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Conserved domains on  [gi|21355531|ref|NP_651281|]
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uncharacterized protein Dmel_CG13630 [Drosophila melanogaster]

Protein Classification

M24 family metallopeptidase( domain architecture ID 320)

M24 family metallopeptidase cleaves amido-, imido-, or amidino-containing bonds, exhibiting a fairly narrow substrate specificity compared to other metallo-aminopeptidases, possibly playing roles in regulation of biological processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
APP_MetAP super family cl00279
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
10-369 1.21e-177

A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.


The actual alignment was detected with superfamily member PLN03158:

Pssm-ID: 469704 [Multi-domain]  Cd Length: 396  Bit Score: 499.36  E-value: 1.21e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   10 CGKDATLQCPTCLKLGI--KGSFFCSQPCFKGFWKEHKAIHALAAGASNSAEQDGAYNPW--------------PHFRFT 73
Cdd:PLN03158  15 CSKPAHLQCPKCLELKLprEGASFCSQDCFKAAWSSHKSVHTKAKLSSIGQNSDAPAEGWlyclkkgqartsklPDFDWT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   74 GKLRPFPQTPKRTVPNAIQRPDYADHpaGRSLSEEALRGTKI-KVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDE 152
Cdd:PLN03158  95 GPLRPYPISPRRVVPDHIPKPDWALD--GTPKIEPNSDLQHSvEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  153 LDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKH 232
Cdd:PLN03158 173 IDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEAS 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  233 KKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFT 312
Cdd:PLN03158 253 RQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFT 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355531  313 IEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTKRRENNGQ--PW 369
Cdd:PLN03158 333 IEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDvfPW 391
 
Name Accession Description Interval E-value
PLN03158 PLN03158
methionine aminopeptidase; Provisional
10-369 1.21e-177

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 499.36  E-value: 1.21e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   10 CGKDATLQCPTCLKLGI--KGSFFCSQPCFKGFWKEHKAIHALAAGASNSAEQDGAYNPW--------------PHFRFT 73
Cdd:PLN03158  15 CSKPAHLQCPKCLELKLprEGASFCSQDCFKAAWSSHKSVHTKAKLSSIGQNSDAPAEGWlyclkkgqartsklPDFDWT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   74 GKLRPFPQTPKRTVPNAIQRPDYADHpaGRSLSEEALRGTKI-KVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDE 152
Cdd:PLN03158  95 GPLRPYPISPRRVVPDHIPKPDWALD--GTPKIEPNSDLQHSvEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  153 LDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKH 232
Cdd:PLN03158 173 IDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEAS 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  233 KKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFT 312
Cdd:PLN03158 253 RQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFT 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355531  313 IEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTKRRENNGQ--PW 369
Cdd:PLN03158 333 IEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDvfPW 391
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
123-360 1.68e-145

Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.


Pssm-ID: 238519 [Multi-domain]  Cd Length: 238  Bit Score: 411.50  E-value: 1.68e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGD 202
Cdd:cd01086   1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 203 LCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHG 282
Cdd:cd01086  81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355531 283 IHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTK 360
Cdd:cd01086 161 IGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
115-363 1.49e-133

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 381.66  E-value: 1.49e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:COG0024   1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:COG0024  81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240

                ....*....
gi 21355531 355 CEILTKRRE 363
Cdd:COG0024 241 PEILTLPDG 249
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
115-361 6.66e-110

methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 321.60  E-value: 6.66e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:TIGR00500   1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:TIGR00500  81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240

                  ....*..
gi 21355531   355 CEILTKR 361
Cdd:TIGR00500 241 PEILTER 247
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
124-352 9.28e-57

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 184.37  E-value: 9.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   124 EGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYpsplNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDL 203
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   204 CNIDVTV-YHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFS-VVRSYCGH 281
Cdd:pfam00557  77 VLIDVGAeYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGLGH 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355531   282 GIHRVFHTAPNVPHYAKNsavGVMAPGHCFTIEPMIsvgvqkaetwpddwtaVTADGLYSAQFEQTLLVNE 352
Cdd:pfam00557 157 GIGLEVHEGPYISRGGDD---RVLEPGMVFTIEPGI----------------YFIPGWGGVRIEDTVLVTE 208
 
Name Accession Description Interval E-value
PLN03158 PLN03158
methionine aminopeptidase; Provisional
10-369 1.21e-177

