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Conserved domains on  [gi|309747091|ref|NP_001185470.1|]
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endoplasmic reticulum aminopeptidase 1 isoform b precursor

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List of domain hits

Name Accession Description Interval E-value
M1_APN_2 cd09601
Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic ...
61-531 0e+00

Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ); This M1 peptidase family includes eukaryotic and bacterial members: 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, consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189008 [Multi-domain]  Cd Length: 446  Bit Score: 669.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  61 VHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLl 140
Cdd:cd09601    1 VHYDLTLTPDLDNFTFSGSVTITLEVTEPTNEIVLHAKDLTITSATVTVGGGNVDILVTITYSEENEFLVITLDEPLTL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 141 VGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMP 220
Cdd:cd09601   80 AGGNYTLTIEFTGELNDDLRGFYRSSYTDNGGETRYLAATQFEPTDARRAFPCFDEPAFKATFTITITHPAGYTALSNMP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 221 LVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIP 300
Cdd:cd09601  160 VESEEVLGDGWKTTEFETTPPMSTYLVAFVVGDFDYVEGTTKNGVPVRVYARPGKIEQGDYALEVAPKILEFFEDYFGIP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 301 YPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAK 380
Cdd:cd09601  240 YPLPKLDLVAIPDFAAGAMENWGLITYRETALLYDPKTSSASNKQRVATVVAHELAHQWFGNLVTMKWWDDLWLNEGFAT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 381 FMEFVSVSVTHPELKVGDYFF-GKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKS 459
Cdd:cd09601  320 YMEYLGVDHLEPEWNMWDQFVlDDLQSALALDSLASSHPISVPVETPDEISEIFDAISYSKGASVLRMLEHFLGEEVFRK 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091 460 GIVQYLQKHSYKNTKNEDLWDSMASICPtdgvkgmdgfcsrsqhssssshwhqEGVDVKTMMNTWTLQKGFP 531
Cdd:cd09601  400 GLRNYLKKHAYGNATTDDLWEALSEASK-------------------------LGKDVKEIMDTWTLQPGYP 446
ERAP1_C pfam11838
ERAP1-like C-terminal domain; This large domain is composed of 16 alpha helices organized as 8 ...
597-916 4.60e-50

ERAP1-like C-terminal domain; This large domain is composed of 16 alpha helices organized as 8 HEAT-like repeats. This domain forms a concave face that faces towards the active site of the peptidase.


:

Pssm-ID: 256661  Cd Length: 323  Bit Score: 180.20  E-value: 4.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  597 WIKFNVGMNGYYIVHYEDDGWDSLTGLLKGThtAVSSNDRASLINNAFQLVSIGKLSIEKALDLSL-YLKHETEIMPVFQ 675
Cdd:pfam11838   1 LVLLNDDDLGYYRVRYDPESLATLGEALARL--KLDPLDRAGLWADAWALVRDGELPTRDFLDLVLaFLPNETDYVVWSE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  676 GLNELIPMYKLMEKRDmNEVETQFKAFLIRLLRDLIDKQTWTDEG--SVSERMLRSQLLLLACVHnyQPCVQRAEGYFRK 753
Cdd:pfam11838  79 ILAQLGTLKSALYFEP-EERKEALKKFVRKLAAPLLEKLGWEFGPgsDHQLQQLRALLASLAGGD--EEVVAAALERFRA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  754 WKESNGNL-SLPVDVTLAVFAVGAQ--STEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQ 830
Cdd:pfam11838 156 LLDGDKSLaAIDPDLRWSVFAALAAngGAKEYDQILAEYKNDPTADGKEAALRALAAVPDPELKAKALNFLLDDDSVSNQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  831 EFPQILT-LIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQL-RCV 908
Cdd:pfam11838 236 DIRAVMAgLRRSNQAGRELLWPWVERNFDALAKRWPRGSSALARVVGLYPSGFSSAELLDEVEAFLARKDKDTPGLrRSL 315

                  ....*...
gi 309747091  909 QQTIETIE 916
Cdd:pfam11838 316 AQALDSIR 323
Peptidase_M1 pfam01433
Peptidase family M1; Members of this family are aminopeptidases. The members differ widely in ...
53-441 2.18e-165

Peptidase family M1; 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: 250618 [Multi-domain]  Cd Length: 389  Bit Score: 491.82  E-value: 2.18e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091   53 RLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRkgaGERLSEEPLQV--LEHPRQEQ 130
Cdd:pfam01433   1 RLPTTVVPIHYDLTLTPDFTPPTFSGSVTITLQAKAATNEIVLHSKDLEITSVTIR---GEPVSVNNLISvfQLDDEDEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  131 IALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRRE 210
Cdd:pfam01433  78 LVINLAETLQAGQPYTLEIEYSGELNDDMRGFYRSTYLDTNGEKKYMATTQFEPTDARRAFPCFDEPAFKATFDITINHP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  211 PRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLL 290
Cdd:pfam01433 158 ADYTALSNMPEIESESLDDGRVITEFETTPKMSTYLLAFAVGDLDSLETKTKSGVPVRVYARPGAINAGQYALEVTQKLL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  291 EFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWN 370
Cdd:pfam01433 238 EFFEDYFGFPYPLPKLDQVALPDFSAGAMENWGLITYREAALLYDPGNSTSSDKQRVAEVIAHELAHQWFGNLVTMDWWD 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091  371 DLWLNEGFAKFMEFVSVSVTHPELKVGDYFF-GKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKG 441
Cdd:pfam01433 318 DLWLNEGFATYMEYLITDALEPEWRIEEQFVlREVQSALALDSLDSSHPITVNVNTPSEIDDIFDAISYEKG 389
 
Name Accession Description Interval E-value
M1_APN_2 cd09601
Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic ...
61-531 0e+00

Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ); This M1 peptidase family includes eukaryotic and bacterial members: 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, consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189008 [Multi-domain]  Cd Length: 446  Bit Score: 669.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  61 VHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLl 140
Cdd:cd09601    1 VHYDLTLTPDLDNFTFSGSVTITLEVTEPTNEIVLHAKDLTITSATVTVGGGNVDILVTITYSEENEFLVITLDEPLTL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 141 VGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMP 220
Cdd:cd09601   80 AGGNYTLTIEFTGELNDDLRGFYRSSYTDNGGETRYLAATQFEPTDARRAFPCFDEPAFKATFTITITHPAGYTALSNMP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 221 LVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIP 300
Cdd:cd09601  160 VESEEVLGDGWKTTEFETTPPMSTYLVAFVVGDFDYVEGTTKNGVPVRVYARPGKIEQGDYALEVAPKILEFFEDYFGIP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 301 YPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAK 380
Cdd:cd09601  240 YPLPKLDLVAIPDFAAGAMENWGLITYRETALLYDPKTSSASNKQRVATVVAHELAHQWFGNLVTMKWWDDLWLNEGFAT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 381 FMEFVSVSVTHPELKVGDYFF-GKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKS 459
Cdd:cd09601  320 YMEYLGVDHLEPEWNMWDQFVlDDLQSALALDSLASSHPISVPVETPDEISEIFDAISYSKGASVLRMLEHFLGEEVFRK 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091 460 GIVQYLQKHSYKNTKNEDLWDSMASICPtdgvkgmdgfcsrsqhssssshwhqEGVDVKTMMNTWTLQKGFP 531
Cdd:cd09601  400 GLRNYLKKHAYGNATTDDLWEALSEASK-------------------------LGKDVKEIMDTWTLQPGYP 446
ERAP1_C pfam11838
ERAP1-like C-terminal domain; This large domain is composed of 16 alpha helices organized as 8 ...
597-916 4.60e-50

ERAP1-like C-terminal domain; This large domain is composed of 16 alpha helices organized as 8 HEAT-like repeats. This domain forms a concave face that faces towards the active site of the peptidase.


