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Conserved domains on  [gi|28380715|gb|AAF57570|]
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uncharacterized protein Dmel_CG10073, isoform A [Drosophila melanogaster]

Protein Classification

M28 family metallopeptidase( domain architecture ID 10133732)

M28 family metallopeptidase is a zinc-dependent peptidase that may be an aminopeptidase or a carboxypeptidase with co-catalytic zinc ions; similar to Homo sapiens endoplasmic reticulum metallopeptidase 1 that is required for the organization of somatic cells and oocytes into discrete follicular structures

CATH:  3.40.630.10
EC:  3.-.-.-
Gene Ontology:  GO:0008237|GO:0006508|GO:0008270
MEROPS:  M28
PubMed:  7674922|10493853|12773192|18429165

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 72-379 9.57e-149

M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.


:

Pssm-ID: 349872 [Multi-domain]  Cd Length: 307  Bit Score: 440.10  E-value: 9.57e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715  72 KGVFIAERAQSNLYKLAEIGTKVVGSDNNEnKTVDYLMGLVNEIQENCLDDYFDIEVDLQEVSGS--YIHWTMVNMYQGV 149
Cdd:cd03875   1 PGGFSLERAWEDLQVLISIGPHPYGSHNND-KVRDYLLARVEEIKERANANGLEVEVQDDTGSGSfnFLSSGMTLVYFEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 150 QNIVIKLSPKNTTSTTYLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMCSTKQAIRHPVVFLLNGAEENPLQASHGFI 229
Cdd:cd03875  80 TNIVVRISGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAFI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 230 TQHKWAKNCKVVLNLDAAGNGGSDIVFQTGPnsPWLVEKYKENAPHYLATTMAEEIFQTGILPSDTDFAIFVKYGNLIGL 309
Cdd:cd03875 160 TQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPGL 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 310 DMAKFINGFAYHTKYDQFSNIPRGSIQNTGDNLLGLVRSIANSTELDNTEAYATGHAIFFDVLGLYFISY 379
Cdd:cd03875 238 DIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYRGGPAVFFDLLGLFFVYY 307
 
Name Accession Description Interval E-value
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 72-379 9.57e-149

M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.


Pssm-ID: 349872 [Multi-domain]  Cd Length: 307  Bit Score: 440.10  E-value: 9.57e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715  72 KGVFIAERAQSNLYKLAEIGTKVVGSDNNEnKTVDYLMGLVNEIQENCLDDYFDIEVDLQEVSGS--YIHWTMVNMYQGV 149
Cdd:cd03875   1 PGGFSLERAWEDLQVLISIGPHPYGSHNND-KVRDYLLARVEEIKERANANGLEVEVQDDTGSGSfnFLSSGMTLVYFEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 150 QNIVIKLSPKNTTSTTYLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMCSTKQAIRHPVVFLLNGAEENPLQASHGFI 229
Cdd:cd03875  80 TNIVVRISGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAFI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 230 TQHKWAKNCKVVLNLDAAGNGGSDIVFQTGPnsPWLVEKYKENAPHYLATTMAEEIFQTGILPSDTDFAIFVKYGNLIGL 309
Cdd:cd03875 160 TQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPGL 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 310 DMAKFINGFAYHTKYDQFSNIPRGSIQNTGDNLLGLVRSIANSTELDNTEAYATGHAIFFDVLGLYFISY 379
Cdd:cd03875 238 DIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYRGGPAVFFDLLGLFFVYY 307
Peptidase_M28 pfam04389
Peptidase family M28;
151-346 5.92e-55

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 188.26  E-value: 5.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715   151 NIVIKLSPKNttSTTYLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMcSTKQAIRHPVVFLLNGAEENPLQASHGFIT 230
Cdd:pfam04389   1 NVIAKLPGKA--PDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVL-AAGQRPKRSVRFLFFDAEEAGLLGSHHFAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715   231 QHKWAKNCKVVLNLDAAGNGGSDIVFQTGPNSPWLVEKYKENAPHYLATTMAEEIFQTGILPSDTDFAIFVKYGnlI-GL 309
Cdd:pfam04389  78 SHPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERGGPGRSDHAPFIKAG--IpGL 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 28380715   310 DMAKFINGFAYHTKYDQFSNIPRGSIQNTGDNLLGLV 346
Cdd:pfam04389 156 DLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 141-354 8.64e-20