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 499.36  E-value: 1.21e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   10 CGKDATLQCPTCLKLGI--KGSFFCSQPCFKGFWKEHKAIHALAAGASNSAEQDGAYNPW--------------PHFRFT 73
Cdd:PLN03158  15 CSKPAHLQCPKCLELKLprEGASFCSQDCFKAAWSSHKSVHTKAKLSSIGQNSDAPAEGWlyclkkgqartsklPDFDWT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   74 GKLRPFPQTPKRTVPNAIQRPDYADHpaGRSLSEEALRGTKI-KVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDE 152
Cdd:PLN03158  95 GPLRPYPISPRRVVPDHIPKPDWALD--GTPKIEPNSDLQHSvEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  153 LDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKH 232
Cdd:PLN03158 173 IDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEAS 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  233 KKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFT 312
Cdd:PLN03158 253 RQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFT 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355531  313 IEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTKRRENNGQ--PW 369
Cdd:PLN03158 333 IEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDvfPW 391
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
123-360 1.68e-145

Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.


Pssm-ID: 238519 [Multi-domain]  Cd Length: 238  Bit Score: 411.50  E-value: 1.68e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPDQRPLQDGD 202
Cdd:cd01086   1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 203 LCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHG 282
Cdd:cd01086  81 IVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHG 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355531 283 IHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETGCEILTK 360
Cdd:cd01086 161 IGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
115-363 1.49e-133

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 381.66  E-value: 1.49e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:COG0024   1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:COG0024  81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240

                ....*....
gi 21355531 355 CEILTKRRE 363
Cdd:COG0024 241 PEILTLPDG 249
PRK05716 PRK05716
methionine aminopeptidase; Validated
115-364 1.34e-130

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 374.09  E-value: 1.34e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:PRK05716   3 ITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIPS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:PRK05716  83 DKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:PRK05716 163 VREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDG 242
                        250
                 ....*....|
gi 21355531  355 CEILTKRREN 364
Cdd:PRK05716 243 PEILTLRPEE 252
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
115-361 6.66e-110

methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 321.60  E-value: 6.66e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVICHGIPD 194
Cdd:TIGR00500   1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSV 274
Cdd:TIGR00500  81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   275 VRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNETG 354
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240

                  ....*..
gi 21355531   355 CEILTKR 361
Cdd:TIGR00500 241 PEILTER 247
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
109-361 1.34e-107

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 316.01  E-value: 1.34e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  109 ALRGTKIKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYNFPKSCCTSVNEVI 188
Cdd:PRK12896   2 AQEGRGMEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  189 CHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVA 268
Cdd:PRK12896  82 AHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  269 PHGFSVVRSYCGHGIHRVFHTAPNV-PHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQT 347
Cdd:PRK12896 162 KNGYSVVRDLTGHGVGRSLHEEPSViLTYTDPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHT 241
                        250
                 ....*....|....
gi 21355531  348 LLVNETGCEILTKR 361
Cdd:PRK12896 242 VVVTRDGPEILTDR 255
PRK12318 PRK12318
methionyl aminopeptidase;
104-359 3.16e-80

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 247.42  E-value: 3.16e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  104 SLSEEALRGTKIKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPLNYYN--FPKSCC 181
Cdd:PRK12318  30 NLKQLYASQYDIIIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAIPAPLNYGSppFPKTIC 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  182 TSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGN 261
Cdd:PRK12318 110 TSLNEVICHGIPNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGE 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  262 VIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYaKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDD-WTAVTADGLY 340
Cdd:PRK12318 190 VIENCADKYGFSVVDQFVGHGVGIKFHENPYVPHH-RNSSKIPLAPGMIFTIEPMINVGKKEGVIDPINhWEARTCDNQP 268
                        250
                 ....*....|....*....
gi 21355531  341 SAQFEQTLLVNETGCEILT 359
Cdd:PRK12318 269 SAQWEHTILITETGYEILT 287
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
124-352 9.28e-57

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 184.37  E-value: 9.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   124 EGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYpsplNYYNFPKSCCTSVNEVICHGIPDQRPLQDGDL 203
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   204 CNIDVTV-YHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFS-VVRSYCGH 281
Cdd:pfam00557  77 VLIDVGAeYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGLGH 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355531   282 GIHRVFHTAPNVPHYAKNsavGVMAPGHCFTIEPMIsvgvqkaetwpddwtaVTADGLYSAQFEQTLLVNE 352
Cdd:pfam00557 157 GIGLEVHEGPYISRGGDD---RVLEPGMVFTIEPGI----------------YFIPGWGGVRIEDTVLVTE 208
PRK12897 PRK12897
type I methionyl aminopeptidase;
115-360 1.19e-52

type I methionyl aminopeptidase;