Pssm-ID: 256661  Cd Length: 323  Bit Score: 180.20  E-value: 4.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  597 WIKFNVGMNGYYIVHYEDDGWDSLTGLLKGThtAVSSNDRASLINNAFQLVSIGKLSIEKALDLSL-YLKHETEIMPVFQ 675
Cdd:pfam11838   1 LVLLNDDDLGYYRVRYDPESLATLGEALARL--KLDPLDRAGLWADAWALVRDGELPTRDFLDLVLaFLPNETDYVVWSE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  676 GLNELIPMYKLMEKRDmNEVETQFKAFLIRLLRDLIDKQTWTDEG--SVSERMLRSQLLLLACVHnyQPCVQRAEGYFRK 753
Cdd:pfam11838  79 ILAQLGTLKSALYFEP-EERKEALKKFVRKLAAPLLEKLGWEFGPgsDHQLQQLRALLASLAGGD--EEVVAAALERFRA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  754 WKESNGNL-SLPVDVTLAVFAVGAQ--STEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQ 830
Cdd:pfam11838 156 LLDGDKSLaAIDPDLRWSVFAALAAngGAKEYDQILAEYKNDPTADGKEAALRALAAVPDPELKAKALNFLLDDDSVSNQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  831 EFPQILT-LIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQL-RCV 908
Cdd:pfam11838 236 DIRAVMAgLRRSNQAGRELLWPWVERNFDALAKRWPRGSSALARVVGLYPSGFSSAELLDEVEAFLARKDKDTPGLrRSL 315

                  ....*...
gi 309747091  909 QQTIETIE 916
Cdd:pfam11838 316 AQALDSIR 323
Peptidase_MA_2 pfam13485
Peptidase MA superfamily;
321-464 3.65e-13

Peptidase MA superfamily;


Pssm-ID: 257809  Cd Length: 128  Bit Score: 67.97  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  321 NWGLTTYRESALLFDAEKSSASSKLGitMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKvgdyf 400
Cdd:pfam13485   1 GVGGVYYPGSRLIVPPVASGDPDWLR--GVLAHELAHVVLGQLVGGNGNLPRWLTEGLAEYVAGRIDAERAEELR----- 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309747091  401 fgkcfDAMEVDALNSSHPVSTPVENpaqiREMFDDVSYDKGACILNMLREYLSADAFKSGIVQY 464
Cdd:pfam13485  74 -----DAVRSGRLPPLDELSADFSA----NSEDGSLAYAQGALFVRYLAERYGEEKLRALLRAL 128
Peptidase_M1 pfam01433
Peptidase family M1; Members of this family are aminopeptidases. The members differ widely in ...
53-441 2.18e-165

Peptidase family M1; 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: 250618 [Multi-domain]  Cd Length: 389  Bit Score: 491.82  E-value: 2.18e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091   53 RLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRkgaGERLSEEPLQV--LEHPRQEQ 130
Cdd:pfam01433   1 RLPTTVVPIHYDLTLTPDFTPPTFSGSVTITLQAKAATNEIVLHSKDLEITSVTIR---GEPVSVNNLISvfQLDDEDEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  131 IALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRRE 210
Cdd:pfam01433  78 LVINLAETLQAGQPYTLEIEYSGELNDDMRGFYRSTYLDTNGEKKYMATTQFEPTDARRAFPCFDEPAFKATFDITINHP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  211 PRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLL 290
Cdd:pfam01433 158 ADYTALSNMPEIESESLDDGRVITEFETTPKMSTYLLAFAVGDLDSLETKTKSGVPVRVYARPGAINAGQYALEVTQKLL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  291 EFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWN 370
Cdd:pfam01433 238 EFFEDYFGFPYPLPKLDQVALPDFSAGAMENWGLITYREAALLYDPGNSTSSDKQRVAEVIAHELAHQWFGNLVTMDWWD 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091  371 DLWLNEGFAKFMEFVSVSVTHPELKVGDYFF-GKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKG 441
Cdd:pfam01433 318 DLWLNEGFATYMEYLITDALEPEWRIEEQFVlREVQSALALDSLDSSHPITVNVNTPSEIDDIFDAISYEKG 389
PepN COG0308
Aminopeptidase N [Amino acid transport and metabolism];
51-928 5.87e-124

Aminopeptidase N [Amino acid transport and metabolism];