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 89.81  E-value: 8.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 141 TMVNMYQGVQNIVIKLsPKNTTSTTYLLVNSHFDSKPT-SPSAGD--AGqmVVAILEVLRVMCSTKQAIRHPVVFLLNGA 217
Cdd:COG2234  38 LLEAAGGDSRNVIAEI-PGTDPPDEVVVLGAHYDSVGSiGPGADDnaSG--VAALLELARALAALGPKPKRTIRFVAFGA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 218 EENPLQASHGFITQHKWA-KNCKVVLNLDAAGNGG--SDIVFQTGPNSPWLVEKYKENAPHYLATTMAEEIFQTGiLPSD 294
Cdd:COG2234 115 EEQGLLGSRYYAENLKAPlEKIVAVLNLDMIGRGGprNYLYVDGDGGSPELADLLEAAAKAYLPGLGVDPPEETG-GYGR 193

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28380715 295 TDFAIFVKYG-NLIGLDMAKFINGFAYHTKYDQFSNIPRGSIQNTGDNLLGLVRSIANSTE 354
Cdd:COG2234 194 SDHAPFAKAGiPALFLFTGAEDYHPDYHTPSDTLDKIDLDALAKVAQLLAALVYELANADE 254
 
Name Accession Description Interval E-value
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 72-379 9.57e-149

M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.


Pssm-ID: 349872 [Multi-domain]  Cd Length: 307  Bit Score: 440.10  E-value: 9.57e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715  72 KGVFIAERAQSNLYKLAEIGTKVVGSDNNEnKTVDYLMGLVNEIQENCLDDYFDIEVDLQEVSGS--YIHWTMVNMYQGV 149
Cdd:cd03875   1 PGGFSLERAWEDLQVLISIGPHPYGSHNND-KVRDYLLARVEEIKERANANGLEVEVQDDTGSGSfnFLSSGMTLVYFEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 150 QNIVIKLSPKNTTSTTYLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMCSTKQAIRHPVVFLLNGAEENPLQASHGFI 229
Cdd:cd03875  80 TNIVVRISGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAFI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 230 TQHKWAKNCKVVLNLDAAGNGGSDIVFQTGPnsPWLVEKYKENAPHYLATTMAEEIFQTGILPSDTDFAIFVKYGNLIGL 309
Cdd:cd03875 160 TQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPGL 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 310 DMAKFINGFAYHTKYDQFSNIPRGSIQNTGDNLLGLVRSIANSTELDNTEAYATGHAIFFDVLGLYFISY 379
Cdd:cd03875 238 DIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYRGGPAVFFDLLGLFFVYY 307
Peptidase_M28 pfam04389
Peptidase family M28;
151-346 5.92e-55

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 188.26  E-value: 5.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715   151 NIVIKLSPKNttSTTYLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMcSTKQAIRHPVVFLLNGAEENPLQASHGFIT 230
Cdd:pfam04389   1 NVIAKLPGKA--PDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVL-AAGQRPKRSVRFLFFDAEEAGLLGSHHFAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715   231 QHKWAKNCKVVLNLDAAGNGGSDIVFQTGPNSPWLVEKYKENAPHYLATTMAEEIFQTGILPSDTDFAIFVKYGnlI-GL 309
Cdd:pfam04389  78 SHPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERGGPGRSDHAPFIKAG--IpGL 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 28380715   310 DMAKFINGFAYHTKYDQFSNIPRGSIQNTGDNLLGLV 346
Cdd:pfam04389 156 DLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 150-349 1.46e-27

M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.


