpression is associated with different pathological conditions and diseases such as cystic fibrosis, coronary heart disease, sepsis, shock, connective tissue disease, and chronic obstructive pulmonary disease. It is also overexpressed in certain human cancers, and has been identified as a functionally important target for mediating anticancer properties of resveratrol, a well-known red wine polyphenolic compound with cancer chemopreventive activity.


Pssm-ID: 341062 [Multi-domain]  Cd Length: 442  Bit Score: 124.11  E-value: 1.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 234 TQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALsnMPQLGQSERIDVNgsrWTVTTFHTTPRMPTYLVALVVCDLD 313
Cdd:cd09599 129 TQCQAIHARSLFPCQDTPSVKSTYSATVTVPKGLTAL--MSALRTGEKEEAG---TGTYTFEQPVPIPSYLIAIAVGDLE 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 314 HisrTERGKEIRVWARKDDIANGYLDFAAniTGPIFSFLEDLFnISYRLPKTDIVALPI-FASGAMENWGL------LIF 386
Cdd:cd09599 204 S---REIGPRSGVWAEPSVVDAAAEEFAD--TEKFLKAAEKLY-GPYVWGRYDLLVLPPsFPYGGMENPCLtfatptLIA 277

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 387 DESSLLlepedeltekramilSIIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKvpmnmifFFTVLHG 466
Cdd:cd09599 278 GDRSLV---------------DVIAHEIAHSWSGNLVTNANWEHFWLNEGFTVYLERRILERLYGE-------EYRQFEA 335

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86577810 467 ILGEDHALESravstaVENFTETSEINRLFDLYT------------YKKGACMAWMLASFLSPHLFINALKSYLETFSY 533
Cdd:cd09599 336 ILGWKDLQES------IKEFGEDPPYTLLVPDLKgvdpddafssvpYEKGFQFLYYLEQLGGREVFDPFLRAYFKKFAF 408
leuko_A4_hydro TIGR02411
leukotriene A-4 hydrolase/aminopeptidase; Members of this family represent a distinctive ...
 234-540 1.62e-22

leukotriene A-4 hydrolase/aminopeptidase; Members of this family represent a distinctive subset within the zinc metallopeptidase family M1 (pfam01433). The majority of the members of pfam01433 are aminopeptidases, but the sequences in this family for which the function is known are leukotriene A-4 hydrolase. A dual epoxide hydrolase and aminopeptidase activity at the same active site is indicated. The physiological substrate for aminopeptidase activity is not known.


Pssm-ID: 274120 [Multi-domain]  Cd Length: 602  Bit Score: 101.39  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   234 TQMEPTFARHVFPCFDEPALKATFNITvIHHPGYAALSNMPQLGQSEriDVNgsrwtVTTFHTTPRMPTYLVALVVCDLD 313
Cdd:TIGR02411 128 SQCQAIHARSLFPCQDTPSVKSTYTAE-VESPLPVLMSGIRDGETSN--DPG-----KYLFKQKVPIPAYLIAIASGDLA 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   314 hisRTERGKEIRVWARKDDIANGYLDFAANITgpifSFLEDLFNI--SYRLPKTDIVALP-IFASGAMENwGLLIFDESS 390
Cdd:TIGR02411 200 ---SAPIGPRSTVYSEPEQLEKCQYEFENDTE----KFIKTAEDLifPYEWGQYDLLVLPpSFPYGGMEN-PNLTFATPT 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810   391 LLlepedelTEKRAMIlSIIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFY--PKVPMNMIFFFTVLHG-- 466
Cdd:TIGR02411 272 LI-------AGDRSNV-DVIAHELAHSWSGNLVTNCSWEHFWLNEGWTVYLERRIIGRLYgeKTRHFSALIGWGDLQEsv 343

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86577810   467 -ILGEDHALesravSTAVENFTEtSEINRLFDLYTYKKGACMAWMLASFL-SPHLFINALKSYLETFSYSNAEQDD 540
Cdd:TIGR02411 344 kTLGETPEF-----TKLVVDLKD-NDPDDAFSSVPYEKGFNFLFYLEQLLgGPAEFDPFLRHYFKKFAYKSLDTYQ 413
M1_APN cd09600
Peptidase M1 family, including aminopeptidase N catalytic domain; This model represents the ...
 214-546 1.38e-21