Pssm-ID: 223385 [Multi-domain]  Cd Length: 859  Bit Score: 399.16  E-value: 5.87e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  51 KIRLPEYVIP------VHYDLLIHANLTTLTfwGTTKVEITASQ--PTSTIILHSHHLQISRATLRKGAGERLSEeplqv 122
Cdd:COG0308   11 AALSLDYRPPeyaiydIDLDLDLDPEKTTFE--GSVTIRLDAGWrsGADPLVLDAVGLEIRSVKIDGKALTAWYR----- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 123 LEHPRQEqIALLAPEPLLVGLPYTVVIHYAGNLSET---FHGFYKSTYRTKEgelriLASTQFEPTAARMAFPCFDEPAF 199
Cdd:COG0308   84 LDGDALT-ITVAPPIPERSERPFTLAITYEFTGPVSndtLEGLYRSGYGGKP-----YLITQCEAEGARRIFPCIDEPDV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 200 KASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKS---GVKVSVYAVPDKI 276
Cdd:COG0308  158 KATFTLTIRADKGPKLISNGNLIDGGTLVDGRKIVKFEDTPPMPTYLFALVAGDLEVFRDKFDTrsrDVPLEIYVPPGVL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 277 NQADYALDAAVTLLEFYEDYFSIPYPLPKqDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELA 356
Cdd:COG0308  238 DRAKYALDETKRSIEFYEEYFGLPYALPI-DIVAVPDFSAGAMENWGLVTFREKYLLADPETATDSDYENVEEVIAHELA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 357 HQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHP-ELKV-GDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFD 434
Cdd:COG0308  317 HQWFGNLVTMKWWDDLWLNEGFATFREVLWSEDLGGrAWKRwEDFRTLRTSIALAEDSLPSSHPIRVDVYDPKEINDFFD 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 435 DVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMAsicptdgvkgmdgfcsrsqhssssshwHQEG 514
Cdd:COG0308  397 AIVYEKGASVLRMLETLLGEEAFRKGLSLYFKRHAGGNATTMDLWKALE---------------------------DASG 449
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 515 VDVKTMMNTWTLQKGFPLITITVRG-RNVHMKQEHYMKGSDgapDTGYLWHVPLTFITSKSDMVHRFLLK----TKTDVL 589
Cdd:COG0308  450 KDLSAFFESWLSQAGYPVLTVSVRYdDFFKLTQKQFTPPGQ---EEKRPWPIPLAIKLLDGGGVKVLLLTegeqTVTFEL 526
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 590 ILPEEVEWIKFNVGMNGYYIVHYEDdgwDSLTGLLK--GTHTAVssnDRASLINNAFQLVSIGKLSIEKALDLSLYLKHE 667
Cdd:COG0308  527 VGIPPFPSLKVNDSAPVFYRVDYSD---QSLSKLLQhdPRLEAA---QRLALVADRRALTAAGKGSAEDKLALVSRAFNA 600
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 668 teimPVFQGLNEliPMYK--LMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQ 745
Cdd:COG0308  601 ----ELLYVSLE--QAFKslLLALPSFADLEKFIDPDAIDQLRDALVRLGAEAVADDLLALYHIGALSQSLYEEDASLAA 674
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 746 RAEGYFRKWKesNGNLSLPVDVTLAV---FAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESF 822
Cdd:COG0308  675 LRALRNACLE--RLEKQEDPELRSLVvkaYAAAGNMTDALKALLEAYQSPTRAEALRDFADAFGRFPLVMDKWFALQAIS 752
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 823 KGDKIKTQ--EFPQILTLigRNPVGYPLAWQFLRKNWNKLVQK---FELGSSSIAHMVMgTTNQFSTRTRLEEVKGFFSS 897
Cdd:COG0308  753 PGDTVLEQdiGLMIHAAF--EAPNPNEARWLYGTFAFENPALLhalDGSGYRFLGVIVL-ELNIFNPQLALRKIEEFLEL 829
                        890       900       910
                 ....*....|....*....|....*....|.
gi 309747091 898 LKENGSQlRCVQQTIETIEENIGWMDKNFDK 928
Cdd:COG0308  830 KKLKALE-RLIREALETIAARERLSKDLAEK 859
pepN_strep_liv TIGR02412
aminopeptidase N, Streptomyces lividans type; This family is a subset of the members of the ...
180-489 1.69e-64

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: 232.76  E-value: 1.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  180 TQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNmPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSK 259
Cdd:TIGR02412 122 TQFEPADARRVFAVFDQPDLKANFKFSVKAPEDWTVISN-SRETDVTPEPADRRWEFPETPKLSTYLTAVAAGPYHSVQD 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  260 iTKSGVKVSVYAVPD--KINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESaLLFDAE 337
Cdd:TIGR02412 201 -ESRSYPLGIYARRSlaQYLDADAIFTITRQGLAFFHRKFGYPYPFKKYDQIFVPEFNAGAMENAGCVTFAEN-FLHRAE 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  338 kSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFME-FVSVSVT-HPELKVGDYFFGKCFdAMEVDALNS 415
Cdd:TIGR02412 279 -ATRAEKENRAGVILHEMAHMWFGDLVTMRWWNDLWLNESFAEYMGtLASAEATeYTDAWTTFAAQGKQW-AYEADQLPT 356
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309747091  416 SHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTD 489
Cdd:TIGR02412 357 THPIVADVADLADALSNFDGITYAKGASVLKQLVAWVGEEAFFAGVNAYFKRHAFGNATLDDLIDSLAKASGRD 430
pepN PRK14015
aminopeptidase N; Provisional
245-468 2.29e-09

aminopeptidase N; Provisional


Pssm-ID: 237585 [Multi-domain]  Cd Length: 875  Bit Score: 59.76  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 245 YLVAFIISDFESVSK--ITKSG--VKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYplpkqDL-----AAIPDFQ 315
Cdd:PRK14015 190 YLFALVAGDLDVLEDtfTTRSGreVALEIYVEPGNLDKCDHAMDSLKKSMKWDEERFGLEY-----DLdifmiVAVDDFN 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 316 SGAMENWGLTTYRESALLFDAEksSASSK--LGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKF--MEF------- 384
Cdd:PRK14015 265 MGAMENKGLNIFNSKYVLADPE--TATDAdyERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGLTVFrdQEFsadlgsr 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 385 -------VSVSVTH--PElkvgdyffgkcfDA--MevdalnsSHPVstpveNPAQIREM--FDDVS-YDKGACILNMLRE 450
Cdd:PRK14015 343 avkriedVRVLRAAqfAE------------DAgpM-------AHPV-----RPDSYIEInnFYTATvYEKGAEVIRMLHT 398
                        250
                 ....*....|....*...
gi 309747091 451 YLSADAFKSGIVQYLQKH 468
Cdd:PRK14015 399 LLGEEGFRKGMDLYFERH 416
 
Name Accession Description Interval E-value
M1_APN_2 cd09601
Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic ...
61-531 0e+00

Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ); This M1 peptidase family includes eukaryotic and bacterial members: 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, consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189008 [Multi-domain]  Cd Length: 446  Bit Score: 669.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  61 VHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLl 140
Cdd:cd09601    1 VHYDLTLTPDLDNFTFSGSVTITLEVTEPTNEIVLHAKDLTITSATVTVGGGNVDILVTITYSEENEFLVITLDEPLTL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 141 VGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMP 220
Cdd:cd09601   80 AGGNYTLTIEFTGELNDDLRGFYRSSYTDNGGETRYLAATQFEPTDARRAFPCFDEPAFKATFTITITHPAGYTALSNMP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 221 LVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIP 300
Cdd:cd09601  160 VESEEVLGDGWKTTEFETTPPMSTYLVAFVVGDFDYVEGTTKNGVPVRVYARPGKIEQGDYALEVAPKILEFFEDYFGIP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 301 YPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAK 380
Cdd:cd09601  240 YPLPKLDLVAIPDFAAGAMENWGLITYRETALLYDPKTSSASNKQRVATVVAHELAHQWFGNLVTMKWWDDLWLNEGFAT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 381 FMEFVSVSVTHPELKVGDYFF-GKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKS 459
Cdd:cd09601  320 YMEYLGVDHLEPEWNMWDQFVlDDLQSALALDSLASSHPISVPVETPDEISEIFDAISYSKGASVLRMLEHFLGEEVFRK 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091 460 GIVQYLQKHSYKNTKNEDLWDSMASICPtdgvkgmdgfcsrsqhssssshwhqEGVDVKTMMNTWTLQKGFP 531
Cdd:cd09601  400 GLRNYLKKHAYGNATTDDLWEALSEASK-------------------------LGKDVKEIMDTWTLQPGYP 446
M1_APN_3 cd09602
Peptidase M1 family containing Aminopeptidase N; This family contains bacterial and eukaryotic ...
61-483 1.67e-86