Pssm-ID: 349868 [Multi-domain]  Cd Length: 202  Bit Score: 110.90  E-value: 1.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 150 QNIVIKLSPKnTTSTTYLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMCSTKQAIRHPVVFLLNGAEENPLQASHGFI 229
Cdd:cd02690   2 YNVIATIKGS-DKPDEVILIGAHYDSVPLSPGANDNASGVAVLLELARVLSKLQLKPKRSIRFAFWDAEELGLLGSKYYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 230 TQHKW-AKNCKVVLNLDAAGNGGSDIVFQTGPNSPWLVEKYKENAPHYLATTMAEEIFQTGILPSDTDFAIFVKYG---- 304
Cdd:cd02690  81 EQLLSsLKNIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELENVVYTVVYKEDGGTGGSDHRPFLARGipaa 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 28380715 305 NLIGLDMAkfiNGFAYHTKYDQFSNIPRGSIQNTGDNLLGLVRSI 349
Cdd:cd02690 161 SLIQSESY---NFPYYHTTQDTLENIDKDTLKRAGDILASFLYRL 202
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 141-354 8.64e-20

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 89.81  E-value: 8.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 141 TMVNMYQGVQNIVIKLsPKNTTSTTYLLVNSHFDSKPT-SPSAGD--AGqmVVAILEVLRVMCSTKQAIRHPVVFLLNGA 217
Cdd:COG2234  38 LLEAAGGDSRNVIAEI-PGTDPPDEVVVLGAHYDSVGSiGPGADDnaSG--VAALLELARALAALGPKPKRTIRFVAFGA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 218 EENPLQASHGFITQHKWA-KNCKVVLNLDAAGNGG--SDIVFQTGPNSPWLVEKYKENAPHYLATTMAEEIFQTGiLPSD 294
Cdd:COG2234 115 EEQGLLGSRYYAENLKAPlEKIVAVLNLDMIGRGGprNYLYVDGDGGSPELADLLEAAAKAYLPGLGVDPPEETG-GYGR 193

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28380715 295 TDFAIFVKYG-NLIGLDMAKFINGFAYHTKYDQFSNIPRGSIQNTGDNLLGLVRSIANSTE 354
Cdd:COG2234 194 SDHAPFAKAGiPALFLFTGAEDYHPDYHTPSDTLDKIDLDALAKVAQLLAALVYELANADE 254
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 150-340 2.25e-10

M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349911 [Multi-domain]  Cd Length: 262  Bit Score: 62.20  E-value: 2.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 150 QNIVIKLSPKNTTSTT-YLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMCS--TKQAIRhpvvFLLNGAEENPLQASH 226
Cdd:cd05661  61 HNVIATKKPDNNKNNNdIIIVTSHYDSVVKAPGANDNASGTAVTLELARVFKKvkTDKELR----FIAFGAEENGLLGSK 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 227 GFITQ--HKWAKNCKVVLNLDAAGNG---GSDIVFQTGPNSPWLVEKYKENAPHYLATTMAEeifqtgILPSDTDFAIFV 301
Cdd:cd05661 137 YYVASlsEDEIKRTIGVFNLDMVGTSdakAGDLYAYTIDGKPNLVTDSGAAASKRLSGVLPL------VQQGSSDHVPFH 210

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 28380715 302 KygnlIGLDMAKFINGFA--------YHTKYDQFSNIPRGSIQNTGD 340
Cdd:cd05661 211 E----AGIPAALFIHMDPetepvepwYHTPNDTVENISKERLDNALD 253
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 150-248 5.81e-05

M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position.


Pssm-ID: 349875 [Multi-domain]  Cd Length: 286  Bit Score: 46.08  E-value: 5.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 150 QNIVIKLSPKNTTSTTYLLVNSHFDS-------KPTSPSAGDAGQMVVAILEVLRVMCSTKQAIRHPVVFLLNGAEENPL 222
Cdd:cd03879  74 QPSIIATIPGSEKSDEIVVIGAHQDSingsnpsNGRAPGADDDGSGTVTILEALRVLLESGFQPKNTIEFHWYAAEEGGL 153

                        90       100
                ....*....|....*....|....*..
gi 28380715 223 QASHGFITQHKWA-KNCKVVLNLDAAG 248
Cdd:cd03879 154 LGSQAIATQYKSEgKNVKAMLQLDMTG 180
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 153-302 3.74e-04