Pssm-ID: 171806  Cd Length: 248  Bit Score: 175.22  E-value: 1.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  115 IKVLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVhEAAIERECYPSPLNYYN-FPKSCCTSVNEVICHGIP 193
Cdd:PRK12897   2 ITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFV-EAYLEKHGATSEQKGYNgYPYAICASVNDEMCHAFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  194 DQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFS 273
Cdd:PRK12897  81 ADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  274 VVRSYCGHGIHRVFHTAPNVPHYAKNSAVGVMAPGHCFTIEPMISVGVQKAETWPDDWTAVTADGLYSAQFEQTLLVNET 353
Cdd:PRK12897 161 VARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKD 240

                 ....*..
gi 21355531  354 GCEILTK 360
Cdd:PRK12897 241 GPIILTK 247
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
123-355 1.76e-45

A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.


Pssm-ID: 238514 [Multi-domain]  Cd Length: 207  Bit Score: 154.92  E-value: 1.76e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSPlnyynfpkSCCTSVNEV--ICHGIPDQRPLQD 200
Cdd:cd01066   1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYPAG--------PTIVGSGARtaLPHYRPDDRRLQE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVR-SYC 279
Cdd:cd01066  73 GDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFgHRT 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355531 280 GHGIHRVFHTAPNVPHYAKnsavGVMAPGHCFTIEPMISVgvqkaetwpddwtavtaDGLYSAQFEQTLLVNETGC 355
Cdd:cd01066 153 GHGIGLEIHEPPVLKAGDD----TVLEPGMVFAVEPGLYL-----------------PGGGGVRIEDTVLVTEDGP 207
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
117-360 4.32e-37

Xaa-Pro aminopeptidase [Amino acid transport and metabolism];


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 135.72  E-value: 4.32e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 117 VLDDEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECypsplNYYNFPKSCCTSVNEVICHGIPDQR 196
Cdd:COG0006  73 IKSPEEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGA-----EGPSFDTIVASGENAAIPHYTPTDR 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 197 PLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFsvvR 276
Cdd:COG0006 148 PLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGY---G 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 277 SY----CGHGIHRVFHTapnVPHYAKNSAVgVMAPGHCFTIEPMISVgvqkaetwpddwtavtaDGLYSAQFEQTLLVNE 352
Cdd:COG0006 225 EYfphgTGHGVGLDVHE---GPQISPGNDR-PLEPGMVFTIEPGIYI-----------------PGIGGVRIEDTVLVTE 283

                ....*...
gi 21355531 353 TGCEILTK 360
Cdd:COG0006 284 DGAEVLTR 291
PRK07281 PRK07281
methionyl aminopeptidase;
172-363 7.30e-30

methionyl aminopeptidase;


Pssm-ID: 180918  Cd Length: 286  Bit Score: 116.10  E-value: 7.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  172 NYYNFPKSCCTSVNEVICHGIPDQRPLQDGDLCNIDVTV------------------------YHRGFHGDLNET---FF 224
Cdd:PRK07281  63 AMMDYPYATCCGLNDEVAHAFPRHYILKEGDLLKVDMVLsepldksivdvsklnfdnveqmkkYTESYRGGLADScwaYA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  225 VGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHRVFHTAPNVPHYAKNSAVGV 304
Cdd:PRK07281 143 VGTPSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLR 222
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355531  305 MAPGHCFTIEPMISVGvqkaeTWPDD------WTAVTADGLYSAQFEQTLLVNETGCEILTKRRE 363
Cdd:PRK07281 223 LREGMVLTIEPMINTG-----TWEIDtdmktgWAHKTLDGGLSCQYEHQFVITKDGPVILTSQGE 282
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
123-360 5.47e-28

Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.


Pssm-ID: 238521 [Multi-domain]  Cd Length: 291  Bit Score: 111.19  E-value: 5.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSplnyynFPKSCctSVNEVICHGIP---DQRPLQ 199
Cdd:cd01088   1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAGPA------FPVNL--SINECAAHYTPnagDDTVLK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 200 DGDLCNIDVTVYHRGFHGDlneTFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYC 279
Cdd:cd01088  73 EGDVVKLDFGAHVDGYIAD---SAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 280 GHGIHR-VFHTAPNVPHYaKNSAVGVMAPGHCFTIEPMISVGVQK----------------------------------- 323
Cdd:cd01088 150 GHSIERyRLHAGKSIPNV-KGGEGTRLEEGDVYAIEPFATTGKGYvhdgpecsiymlnrdkplrlprarklldviyenfg 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355531 324 ----AETWPDDWTA----------------------VTADGLYSAQFEQTLLVNETGCEILTK 360
Cdd:cd01088 229 tlpfARRWLDRLGEtkllmalknlckagivypypvlKEISGGYVAQFEHTIIVREDGKEVTTR 291
zf-C6H2 pfam15801
zf-MYND-like zinc finger, mRNA-binding; zf-C6H2 is an unusual zinc-finger similar to zf-MYND, ...
5-48 3.73e-25

zf-MYND-like zinc finger, mRNA-binding; zf-C6H2 is an unusual zinc-finger similar to zf-MYND, pfam01753.This zinc-finger is found at the N-terminus of Pfam families Exo_endo_phos pfam03372 and Peptidase_M24 pfam00557. The domain is missing in prokaryotic methionine aminopeptidases, and is a unique type of zinc-finger domain. It consists of a C2-C2 zinc-finger motif similar to the RING finger family followed by a C2H2 motif similar to zinc-fingers involved in RNA-binding. In yeast the domain chelates zinc in a 2:1 ratio. The domain is found in yeast, plants and mammals. The domain is necessary for the association of the methionine aminopeptidase with the ribosome and the normal processing of the peptidase.


Pssm-ID: 464880 [Multi-domain]  Cd Length: 46  Bit Score: 96.15  E-value: 3.73e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 21355531     5 CETTNCGKDA-TLQCPTCLKLGIKGSFFCSQPCFKGFWKEHKAIH 48
Cdd:pfam15801   1 CAGPGCGKEAsSLQCPTCLKLGIKGSFFCSQDCFKKNWKSHKAIH 45
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
123-317 1.02e-24

Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline.


Pssm-ID: 238525 [Multi-domain]  Cd Length: 208  Bit Score: 99.89  E-value: 1.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGIT----TDELDRLVHEAAIERecyPSplnyynFPKSCCTSVNEVICHGIPDQRPL 198
Cdd:cd01092   1 IELLRKAARIADKAFEELLEFIKPGMTerevAAELEYFMRKLGAEG---PS------FDTIVASGPNSALPHGVPSDRKI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 199 QDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGFSvvrSY 278
Cdd:cd01092  72 EEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYG---EY 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21355531 279 ----CGHGIHRVFHTAPNVPHYAKnsavGVMAPGHCFTIEPMI 317
Cdd:cd01092 149 fihrTGHGVGLEVHEAPYISPGSD----DVLEEGMVFTIEPGI 187
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
123-360 3.27e-11

Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.


Pssm-ID: 238520 [Multi-domain]  Cd Length: 243  Bit Score: 62.59  E-value: 3.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 123 IEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERECYPSplnyYNFPksCCTSVNEVICHGIPDQRPLQDGD 202
Cdd:cd01087   1 IELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGARLA----YSYI--VAAGSNAAILHYVHNDQPLKDGD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 203 LCNIDVTVYHRGFHGDLNETFFV-GNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDI----GNVIQKYVAPHGF----- 272
Cdd:cd01087  75 LVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIhllaHRVLAEGLKELGIlkgdv 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 273 ------SVVRSYCGHGI-HRVFHTAPNVPHYAK-NSAVGVMAPGHCFTIEPMISVgvqkaetwPDDWTAVTADglysAQF 344
Cdd:cd01087 155 deivesGAYAKFFPHGLgHYLGLDVHDVGGYLRyLRRARPLEPGMVITIEPGIYF--------IPDLLDVPEY----FRG 222
                       250       260
                ....*....|....*....|.
gi 21355531 345 -----EQTLLVNETGCEILTK 360
Cdd:cd01087 223 ggiriEDDVLVTEDGPENLTR 243
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
176-285 1.41e-08

42K curved DNA binding protein; Proteins identified by this model have been identified in a number of species as a nuclear (but not nucleolar) protein with a cell cycle dependence. Various names given to members of this family have included cell cycle protein p38-2G4, DNA-binding protein GBP16, and proliferation-associated protein 1. This protein is closely related to methionine aminopeptidase, a cobolt-binding protein. [Unknown function, General]


Pssm-ID: 273105  Cd Length: 390  Bit Score: 56.05  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   176 FPKscCTSVNEVICHGIP----DQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSE-----KHKKLVQVTHEALSKA 246
Cdd:TIGR00495  78 FPT--CISVNNCVGHFSPlksdQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEepvtgRKADVIAAAHLAAEAA 155
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 21355531   247 IEFVRPGEKYRDIGNVIQKYVAPHGFSVVRSYCGHGIHR 285
Cdd:TIGR00495 156 LRLVKPGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQ 194
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
11-107 4.04e-08

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 55.12  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531   11 GKDATLQCPTCLKLGIKG--SFFCSQPCFKGFWKEHKAIHALAA--GASNSAEQD------GAYNPWPHFRFTGKLRPFP 80
Cdd:PLN03144  70 SEPATLQCVGCVKAKLPVskSYHCSPKCFSDAWRHHRVLHERAAsaVRENGNEEDelfgrfNSSGSGVLSTSDSGSASSA 149
                         90       100
                 ....*....|....*....|....*..
gi 21355531   81 QTPKRTVPNAIQRPDYADHPAGRSLSE 107
Cdd:PLN03144 150 SLTNGSVPLYPSGIEQKTQVGGETWIE 176
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
120-359 8.76e-08

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 53.57  E-value: 8.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  120 DEEIEGMRVAGRLGRECLDEGAKAVEVGITTDELD-RLVHEAAIERECYPSplnyYNfpksccTSV----NEVICHGIPD 194
Cdd:PRK10879 176 PEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEgEIHHEFNRHGARYPS----YN------TIVgsgeNGCILHYTEN 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  195 QRPLQDGDLCNIDVTVYHRGFHGDLNETFFV-GNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDI-GNVIQKYVAP--- 269
Cdd:PRK10879 246 ESEMRDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVtGEVVRIMVSGlvk 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  270 ----HG-------FSVVRSYCGHGI-HRVFHTAPNVPHYAKNSAvGVMAPGHCFTIEPMISVGvqkaetwPDDWTAVTAD 337
Cdd:PRK10879 326 lgilKGdvdqliaENAHRPFFMHGLsHWLGLDVHDVGVYGQDRS-RILEPGMVLTVEPGLYIA-------PDADVPEQYR 397
                        250       260
                 ....*....|....*....|..
gi 21355531  338 GLySAQFEQTLLVNETGCEILT 359
Cdd:PRK10879 398 GI-GIRIEDDIVITETGNENLT 418
PRK14576 PRK14576
putative endopeptidase; Provisional
122-360 2.69e-07

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 51.94  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  122 EIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIErecYPSPlnyyNFPKSCCTSVNEVICHGI-PDQRPLQD 200
Cdd:PRK14576 182 EIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVMS---FPET----NFSRFNLISVGDNFSPKIiADTTPAKV 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGN----VIQKYVAPHgfsVVR 276
Cdd:PRK14576 255 GDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDstmaVIKTSGLPH---YNR 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  277 SYCGHGiHRVFHTAPNVPhYAKNSAVGVMAPGHCFTIE-PMISVGVQkaetwpddwtavtadglySAQFEQTLLVNETGC 355
Cdd:PRK14576 332 GHLGHG-DGVFLGLEEVP-FVSTQATETFCPGMVLSLEtPYYGIGVG------------------SIMLEDMILITDSGF 391

                 ....*
gi 21355531  356 EILTK 360
Cdd:PRK14576 392 EFLSK 396
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
127-294 5.91e-07

Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family members have been implicated in cell cycle control.


Pssm-ID: 238522  Cd Length: 228  Bit Score: 50.02  E-value: 5.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 127 RVAGRLGRECLDEGAKAVEVGITTDEL----DRLVHEAAieRECYPSPLNYYN---FPKscCTSVNEVICHGIP----DQ 195
Cdd:cd01089   5 KTAGQIANKVLKQVISLCVPGAKVVDLcekgDKLILEEL--GKVYKKEKKLEKgiaFPT--CISVNNCVCHFSPlksdAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 196 RPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSE-----KHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPH 270
Cdd:cd01089  81 YTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAEtpvtgKKADVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVDY 160
                       170       180
                ....*....|....*....|....
gi 21355531 271 GFSVVRSYCGHGIHRVFHTAPNVP 294
Cdd:cd01089 161 GCTPVEGVLSHQLKRVVSSGEGKA 184
PRK15173 PRK15173
peptidase; Provisional
122-360 9.25e-07

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 50.10  E-value: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  122 EIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERecypsplNYYNFPKSCCTSVNEVICHG-IPDQRPLQD 200
Cdd:PRK15173 100 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK-------SETHFSRFHLISVGADFSPKlIPSNTKACS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGF-SVVRSYC 279
Cdd:PRK15173 173 GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLpNYNRGHL 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  280 GHGiHRVFHTAPNVPhYAKNSAVGVMAPGHCFTIEpmisvgvqkaetwpddwTAVTADGLYSAQFEQTLLVNETGCEILT 359
Cdd:PRK15173 253 GHG-NGVFLGLEESP-FVSTHATESFTSGMVLSLE-----------------TPYYGYNLGSIMIEDMILINKEGIEFLS 313

                 .
gi 21355531  360 K 360
Cdd:PRK15173 314 K 314
PRK14575 PRK14575
putative peptidase; Provisional
122-360 1.67e-06

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 49.70  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  122 EIEGMRVAGRLGRECLDEGAKAVEVGITTDELDRLVHEAAIERecypsplNYYNFPKSCCTSVNEVICHG-IPDQRPLQD 200
Cdd:PRK14575 183 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSK-------SETHFSRFHLISVGADFSPKlIPSNTKACS 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  201 GDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGF-SVVRSYC 279
Cdd:PRK14575 256 GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLpNYNRGHL 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  280 GHGiHRVFHTAPNVPhYAKNSAVGVMAPGHCFTIEpmisvgvqkaetwpddwTAVTADGLYSAQFEQTLLVNETGCEILT 359
Cdd:PRK14575 336 GHG-NGVFLGLEESP-FVSTHATESFTSGMVLSLE-----------------TPYYGYNLGSIMIEDMILINKEGIEFLS 396

                 .
gi 21355531  360 K 360
Cdd:PRK14575 397 K 397
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
124-320 9.24e-06

Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.


Pssm-ID: 238523 [Multi-domain]  Cd Length: 228  Bit Score: 46.38  E-value: 9.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 124 EGMRVA---GRLGRECLDEGAKAVEVGITTDEldrlvheaAIERECYPSplnyynFPKSCC--------TSVNEVICHGI 192
Cdd:cd01090   6 HGARIAdigGAAVVEAIREGVPEYEVALAGTQ--------AMVREIAKT------FPEVELmdtwtwfqSGINTDGAHNP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531 193 PDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFVGNVSEKHKKLVQVTHEALSKAIEFVRPGEKYRDIGNVIQKYVAPHGF 272
Cdd:cd01090  72 VTNRKVQRGDILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDL 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21355531 273 SVVRSYcGHGihrvfHTAPNVPHYAKNSA--------VGVMAPGHCFTIEPMISVG 320
Cdd:cd01090 152 LRYRTF-GYG-----HSFGVLSHYYGREAglelrediDTVLEPGMVVSMEPMIMLP 201
PRK09795 PRK09795
aminopeptidase; Provisional
104-358 1.17e-04

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 43.77  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  104 SLSEEALRGTKIKvlddEEIEGMRVAGRLGreclDEGAKAVEVGITTDELDRlvhEAAIERECY--PSPLNYYNFPKSCC 181
Cdd:PRK09795 118 SATPDVLRQIKTP----EEVEKIRLACGIA----DRGAEHIRRFIQAGMSER---EIAAELEWFmrQQGAEKASFDTIVA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  182 TSVNEVICHGIPDQRPLQDGDLCNIDVTVYHRGFHGDLNETFFV---GNVSEKHK--KLVQVTHEALSKAIEFVRPGEKY 256
Cdd:PRK09795 187 SGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHPlfNVYQIVLQAQLAAISAIRPGVRC 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355531  257 RDIGNVIQKYVAPHGFSVVRSY-CGHGIHRVFHTAPNVphyaKNSAVGVMAPGHCFTIEPMISVGVQKAetwpddwtavt 335
Cdd:PRK09795 267 QQVDDAARRVITEAGYGDYFGHnTGHAIGIEVHEDPRF----SPRDTTTLQPGMLLTVEPGIYLPGQGG----------- 331
                        250       260
                 ....*....|....*....|...
gi 21355531  336 adglysAQFEQTLLVNETGCEIL 358
Cdd:PRK09795 332 ------VRIEDVVLVTPQGAEVL 348
 
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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