Peptidase M1 family containing Aminopeptidase N; This family contains 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 consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189009 [Multi-domain]  Cd Length: 438  Bit Score: 286.05  E-value: 1.67e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  61 VHYDllIHANLTTL--TFWGTTKVEITASQPTSTIILHSHHLQISRATLRkgaGERLSEEPLqvlehpRQEQIALlaPEP 138
Cdd:cd09602    8 VSYE--LDLDLTKGkeTFRGTTTITFDLRKNGGDLFIDFKGGQVLSVSLN---GNPVDPDTF------EDGRIPL--PGL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 139 LLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRIlasTQFEPTAARMAFPCFDEPAFKASFSIKIRrEPRH-LAIS 217
Cdd:cd09602   75 ELKNGRNEVVIDFTNPYSNDGEGLHRFVDPADGKTYLY---TQFEPDDARRVFPCFDQPDLKAPFTLTVT-APKDwTVIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 218 NMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYA----VPDKINQADYALDAAVTLLEFY 293
Cdd:cd09602  151 NTAATEQSTIRNGYVRWEFPETPPLSTYLFAFVAGPYHVISDKEHDGIPLGLYCreslAQALDRDADEIFEITKQGLDFF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 294 EDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEksSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLW 373
Cdd:cd09602  231 EEYFGIPYPFGKYDQVFVPEFNFGAMENPGCVTFRENYVFREEV--TTAQRLRRANTIAHEMAHMWFGDLVTMKWWNDLW 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 374 LNEGFAKFME-FVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYL 452
Cdd:cd09602  309 LNESFAEYMAyKALSEATPFTDAWLTFFLDRKQWAYRADQTPTTHPIAGDVENTEDALNNFDGITYAKGASVLKQLVALL 388
                        410       420       430
                 ....*....|....*....|....*....|.
gi 309747091 453 SADAFKSGIVQYLQKHSYKNTKNEDLWDSMA 483
Cdd:cd09602  389 GEEKFREGLREYFKKHAFGNATLADFLGALD 419
M1_APN_4 cd09603
Peptidase M1 family Aminopeptidase N; This family contains mostly bacterial and some archaeal ...
62-478 4.19e-74

Peptidase M1 family Aminopeptidase N; This family contains mostly bacterial and some archaeal aminopeptidase N (APN; CD13; Alanyl aminopeptidase; EC 3.4.11.2), a Type II integral membrane protease belonging to the M1 gluzincin family. APN consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189010 [Multi-domain]  Cd Length: 415  Bit Score: 250.99  E-value: 4.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  62 HYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATL--RKGAGERlseeplqvlehpRQEQIALLAPEPL 139
Cdd:cd09603    4 HYDLDLDYDPATNRLSGTATITARATQDLSSLNLDLAGLTVSSVTVdgRPAAFRH------------DGDELTITPPRPL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 140 LVGLPYTVVIHYAGNLSET--FHGFYKSTYRTKEGelrilASTQFEPTAARMAFPCFDEPAFKASFSIKIRrEPRHL-AI 216
Cdd:cd09603   72 PKGQTFTVTVRYSGVPRPGlyPWGGDGGWEEGPDG-----VWTAGQPEGASTWFPCNDHPSDKATFDISVT-VPAGYtVV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 217 SNMPLVkSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDY 296
Cdd:cd09603  146 SNGRLV-SRTDLGGRTTWHWRMDEPMATYLVTLAVGRYEVLEDTTAGGVPVVYYVPPGLAADARRAFARTPEMLDFFEEL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 297 FsIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSassklgitmTVAHELAHQWFGNLVTMEWWNDLWLNE 376
Cdd:cd09603  225 F-GPYPFEKYGQVVVDDFLGGGMENQTRTVYGAGFLDGDRSSER---------LIAHELAHQWFGDSVTCADWSDIWLNE 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 377 GFAKFMEFVsvsvthpelkVGDYFFGKCFDAMEV------DALNSSHPVSTPVENPAqirEMFDDVSYDKGACILNMLRE 450
Cdd:cd09603  295 GFATYAEWL----------WSEHSGGRDAAQYALyayarlYANEADLGPRPPVPGPA---ELFDDHVYEKGALVLHALRR 361
                        410       420
                 ....*....|....*....|....*...
gi 309747091 451 YLSADAFKSGIVQYLQKHSYKNTKNEDL 478
Cdd:cd09603  362 LLGDEAFFRLLRTYLAEHRGGNVTTEDF 389
M1 cd09595
Peptidase M1 family contains aminopeptidase N and leukotriene A4 hydrolase; M1 Peptidase ...
63-484 2.95e-62

Peptidase M1 family contains aminopeptidase N and leukotriene A4 hydrolase; M1 Peptidase family includes 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 on activation during catalysis. APN consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189002 [Multi-domain]  Cd Length: 407  Bit Score: 216.91  E-value: 2.95e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  63 YDLLIHANLTTLTFWGTTKVEITASQPT-STIILHSHHLQISRATLRKGAGERLSEEPLQVlehpRQEQIALLAPEPLLV 141
Cdd:cd09595    1 YKVELDLDVDTKTLVGTATLTVDPTEPNlGELVLDLKALAISSVDVNGAAAAFAKNERPVV----EGSRLTIPGPIALDK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 142 GLPYTVVIHYAGNLSETFHGFYkstyrTKEGELRILAStQFEPTAARMAFPCFDEPAFKAS-FSIKIRREPRHLAISNMP 220
Cdd:cd09595   77 GQSLKVEVEFSGKPPPMGLGWQ-----TAGAEGAFLFS-QGEAIGARSWFPCQDRPDSVATyYTTVTVPDKTLVAASNGN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 221 LVKSVTVAEgliEDHFDVTVKMSTYLVAFIISDFES-VSKITKSGVKVSVYAVPDKinqADYALDAAVTLLEFYEDYFSI 299
Cdd:cd09595  151 KDDGEVRRK---WVEFSPPIPIAPYLIALVVGDLEYpVREQTVQGIPLHLYFLTPL---AVDTVLRLQSAFLFYETDLGG 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 300 PYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLfdaeKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFA 379
Cdd:cd09595  225 PYPYSEYDVVEVPEFPSGAMENPGLIFFSQSLLL----AMIDAGDELLENVIAHELAHQWFGNLVTGARWNDLWLNEGFA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 380 KFMEFVSVSVTHPELKVGDYFFGKCFD----AMEVDALNSSHPVStpVENPAQIREMFDDVSYDKGACILNMLREYLSAD 455
Cdd:cd09595  301 TYLEGLWMEATFGTSAREAYRLEGTRGlrrwRKLQDELPPAPPVM--GKHPDDPSVEFDGVFYEKGALVLRYLEKRLGDE 378
                        410       420
                 ....*....|....*....|....*....
gi 309747091 456 AFKSGIVQYLQKHSYKNTKNEDLWDSMAS 484
Cdd:cd09595  379 AFFKGLRKYVEKHAGQSATTDDLLQALES 407
ERAP1_C pfam11838
ERAP1-like C-terminal domain; This large domain is composed of 16 alpha helices organized as 8 ...
597-916 4.60e-50

ERAP1-like C-terminal domain; This large domain is composed of 16 alpha helices organized as 8 HEAT-like repeats. This domain forms a concave face that faces towards the active site of the peptidase.


Pssm-ID: 256661  Cd Length: 323  Bit Score: 180.20  E-value: 4.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  597 WIKFNVGMNGYYIVHYEDDGWDSLTGLLKGThtAVSSNDRASLINNAFQLVSIGKLSIEKALDLSL-YLKHETEIMPVFQ 675
Cdd:pfam11838   1 LVLLNDDDLGYYRVRYDPESLATLGEALARL--KLDPLDRAGLWADAWALVRDGELPTRDFLDLVLaFLPNETDYVVWSE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  676 GLNELIPMYKLMEKRDmNEVETQFKAFLIRLLRDLIDKQTWTDEG--SVSERMLRSQLLLLACVHnyQPCVQRAEGYFRK 753
Cdd:pfam11838  79 ILAQLGTLKSALYFEP-EERKEALKKFVRKLAAPLLEKLGWEFGPgsDHQLQQLRALLASLAGGD--EEVVAAALERFRA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  754 WKESNGNL-SLPVDVTLAVFAVGAQ--STEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQ 830
Cdd:pfam11838 156 LLDGDKSLaAIDPDLRWSVFAALAAngGAKEYDQILAEYKNDPTADGKEAALRALAAVPDPELKAKALNFLLDDDSVSNQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  831 EFPQILT-LIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQL-RCV 908
Cdd:pfam11838 236 DIRAVMAgLRRSNQAGRELLWPWVERNFDALAKRWPRGSSALARVVGLYPSGFSSAELLDEVEAFLARKDKDTPGLrRSL 315

                  ....*...
gi 309747091  909 QQTIETIE 916
Cdd:pfam11838 316 AQALDSIR 323
M1_LTA4H cd09599
Peptidase M1 family contains leukotriene A4 hydrolase; This family includes leukotriene A4 ...
55-471 4.09e-30

Peptidase M1 family contains leukotriene A4 hydrolase; This family includes 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 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. 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. LTA4H is 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: 189006 [Multi-domain]  Cd Length: 442  Bit Score: 123.79  E-value: 4.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  55 PEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQP-TSTIILHSHHLQISRATLRkgagerlSEEPLQVLEHPRQE---- 129
Cdd:cd09599    8 YDEVRVTHLHLDLTVDFEKKILSGSATLTLEVLKDgASELVLDTRDLDIHSVYVD-------GGKELPFELGPRDEvlgs 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 130 --QIALlaPEPLLVGLPYTVVIHYagnlsetfhgfyKSTYR-------TKE---GELRILASTQFEPTAARMAFPCFDEP 197
Cdd:cd09599   81 plTISL--PPEYAKGDTFQVTIKY------------ETTPKasalqwlTPEqtaGKKHPYLFSQCQAIHARSLFPCQDTP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 198 AFKASFSIKIRreprhlAISNMPLVKSvtvAEGLIED--------HFDVTVKMSTYLVAFIISDFESVsKItksGVKVSV 269
Cdd:cd09599  147 SVKSTYSATVT------VPKELTALMS---AIPPVEDgeeprktyHFEQPVPIPSYLIAIAVGDLESR-PI---GPRSRV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 270 YAVPDKINQADYALDAAVTLLEFYEDYFsIPYPLPKQDLAAIPD-FQSGAMENWGLTTYRESALLFDaeKSSASsklgit 348
Cdd:cd09599  214 WAEPSLLDAAAEEFADTEKFLKAAEDLI-GPYVWGRYDLLVLPPsFPYGGMENPCLTFATPTLIAGD--RSLVD------ 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 349 mTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPElkvgDYFfgkCFDAM--------EVDALNSSHPVS 420
Cdd:cd09599  285 -VVAHEIAHSWSGNLVTNATWEHFWLNEGFTVYLERRILERLYGE----DYR---QFEAIigwkelqeSIKTFGEDPEYT 356
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 309747091 421 TPVENPAQIR--EMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYK 471
Cdd:cd09599  357 KLVPDLKGVDpdDAFSSVPYEKGFQFLYYLEQLGGREVFDPFLRSYFDKFKFK 409
M1_APN_1 cd09600
Peptidase M1 family containing Aminopeptidase N; This family contains aminopeptidase N (APN; ...
55-483 2.57e-27

Peptidase M1 family containing Aminopeptidase N; This family contains 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 consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189007 [Multi-domain]  Cd Length: 861  Bit Score: 118.13  E-value: 2.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  55 PEYVIP-VHYDLLIHANLTTLTfwGTTKVEITASQPTStIILHSHHLQISRATLrkgAGERLSEEPLQvlehPRQEQIAL 133
Cdd:cd09600    5 PDYLIPkVDLDFDLDEEKTIVT--STLQVVRNGGSGAP-LVLDGEDLKLVSIKI---NGEPLEEGEYQ----LDSESLTI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 134 LAPEPLLVGLPYTVVIHYAGNLSETfhGFYKStyrtkEGELrilaSTQFEPTAARMAFPCFDEPAFKASFSIKIR----R 209
Cdd:cd09600   75 SSLPPDKFTLEIETEIDPAENTALE--GLYKS-----GGIF----CTQCEAEGFRRITYYLDRPDVMSKFTVRIEadktK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 210 EPRHLAISNMplvksvtVAEGLIED--HF----DVTVKMStYLVAFIISDFESVSK--ITKSG--VKVSVYAVPDKINQA 279
Cdd:cd09600  144 YPVLLSNGNL-------VEEGELEDgrHFavweDPFPKPC-YLFALVAGDLGVLEDkfTTKSGrkVALEIYVEPGDESKC 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 280 DYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQW 359
Cdd:cd09600  216 AHAMESLKKSMKWDEDRFGLEYDLDLFNIVAVDDFNMGAMENKGLNIFNSKLVLADPETATDADYERIESVIGHEYFHNW 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 360 FGNLVTMEWWNDLWLNEGFAKF--MEFvSVSVTHPELK-VGDyffgkcfdameVDALNSSH------PVSTPVEnPAQIR 430
Cdd:cd09600  296 TGNRVTCRDWFQLSLKEGLTVFrdQEF-SADMGSRAVKrIED-----------VRFLRAHQfpedagPMAHPIR-PDSYI 362
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 309747091 431 EM--FDDVS-YDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMA 483
Cdd:cd09600  363 EMnnFYTATvYEKGAEVIRMYHTLLGEEGFRKGMDLYFQRHDGQAVTCEDFVAAME 418
M1_APN_5 cd09604
Peptidase M1 family containing bacterial Aminopeptidase N; This family contains bacterial ...
136-478 4.46e-27

Peptidase M1 family containing bacterial Aminopeptidase N; This family contains bacterial aminopeptidase N (APN; CD13; Alanyl aminopeptidase; EC 3.4.11.2), a Type II integral membrane protease belonging to the M1 gluzincin family. APN consists of a small N-terminal cytoplasmic domain, a single transmembrane domain and a large extracellular ectodomain that contains the active site. It 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: 189011 [Multi-domain]  Cd Length: 435  Bit Score: 114.38  E-value: 4.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 136 PEPLLVGLPYTVVIHYAGNLSEtfhgfykSTYRTKEGE-LRILAstQFEPTAARmafpcFDEPAFKASFSiKIRREPRHL 214
Cdd:cd09604   90 PEPLKPGESITVTIDFEGKLPE-------RGLRFGYGNnLYSLA--QWYPRLAV-----YDDRGWWLDPY-YLGGDEFYS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 215 AISN----MPLVKS-VTVAEGLIEDHFDVTVKMSTYLV--------AFIISDFESVSKITKSGVKVSVYAVPDKINQADY 281
Cdd:cd09604  155 DFADydvtLTVPAGyIVVATGRLQEETTEDGGTKTWEFeaenvrdfALAASPKFIVDEATVDGIKVRAYYFPEDAELAKR 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 282 ALDAAVTLLEFYEDYFsIPYPLPKQDLAAIPDFqsGAMENWGLTTyresallfdAEKSSASSKLGITMTVAHELAHQWFG 361
Cdd:cd09604  235 YLDAAKKALEFYSELF-GPYPYKEFSVVENPFP--GGMEYPGLTL---------IGGRVLRLPFILETVLAHEIAHQWWY 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 362 NLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFddvsYDKG 441
Cdd:cd09604  303 GIVGNDERNEPWLDEGLTTYLTDYYLEERYGKEAARLYRLRRLTDYAALVNSRNDPPLAFFFRNNGAYSAIA----YGKG 378
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 309747091 442 ACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDL 478
Cdd:cd09604  379 AMVLHMLRKEIGDEAFDKALRTYYREYAFKHATPEDF 415
M1_TAF2 cd09839
TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) ...
96-382 1.52e-14

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 aminopeptidase N (APN) subfamily, belonging 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, does not seem to contain any of the active site residues.


Pssm-ID: 189018 [Multi-domain]  Cd Length: 507  Bit Score: 75.86  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  96 HSHHLQISRATLRKGAGERLseepLQVlehPRQEQIALLAPEPLLVGLPYTVV-----IHYAGNLSETFHGFYKSTYRTK 170
Cdd:cd09839   81 DASLSAVSYVDLDANNGELL----ISV---PKEVRKLVDEQKVLRVRIDFSVEqpkggLHFVGPDPEAERYPHVFTYNSI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 171 EGelrilastqfeptAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIED--HFDVTVKMSTYLVA 248
Cdd:cd09839  154 HG-------------SARCWFPCVDDPSQLCTWELEFTVPANMVAVSSGDLLEQVYDTEDMRKKtyHYALTVPTAAQNIG 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 249 FIISDFESVskITKSGVKVSVYAVP---DKINQADYALDAAVtllEFYEDYFSIPYPLP--KQ---DLAAIpDFQSGAme 320
Cdd:cd09839  221 LAVGPFEIL--VDPHAHEITHFCLPgllPELKNTTSYLHEAF---EFFEEYLSCRFPFSsyKQvfvDEAAE-DVTSYA-- 292
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091 321 nwGLTTYrESALLFDaeKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFM 382
Cdd:cd09839  293 --SLSIF-SSNLLYP--EDIIDQTYDTRRKLAYALASQWFGCFISPEAWSDEWLLKGIAGYI 349
Peptidase_MA_2 pfam13485
Peptidase MA superfamily;
321-464 3.65e-13

Peptidase MA superfamily;


Pssm-ID: 257809  Cd Length: 128  Bit Score: 67.97  E-value: 3.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  321 NWGLTTYRESALLFDAEKSSASSKLGitMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKvgdyf 400
Cdd:pfam13485   1 GVGGVYYPGSRLIVPPVASGDPDWLR--GVLAHELAHVVLGQLVGGNGNLPRWLTEGLAEYVAGRIDAERAEELR----- 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309747091  401 fgkcfDAMEVDALNSSHPVSTPVENpaqiREMFDDVSYDKGACILNMLREYLSADAFKSGIVQY 464
Cdd:pfam13485  74 -----DAVRSGRLPPLDELSADFSA----NSEDGSLAYAQGALFVRYLAERYGEEKLRALLRAL 128
GluZincin cd09594
Peptidase Gluzincin family (thermolysin-like proteinases, TLPs) includes peptidases M1, M2, M3, ...
290-388 4.36e-05

Peptidase Gluzincin family (thermolysin-like proteinases, TLPs) includes peptidases M1, M2, M3, M4, M13, M32 and M36 (fungalysins); Gluzincin family (thermolysin-like peptidases or TLPs) includes several zinc-dependent metallopeptidases such as the M1, M2, M3, M4, M13, M32, M36 peptidases (MEROPS classification), and contain HEXXH and EXXXD motifs as part of their active site. 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 on activation during catalysis. 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 peptidase M3 or neurolysin-like family, includes M3, M2 and M32 metallopeptidases. The M3 peptidases have two subfamilies: M3A, includes thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (3.4.24.16), and the mitochondrial intermediate peptidase; M3B contains oligopeptidase F. 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 part of the renin-angiotensin system that regulates blood pressure, thus ACE inhibitors are important for the treatment of hypertension. M32 family includes two eukaryotic enzymes from protozoa Trypanosoma cruzi, a causative agent of Chagas' disease, and Leishmania major, a parasite that causes leishmaniasis, making them attractive targets for drug development. The M4 family includes secreted protease thermolysin (EC 3.4.24.27), pseudolysin, aureolysin, neutral protease as well as fungalysin and 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. 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. Peptidase M36 (fungamysin) 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: 189001  Cd Length: 125  Bit Score: 42.83  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 290 LEFYEDYFSIPYPLPKQDlaaipdFQSGAMENwgltTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEW- 368
Cdd:cd09594   22 DEVGGGYYSMVYPPSNQG------KVNNAMCN----GLDARIVMNDGILVAFLLDSDDFGVVGHELTHGVTDQLVGNDPd 91
                         90       100
                 ....*....|....*....|....
gi 309747091 369 ----WNDLWLNEGFAKFMEFVSVS 388
Cdd:cd09594   92 llytNGSGGLNEGPSDFFELLVAY 115
Peptidase_M1 pfam01433
Peptidase family M1; Members of this family are aminopeptidases. The members differ widely in ...
53-441 2.18e-165

Peptidase family M1; 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: 250618 [Multi-domain]  Cd Length: 389  Bit Score: 491.82  E-value: 2.18e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091   53 RLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRkgaGERLSEEPLQV--LEHPRQEQ 130
Cdd:pfam01433   1 RLPTTVVPIHYDLTLTPDFTPPTFSGSVTITLQAKAATNEIVLHSKDLEITSVTIR---GEPVSVNNLISvfQLDDEDEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  131 IALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRRE 210
Cdd:pfam01433  78 LVINLAETLQAGQPYTLEIEYSGELNDDMRGFYRSTYLDTNGEKKYMATTQFEPTDARRAFPCFDEPAFKATFDITINHP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  211 PRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLL 290
Cdd:pfam01433 158 ADYTALSNMPEIESESLDDGRVITEFETTPKMSTYLLAFAVGDLDSLETKTKSGVPVRVYARPGAINAGQYALEVTQKLL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  291 EFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWN 370
Cdd:pfam01433 238 EFFEDYFGFPYPLPKLDQVALPDFSAGAMENWGLITYREAALLYDPGNSTSSDKQRVAEVIAHELAHQWFGNLVTMDWWD 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091  371 DLWLNEGFAKFMEFVSVSVTHPELKVGDYFF-GKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKG 441
Cdd:pfam01433 318 DLWLNEGFATYMEYLITDALEPEWRIEEQFVlREVQSALALDSLDSSHPITVNVNTPSEIDDIFDAISYEKG 389
PepN COG0308
Aminopeptidase N [Amino acid transport and metabolism];
51-928 5.87e-124

Aminopeptidase N [Amino acid transport and metabolism];


Pssm-ID: 223385 [Multi-domain]  Cd Length: 859  Bit Score: 399.16  E-value: 5.87e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  51 KIRLPEYVIP------VHYDLLIHANLTTLTfwGTTKVEITASQ--PTSTIILHSHHLQISRATLRKGAGERLSEeplqv 122
Cdd:COG0308   11 AALSLDYRPPeyaiydIDLDLDLDPEKTTFE--GSVTIRLDAGWrsGADPLVLDAVGLEIRSVKIDGKALTAWYR----- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 123 LEHPRQEqIALLAPEPLLVGLPYTVVIHYAGNLSET---FHGFYKSTYRTKEgelriLASTQFEPTAARMAFPCFDEPAF 199
Cdd:COG0308   84 LDGDALT-ITVAPPIPERSERPFTLAITYEFTGPVSndtLEGLYRSGYGGKP-----YLITQCEAEGARRIFPCIDEPDV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 200 KASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKS---GVKVSVYAVPDKI 276
Cdd:COG0308  158 KATFTLTIRADKGPKLISNGNLIDGGTLVDGRKIVKFEDTPPMPTYLFALVAGDLEVFRDKFDTrsrDVPLEIYVPPGVL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 277 NQADYALDAAVTLLEFYEDYFSIPYPLPKqDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELA 356
Cdd:COG0308  238 DRAKYALDETKRSIEFYEEYFGLPYALPI-DIVAVPDFSAGAMENWGLVTFREKYLLADPETATDSDYENVEEVIAHELA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 357 HQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHP-ELKV-GDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFD 434
Cdd:COG0308  317 HQWFGNLVTMKWWDDLWLNEGFATFREVLWSEDLGGrAWKRwEDFRTLRTSIALAEDSLPSSHPIRVDVYDPKEINDFFD 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 435 DVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMAsicptdgvkgmdgfcsrsqhssssshwHQEG 514
Cdd:COG0308  397 AIVYEKGASVLRMLETLLGEEAFRKGLSLYFKRHAGGNATTMDLWKALE---------------------------DASG 449
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 515 VDVKTMMNTWTLQKGFPLITITVRG-RNVHMKQEHYMKGSDgapDTGYLWHVPLTFITSKSDMVHRFLLK----TKTDVL 589
Cdd:COG0308  450 KDLSAFFESWLSQAGYPVLTVSVRYdDFFKLTQKQFTPPGQ---EEKRPWPIPLAIKLLDGGGVKVLLLTegeqTVTFEL 526
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 590 ILPEEVEWIKFNVGMNGYYIVHYEDdgwDSLTGLLK--GTHTAVssnDRASLINNAFQLVSIGKLSIEKALDLSLYLKHE 667
Cdd:COG0308  527 VGIPPFPSLKVNDSAPVFYRVDYSD---QSLSKLLQhdPRLEAA---QRLALVADRRALTAAGKGSAEDKLALVSRAFNA 600
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 668 teimPVFQGLNEliPMYK--LMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQ 745
Cdd:COG0308  601 ----ELLYVSLE--QAFKslLLALPSFADLEKFIDPDAIDQLRDALVRLGAEAVADDLLALYHIGALSQSLYEEDASLAA 674
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 746 RAEGYFRKWKesNGNLSLPVDVTLAV---FAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESF 822
Cdd:COG0308  675 LRALRNACLE--RLEKQEDPELRSLVvkaYAAAGNMTDALKALLEAYQSPTRAEALRDFADAFGRFPLVMDKWFALQAIS 752
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 823 KGDKIKTQ--EFPQILTLigRNPVGYPLAWQFLRKNWNKLVQK---FELGSSSIAHMVMgTTNQFSTRTRLEEVKGFFSS 897
Cdd:COG0308  753 PGDTVLEQdiGLMIHAAF--EAPNPNEARWLYGTFAFENPALLhalDGSGYRFLGVIVL-ELNIFNPQLALRKIEEFLEL 829
                        890       900       910
                 ....*....|....*....|....*....|.
gi 309747091 898 LKENGSQlRCVQQTIETIEENIGWMDKNFDK 928
Cdd:COG0308  830 KKLKALE-RLIREALETIAARERLSKDLAEK 859
pepN_strep_liv TIGR02412
aminopeptidase N, Streptomyces lividans type; This family is a subset of the members of the ...
180-489 1.69e-64

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: 232.76  E-value: 1.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  180 TQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNmPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSK 259
Cdd:TIGR02412 122 TQFEPADARRVFAVFDQPDLKANFKFSVKAPEDWTVISN-SRETDVTPEPADRRWEFPETPKLSTYLTAVAAGPYHSVQD 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  260 iTKSGVKVSVYAVPD--KINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESaLLFDAE 337
Cdd:TIGR02412 201 -ESRSYPLGIYARRSlaQYLDADAIFTITRQGLAFFHRKFGYPYPFKKYDQIFVPEFNAGAMENAGCVTFAEN-FLHRAE 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  338 kSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFME-FVSVSVT-HPELKVGDYFFGKCFdAMEVDALNS 415
Cdd:TIGR02412 279 -ATRAEKENRAGVILHEMAHMWFGDLVTMRWWNDLWLNESFAEYMGtLASAEATeYTDAWTTFAAQGKQW-AYEADQLPT 356
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309747091  416 SHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTD 489
Cdd:TIGR02412 357 THPIVADVADLADALSNFDGITYAKGASVLKQLVAWVGEEAFFAGVNAYFKRHAFGNATLDDLIDSLAKASGRD 430
pepN_proteo TIGR02414
aminopeptidase N, Escherichia coli type; The M1 family of zinc metallopeptidases contains a ...
53-484 3.17e-27

aminopeptidase N, Escherichia coli type; The M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N, EC 3.4.11.2, after the Escherichia coli enzyme, suggesting a similar activity profile (see SP|P04825 for a description of catalytic activity). This family consists of all aminopeptidases closely related to E. coli PepN and presumed to have similar (not identical) function. Nearly all are found in Proteobacteria, but members are found also in Cyanobacteria, plants, and apicomplexan parasites. This family differs greatly in sequence from the family of aminopeptidases typified by Streptomyces lividans PepN (TIGR02412), from the membrane bound aminopeptidase N family in animals, etc. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274122 [Multi-domain]  Cd Length: 863  Bit Score: 117.81  E-value: 3.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091   53 RLPEYVIP-VHYDLLIHANLTTLTfwGTTKVEITASQPTSTIILHSHHLQISRAtlrkgageRLSEEPLQVLEHPRQEQI 131
Cdd:TIGR02414   3 KPPPFLIEkTHLDFDLHEEETVVR--ARLTVRRNPDGNGAPLVLDGEELKLLSI--------AIDGKPLAAGDYQLDDET 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  132 ALLAPEPLLVGLPYTVVIHYAGNLSETfhGFYKStyrtkegelRILASTQFEPTAARMAFPCFDEPAFKASFSIKIR--- 208
Cdd:TIGR02414  73 LTIASVPESFTLEIETEIHPEENTSLE--GLYKS---------GGNFCTQCEAEGFRRITYFPDRPDVMSRYTVTITadk 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  209 -REPRHLAISNMplvksvtVAEGLIED--HF----DVTVKMStYLVAFIISDFESVSK--ITKSG--VKVSVYAVPDKIN 277
Cdd:TIGR02414 142 kKYPVLLSNGNK-------IASGELPDgrHWaeweDPFPKPS-YLFALVAGDLDVLEDtfTTKSGreVALRVYVEEGNKD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  278 QADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAH 357
Cdd:TIGR02414 214 KCDHAMESLKKAMKWDEEVFGLEYDLDIFMIVAVDDFNMGAMENKGLNIFNSKYVLADPETATDADYERIESVIAHEYFH 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  358 QWFGNLVTMEWWNDLWLNEGFAKF--MEFVSVSVTHPELKVGDyffgkcfdameVDALNSSH------PVSTPVEnPAQI 429
Cdd:TIGR02414 294 NWTGNRVTCRDWFQLSLKEGLTVFrdQEFSADMTSRAVKRIED-----------VRLLRAHQfpedagPMAHPVR-PESY 361
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 309747091  430 REM--FDDVS-YDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMAS 484
Cdd:TIGR02414 362 VEInnFYTATvYEKGAEVIRMLHTLLGEEGFRKGMDLYFSRHDGQAVTCEDFVAAMED 419
leuko_A4_hydro TIGR02411
leukotriene A-4 hydrolase/aminopeptidase; Members of this family represent a distinctive ...
55-490 8.62e-23

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: 102.55  E-value: 8.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091   55 PEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQP-TSTIILHSHHLQISRATLRKgagerlSEEPLQVLEhpRQEQIAl 133
Cdd:TIGR02411   8 YKDFRTSHTDLNLSVDFTKRKLSGSVTFTLKSLTDnLNKLVLDTSYLDIQKVTING------LPADFAIGE--RKEPLG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  134 lapEPLLVGLP--------YTVVIHYAGNLSETFHGFYKSTyRTKEGELRILAStQFEPTAARMAFPCFDEPAFKASFSI 205
Cdd:TIGR02411  79 ---SPLTISLPiatskndeFVLNISFSTTPKCTALQWLNPE-QTSGKKHPYLFS-QCQAIHARSLFPCQDTPSVKSTYTA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  206 KIRreprhlaiSNMPLVKSVTVAEGLIEDH----FDVTVKMSTYLVAFIISDFESvskiTKSGVKVSVYAVPDKINQADY 281
Cdd:TIGR02411 154 EVE--------SPLPVLMSGIRDGETSNDPgkylFKQKVPIPAYLIAIASGDLAS----APIGPRSTVYSEPEQLEKCQY 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  282 ALDAAV-TLLEFYEDyFSIPYPLPKQDLAAIPD-FQSGAMENWGLTTyrESALLFDAEKSSASsklgitmTVAHELAHQW 359
Cdd:TIGR02411 222 EFENDTeKFIKTAED-LIFPYEWGQYDLLVLPPsFPYGGMENPNLTF--ATPTLIAGDRSNVD-------VIAHELAHSW 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091  360 FGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKvgdyffgKCFDAM--------EVDALNSSHPVSTPVEN--PAQI 429
Cdd:TIGR02411 292 SGNLVTNCSWEHFWLNEGWTVYLERRIIGRLYGEKT-------RHFSALigwgdlqeSVKTLGETPEFTKLVVDlkDNDP 364
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309747091  430 REMFDDVSYDKGACILNMLREYLSADA-FKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDG 490
Cdd:TIGR02411 365 DDAFSSVPYEKGFNFLFYLEQLLGGPAeFDPFLRHYFKKFAYKSLDTYQFKDALYEYFKDKK 426
pepN PRK14015
aminopeptidase N; Provisional
245-468 2.29e-09

aminopeptidase N; Provisional


Pssm-ID: 237585 [Multi-domain]  Cd Length: 875  Bit Score: 59.76  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 245 YLVAFIISDFESVSK--ITKSG--VKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYplpkqDL-----AAIPDFQ 315
Cdd:PRK14015 190 YLFALVAGDLDVLEDtfTTRSGreVALEIYVEPGNLDKCDHAMDSLKKSMKWDEERFGLEY-----DLdifmiVAVDDFN 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 316 SGAMENWGLTTYRESALLFDAEksSASSK--LGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKF--MEF------- 384
Cdd:PRK14015 265 MGAMENKGLNIFNSKYVLADPE--TATDAdyERIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGLTVFrdQEFsadlgsr 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309747091 385 -------VSVSVTH--PElkvgdyffgkcfDA--MevdalnsSHPVstpveNPAQIREM--FDDVS-YDKGACILNMLRE 450
Cdd:PRK14015 343 avkriedVRVLRAAqfAE------------DAgpM-------AHPV-----RPDSYIEInnFYTATvYEKGAEVIRMLHT 398
                        250
                 ....*....|....*...
gi 309747091 451 YLSADAFKSGIVQYLQKH 468
Cdd:PRK14015 399 LLGEEGFRKGMDLYFERH 416
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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