Peptidase M1 family, including aminopeptidase N catalytic domain; This model represents the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. It includes bacterial-type alanyl aminopeptidases as well as PfA-M1 aminopeptidase (Plasmodium falciparum-type). APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341063 [Multi-domain]  Cd Length: 434  Bit Score: 97.59  E-value: 1.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 214 LEGLflnlYHDEDELralvATQMEPTFARHVFPCFDEPALKATFNITVI----HHPgyAALSNMPQLGQSEriDVNGSRW 289
Cdd:cd09600  99 LEGL----YKSGGIL----CTQCEAEGFRRITYFPDRPDVMSKFTVTIEadkeKYP--VLLSNGNLIEEGE--LPNGRHF 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 290 TVttFHTTPRMPTYLVALVVCDLDHIS---RTERGKEI--RVWARKDDIAngYLDFAanitgpiFSFL-------EDLFN 357
Cdd:cd09600 167 AV--WEDPFPKPSYLFALVAGDLGSVEdtfTTKSGRKVklRIYVEPGNED--KCHHA-------MESLkkamkwdEERFG 235

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 358 ISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGF 437
Cdd:cd09600 236 LEYDLDLFNIVAVDDFNMGAMENKGLNIFNSKYVLADPETATDADYERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGL 315

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 438 ASYFELEltnyfypkvpmnmiffFTvlhgilgEDhaLESRAVS--TAVEN-----FTETS-------------EINRLFD 497
Cdd:cd09600 316 TVFRDQE----------------FS-------AD--MNSRAVKriEDVRRlrsaqFPEDAgpmahpirpdsyiEINNFYT 370

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 86577810 498 LYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQ 546
Cdd:cd09600 371 VTVYEKGAEVIRMLHTLLGEEGFRKGMDLYFERHDGQAVTCEDFVAAME 419
M1_APN_like cd09604
Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains ...
 314-546 2.45e-19

Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341067 [Multi-domain]  Cd Length: 440  Bit Score: 90.80  E-value: 2.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 314 HISRTERGKEIRVWARKDDIANG--YLDFAANItgpiFSFLEDLFnISYRLPKTDIVALPIFAsGAMEnWGLLIFDESSL 391
Cdd:cd09604 214 VDAATVDGVTVNVYYLPENAEAAerALEYAKDA----LEFFSEKF-GPYPYPELDVVQGPFGG-GGME-YPGLVFIGSRL 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 392 llepedelTEKRAMILSIIAHEVGHQWFGNLVTmswwNNI----WLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGI 467
Cdd:cd09604 287 --------YDPKRSLEGVVVHEIAHQWFYGIVG----NDErrepWLDEGLATYAESLYLEEKYGKEAADELLGRRYYRAY 354

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86577810 468 lgedHALESRAVSTAVENFTETSEinrlFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQ 546
Cdd:cd09604 355 ----ARGPGGPINLPLDTFPDGSY----YSNAVYSKGALFLEELREELGDEAFDKALREYYRRYKFKHPTPEDFFRTAE 425
pepN PRK14015
aminopeptidase N; Provisional
 301-437 6.52e-10

aminopeptidase N; Provisional


Pssm-ID: 237585 [Multi-domain]  Cd Length: 875  Bit Score: 62.07  E-value: 6.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810  301 PTYLVALVVCDLDHIS---RTERGKE--IRVWARKDDIanGYLDFAANitgpifSfL-------EDLFNISYRLPKTDIV 368
Cdd:PRK14015 188 PSYLFALVAGDLDVLEdtfTTRSGREvaLEIYVEPGNL--DKCDHAMD------S-LkksmkwdEERFGLEYDLDIFMIV 258

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86577810  369 ALPIFASGAMENWGLLIFDESSLLLEPE----DELtekrAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGF 437
Cdd:PRK14015 259 AVDDFNMGAMENKGLNIFNSKYVLADPEtatdADY----ERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGL 327
GluZincin cd09594
Gluzincin Peptidase family (thermolysin-like proteinases, TLPs) which includes peptidases M1, ...
 344-443 2.05e-06