M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349893 [Multi-domain]  Cd Length: 281  Bit Score: 43.21  E-value: 3.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 153 VIKLSPKNTTSTTYLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMcsTKQAIRHPVVFLLNGAEENP-----LQASHG 227
Cdd:cd05640  55 LIADLPGSYSQDKLILIGAHYDTVPGSPGADDNASGVAALLELARLL--ATLDPNHTLRFVAFDLEEYPffargLMGSHA 132

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28380715 228 FITQ-HKWAKNCKVVLNLDAAGNGGSDivfqtgPNSpwlvEKYKENAPHYLATTMAEEIFQTGILPSDTDFAIFVK 302
Cdd:cd05640 133 YAEDlLRPLTPIVGMLSLEMIGYYDPF------PHS----QAYPAGFELHFYPHMGDFIAVVGRLRSRKLVRAFKR 198
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 101-273 2.54e-03

M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349910 [Multi-domain]  Cd Length: 290  Bit Score: 40.81  E-value: 2.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 101 ENKTVDYLmglVNEIQENCLDDYFDIEVDLQEVSgsyihwtMVNMYQGV--QNIVIKLsPKNTTSTTYLLVNSHFDSKPT 178
Cdd:cd05660  19 EKKTVDYL---AEQFKELGLKPAGSDGSYLQAVP-------LVSKIEYStsHNVVAIL-PGSKLPDEYIVLSAHWDHLGI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 179 SPSAG---------DAGQMVVAILEVLRVMCSTKQAIRHPVVFLLNGAEENPLQASHgFITQHKWAKNCKVV--LNLDAA 247
Cdd:cd05660  88 GPPIGgdeiyngavDNASGVAAVLELARVFAAQDQRPKRSIVFLAVTAEEKGLLGSR-YYAANPIFPLDKIVanLNIDMI 166

                       170       180
                ....*....|....*....|....*..
gi 28380715 248 G-NGGSDIVFQTGPNSPWLvEKYKENA 273
Cdd:cd05660 167 GrIGPTKDVLLIGSGSSEL-ENILKEA 192
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 78-251 6.51e-03

M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures.


Pssm-ID: 349873 [Multi-domain]  Cd Length: 289  Bit Score: 39.59  E-value: 6.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715  78 ERAQSNLYKLAEI-----GTKVVGSdNNENKTVDYLmglvneiqENCLDDYFDIEVDLQEVSGSYIhWTmvnmyqgvQNi 152
Cdd:cd03876   5 DNLMAHLQQLQDIadangGNRAFGS-PGYNASVDYV--------KNELKAAGYYDVTLQPFTSLYR-TT--------YN- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 153 VIKLSP---KNTTsttyLLVNSHFDSKPTSPSAGDAGQMVVAILEVLRVMcsTKQAIRHPVVFLLNGAEENPLQASHGFI 229
Cdd:cd03876  66 VIAETKggdPNNV----VMLGAHLDSVSAGPGINDNGSGSAALLEVALAL--AKFKVKNAVRFAWWTAEEFGLLGSKFYV 139

                       170       180
                ....*....|....*....|....*.
gi 28380715 230 TQ--HKWAKNCKVVLNLD--AAGNGG 251
Cdd:cd03876 140 NNlsSEERSKIRLYLNFDmiASPNYG 165
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 138-251 9.35e-03

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440389 [Multi-domain]  Cd Length: 388  Bit Score: 39.48  E-value: 9.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28380715 138 IHWTMVNMYQGVQNIVIKLSPKNTTSTtyLLVNSHFD-----------SKPTSPS----------AGDAGQMVVAILEVL 196
Cdd:COG0624  47 FEVERLEVPPGRPNLVARRPGDGGGPT--LLLYGHLDvvppgdlelwtSDPFEPTiedgrlygrgAADMKGGLAAMLAAL 124

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28380715 197 RVMCSTKQAIRHPVVFLLNGAEENPLQASHGFITQHKWAKNCKVVLNLDAAGNGG 251
Cdd:COG0624 125 RALLAAGLRLPGNVTLLFTGDEEVGSPGARALVEELAEGLKADAAIVGEPTGVPT 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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