Gluzincin Peptidase family (thermolysin-like proteinases, TLPs) which includes peptidases M1, M2, M3, M4, M13, M32 and M36 (fungalysins); The Gluzincin family (thermolysin-like peptidases or TLPs) includes several zinc-dependent metallopeptidases such as M1, M2, M3, M4, M13, M32, M36 peptidases (MEROPS classification), which contain the HEXXH motif as part of their active site. Peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The M1 family includes aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity such that the two activities occupy different, but overlapping sites. The M3_like peptidases include the M2_ACE, M3 or neurolysin-like family (subfamilies M3B_PepF and M3A) and M32_Taq peptidases. The M2 peptidase angiotensin converting enzyme (ACE, EC 3.4.15.1) catalyzes the conversion of decapeptide angiotensin I to the potent vasopressor octapeptide angiotensin II. ACE is a key component of the renin-angiotensin system that regulates blood pressure, thus ACE inhibitors are important for the treatment of hypertension. M3A includes thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (3.4.24.16), and the mitochondrial intermediate peptidase; and M3B includes oligopeptidase F. The M32 family includes eukaryotic enzymes from protozoa Trypanosoma cruzi, a causative agent of Chagas' disease, and from Leishmania major, a parasite that causes leishmaniasis, making these enzymes attractive targets for drug development. The M4 family includes secreted protease thermolysin (EC 3.4.24.27), pseudolysin, aureolysin, and neutral protease as well as bacillolysin (EC 3.4.24.28) that degrade extracellular proteins and peptides for bacterial nutrition, especially prior to sporulation. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing as well as in production of the artificial sweetener aspartame. The M13 family includes neprilysin (EC 3.4.24.11) and endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), which fulfill a broad range of physiological roles due to the greater variation in the S2' subsite allowing substrate specificity and are prime therapeutic targets for selective inhibition. The peptidase M36 fungalysin family includes endopeptidases from pathogenic fungi. Fungalysin hydrolyzes extracellular matrix proteins such as elastin and keratin. Aspergillus fumigatus causes the pulmonary disease aspergillosis by invading the lungs of immuno-compromised animals and secreting fungalysin that possibly breaks down proteinaceous structural barriers.


Pssm-ID: 341057 [Multi-domain]  Cd Length: 105  Bit Score: 46.32  E-value: 2.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86577810 344 ITGPIFSFLEDLFN-ISYRLP----KTDIVALPI---FASGAMENWGLLIFDESSLLLEpedeltekRAMILSIIAHEVG 415
Cdd:cd09594   3 YAHETYKYYEELLGrTSFRYPvspiYSLLVYPAYvevNAYNAMWIPSTNIFYGAGILDT--------LSGTIDVLAHELT 74

                        90       100
                ....*....|....*....|....*....
gi 86577810 416 HQWFGNLVT-MSWWNNIWLNEGFASYFEL 443
Cdd:cd09594  75 HAFTGQFSNlMYSWSSGWLNEGISDYFGG 103
M1_like_TAF2 cd09839
TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) ...
 382-440 7.60e-04

TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) associated factor 2 (TAF2, TBP-associated factor TAFII150, transcription initiation factor TFIID subunit 2, RNA polymerase II TBP-associated factor subunit B), and has homology to the M1 gluzincin family. TAF2 is part of the TFIID multidomain subunit complex essential for transcription of most protein-encoded genes by RNA polymerase II. TAF2 is known to interact with the initiator element (Inr) found at the transcription start site of many genes, thus possibly playing a key role in promoter binding as well as start-site selection. Image analysis has shown TAF2 to form a complex with TAF1 and TBP, inferring its role in promoter recognition. Peptidases in the M1 family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TAF2, however, lacks these active site residues.


Pssm-ID: 341074 [Multi-domain]  Cd Length: 531  Bit Score: 42.22  E-value: 7.60e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86577810 382 GLLIFDeSSLL-----LEPEDELTEKramilsiIAHEVGHQWFGNLVTMSWWNNIWLNEGFASY 440
Cdd:cd09839 353 SLSICS-SRLLyppdiIDQAYETRRK-------LAHALASQWFGINIIPKTWSDTWLVIGIAGY 408
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH