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Conserved domains on  [gi|1270019200|gb|ATO85842|]
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adenosine deaminase [Actinoplanes sp. SE50]

Protein Classification

adenosine deaminase family protein( domain architecture ID 10013192)

adenosine deaminase family protein such as adenosine deaminase, which catalyzes the zinc-dependent irreversible hydrolytic deamination of adenosine as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively

CATH:  3.20.20.140
EC:  3.5.4.-
Gene Ontology:  GO:0008270
PubMed:  11223861
SCOP:  4003205

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09358 PRK09358
adenosine deaminase; Provisional
 2-338 1.85e-138

adenosine deaminase; Provisional


:

Pssm-ID: 236480  Cd Length: 340  Bit Score: 396.08  E-value: 1.85e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200   2 SDLTEFITGLPKAELHVHHVGSASPRIVAELAARHEGSSPvPADPAALA---DYFEFRDFAHFIEIYLSVVDLIRDAADV 78
Cdd:PRK09358    1 MNLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALP-ATDVEELPwvrAAYDFRDLQSFLDKYDAGVAVLQTEEDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  79 RLLTYEIGRELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVELAWCFDIPGEAGLPAAEETL-RIA 157
Cdd:PRK09358   80 RRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELeALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 158 LEERPDGLISFGLGGPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHL 237
Cdd:PRK09358  160 ARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 238 AEHGIPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRH 317
Cdd:PRK09358  240 ADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEA 319

                         330       340
                  ....*....|....*....|.
gi 1270019200 318 SFLSPQGRATLLAEIDGYAAG 338
Cdd:PRK09358  320 AFLSEEEKAALLAEVDAWLAA 340
 
Name Accession Description Interval E-value
PRK09358 PRK09358
adenosine deaminase; Provisional
 2-338 1.85e-138

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 396.08  E-value: 1.85e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200   2 SDLTEFITGLPKAELHVHHVGSASPRIVAELAARHEGSSPvPADPAALA---DYFEFRDFAHFIEIYLSVVDLIRDAADV 78
Cdd:PRK09358    1 MNLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALP-ATDVEELPwvrAAYDFRDLQSFLDKYDAGVAVLQTEEDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  79 RLLTYEIGRELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVELAWCFDIPGEAGLPAAEETL-RIA 157
Cdd:PRK09358   80 RRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELeALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 158 LEERPDGLISFGLGGPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHL 237
Cdd:PRK09358  160 ARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 238 AEHGIPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRH 317
Cdd:PRK09358  240 ADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEA 319

                         330       340
                  ....*....|....*....|.
gi 1270019200 318 SFLSPQGRATLLAEIDGYAAG 338
Cdd:PRK09358  320 AFLSEEEKAALLAEVDAWLAA 340
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 12-337 1.38e-137

Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441421  Cd Length: 326  Bit Score: 393.30  E-value: 1.38e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  12 PKAELHVHHVGSASPRIVAELAARHeGSSPVPADPAALADYFEFRDFAHFIEIYLSVVDLIRDAADVRLLTYEIGRELSR 91
Cdd:COG1816     1 PKAELHLHLEGSLRPETLLELAARN-GIDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  92 QRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVELAWCFDIPGEAGLPAAEETLRIALEERPDGLISFGLG 171
Cdd:COG1816    80 DGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRGVVGFGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 172 GPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHGIPLEVCPTSN 251
Cdd:COG1816   160 GDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 252 LRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLSPQGRATLLAE 331
Cdd:COG1816   240 VQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALLAE 319


                  ....*.
gi 1270019200 332 IDGYAA 337
Cdd:COG1816   320 LDAYFA 325
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 10-332 1.04e-115

Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.


Pssm-ID: 238645  Cd Length: 325  Bit Score: 338.02  E-value: 1.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  10 GLPKAELHVHHVGSASPRIVAELAARHegSSPVPADPAALADY----FEFRDFAHFIEIYLSVVDLIRDAADVRLLTYEI 85
Cdd:cd01320     1 NLPKAELHLHLDGSLRPETILELAKKN--GITLPASDVELLELvvaaYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  86 GRELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVElAWCFDIPGEAGLP-AAEETLRIALEERPDG 164
Cdd:cd01320    79 LEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIK-ARLILCGLRHLSPeSAQETLELALKYRDKG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 165 LISFGLGGPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHGIPL 244
Cdd:cd01320   158 VVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 245 EVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLSPQG 324
Cdd:cd01320   238 EVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEE 317


                  ....*...
gi 1270019200 325 RATLLAEI 332
Cdd:cd01320   318 KAELLKRI 325
A_deaminase pfam00962
Adenosine deaminase;
12-335 3.50e-115

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 336.71  E-value: 3.50e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  12 PKAELHVHHVGSASPRIVAELAARHEGSSPVpADPAALADYFE----FRDFAHFIEIYLSVVDLIRDAADVRLLTYEIGR 87
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPA-DFPEALEPLFRkykkERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  88 ELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVE---LAWCFDIPGEAglpAAEETLRIALEERPDG 164
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITvrlIVCAMRHEHPE---CSREIAELAPRYRDQG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 165 LISFGLGGPEIGVPRPQFKPY---FDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHG 241
Cdd:pfam00962 157 IVAFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 242 IPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLS 321
Cdd:pfam00962 237 IPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLP 316

                         330
                  ....*....|....
gi 1270019200 322 PQGRATLLAEIDGY 335
Cdd:pfam00962 317 ADEKRALLDEVDKV 330
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 11-332 8.93e-87

adenosine deaminase; This family includes the experimentally verified adenosine deaminases of mammals and E. coli. Other members of this family are predicted also to be adenosine deaminase, an enzyme of nucleotide degradation. This family is distantly related to AMP deaminase.


Pssm-ID: 273619  Cd Length: 324  Bit Score: 264.22  E-value: 8.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  11 LPKAELHVHHVGSASPRIVAELAARHegSSPVPADPAALADYFE----FRDFAHFIEIYLSVVDLIRDAADVRLLTYEIG 86
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLELAQKN--GIPLPADLQSGEELKEaydkFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  87 RELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVE--LAWCFDipGEAGLPAAEETLRIALEERPDG 164
Cdd:TIGR01430  79 EKAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKsrLILCGM--RHKQPEAAEETLELAKPYKEQT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 165 LISFGLGGPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHGIPL 244
Cdd:TIGR01430 157 IVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 245 EVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLSPQG 324
Cdd:TIGR01430 237 EVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDE 316


                  ....*...
gi 1270019200 325 RATLLAEI 332
Cdd:TIGR01430 317 KKELLAKL 324
 
Name Accession Description Interval E-value
PRK09358 PRK09358
adenosine deaminase; Provisional
 2-338 1.85e-138

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 396.08  E-value: 1.85e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200   2 SDLTEFITGLPKAELHVHHVGSASPRIVAELAARHEGSSPvPADPAALA---DYFEFRDFAHFIEIYLSVVDLIRDAADV 78
Cdd:PRK09358    1 MNLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALP-ATDVEELPwvrAAYDFRDLQSFLDKYDAGVAVLQTEEDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  79 RLLTYEIGRELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVELAWCFDIPGEAGLPAAEETL-RIA 157
Cdd:PRK09358   80 RRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELeALA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 158 LEERPDGLISFGLGGPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHL 237
Cdd:PRK09358  160 ARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 238 AEHGIPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRH 317
Cdd:PRK09358  240 ADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEA 319

                         330       340
                  ....*....|....*....|.
gi 1270019200 318 SFLSPQGRATLLAEIDGYAAG 338
Cdd:PRK09358  320 AFLSEEEKAALLAEVDAWLAA 340
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 12-337 1.38e-137

Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441421  Cd Length: 326  Bit Score: 393.30  E-value: 1.38e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  12 PKAELHVHHVGSASPRIVAELAARHeGSSPVPADPAALADYFEFRDFAHFIEIYLSVVDLIRDAADVRLLTYEIGRELSR 91
Cdd:COG1816     1 PKAELHLHLEGSLRPETLLELAARN-GIDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  92 QRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVELAWCFDIPGEAGLPAAEETLRIALEERPDGLISFGLG 171
Cdd:COG1816    80 DGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRGVVGFGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 172 GPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHGIPLEVCPTSN 251
Cdd:COG1816   160 GDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 252 LRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLSPQGRATLLAE 331
Cdd:COG1816   240 VQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALLAE 319


                  ....*.
gi 1270019200 332 IDGYAA 337
Cdd:COG1816   320 LDAYFA 325
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 10-332 1.04e-115

Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.


Pssm-ID: 238645  Cd Length: 325  Bit Score: 338.02  E-value: 1.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  10 GLPKAELHVHHVGSASPRIVAELAARHegSSPVPADPAALADY----FEFRDFAHFIEIYLSVVDLIRDAADVRLLTYEI 85
Cdd:cd01320     1 NLPKAELHLHLDGSLRPETILELAKKN--GITLPASDVELLELvvaaYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  86 GRELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVElAWCFDIPGEAGLP-AAEETLRIALEERPDG 164
Cdd:cd01320    79 LEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIK-ARLILCGLRHLSPeSAQETLELALKYRDKG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 165 LISFGLGGPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHGIPL 244
Cdd:cd01320   158 VVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 245 EVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLSPQG 324
Cdd:cd01320   238 EVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEE 317


                  ....*...
gi 1270019200 325 RATLLAEI 332
Cdd:cd01320   318 KAELLKRI 325
A_deaminase pfam00962
Adenosine deaminase;
12-335 3.50e-115

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 336.71  E-value: 3.50e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  12 PKAELHVHHVGSASPRIVAELAARHEGSSPVpADPAALADYFE----FRDFAHFIEIYLSVVDLIRDAADVRLLTYEIGR 87
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPA-DFPEALEPLFRkykkERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  88 ELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVE---LAWCFDIPGEAglpAAEETLRIALEERPDG 164
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITvrlIVCAMRHEHPE---CSREIAELAPRYRDQG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 165 LISFGLGGPEIGVPRPQFKPY---FDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHG 241
Cdd:pfam00962 157 IVAFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 242 IPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLS 321
Cdd:pfam00962 237 IPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLP 316

                         330
                  ....*....|....
gi 1270019200 322 PQGRATLLAEIDGY 335
Cdd:pfam00962 317 ADEKRALLDEVDKV 330
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 11-332 8.93e-87

adenosine deaminase; This family includes the experimentally verified adenosine deaminases of mammals and E. coli. Other members of this family are predicted also to be adenosine deaminase, an enzyme of nucleotide degradation. This family is distantly related to AMP deaminase.


Pssm-ID: 273619  Cd Length: 324  Bit Score: 264.22  E-value: 8.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  11 LPKAELHVHHVGSASPRIVAELAARHegSSPVPADPAALADYFE----FRDFAHFIEIYLSVVDLIRDAADVRLLTYEIG 86
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLELAQKN--GIPLPADLQSGEELKEaydkFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  87 RELSRQRVRYAELTVTPYSSVRRGIPAPAFCEAIEDARAGARRDFGVE--LAWCFDipGEAGLPAAEETLRIALEERPDG 164
Cdd:TIGR01430  79 EKAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKsrLILCGM--RHKQPEAAEETLELAKPYKEQT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 165 LISFGLGGPEIGVPRPQFKPYFDKARAAGLHSVPHAGETTGPETIWDAIRDLGAERIGHGIAAAQDERLMAHLAEHGIPL 244
Cdd:TIGR01430 157 IVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 245 EVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLSPQG 324
Cdd:TIGR01430 237 EVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDE 316


                  ....*...
gi 1270019200 325 RATLLAEI 332
Cdd:TIGR01430 317 KKELLAKL 324
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 11-332 3.22e-45

Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway.


Pssm-ID: 238250  Cd Length: 305  Bit Score: 156.35  E-value: 3.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  11 LPKAELHVHHVGSASPRIVAELAARHegsspvpadpaaladyfefrdfahFIEIYLSVVDLIRDAADVRLLTYEIGRELS 90
Cdd:cd00443     1 LPKVELHAHLSGSISPETLLELIKKE------------------------FFEKFLLVHNLLQKGEALARALKEVIEEFA 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  91 RQRVRYAELTVTPY-SSVRRGIPAPAFCEAIEDARAGARRDFG---VELAWCFD--IPGEAGLPAAEETLRIAlEERPDG 164
Cdd:cd00443    57 EDNVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPpikVRLILSVDrrGPYVQNYLVASEILELA-KFLSNY 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 165 LISFGLGGPE--IGVPRPQFKPYFDKAR-AAGLHSVPHAGETTGPETIWDAIrDLGAERIGHGIAAAQDERLMAHLAEHG 241
Cdd:cd00443   136 VVGIDLVGDEskGENPLRDFYSYYEYARrLGLLGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIYLVKLRN 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 242 IPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYAVAAELLALDHAGVADLARAAVRHSFLS 321
Cdd:cd00443   215 IPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLSSFAK 294

                         330
                  ....*....|.
gi 1270019200 322 PQGRATLLAEI 332
Cdd:cd00443   295 DEEKKSLLEVL 305
PTZ00124 PTZ00124
adenosine deaminase; Provisional
 11-328 3.97e-31

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 120.36  E-value: 3.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  11 LPKAELHVHHVGSASPRIVAELAARHEgSSPVPADPAALaDYFEF----RDFAHFIEIYLSVVDLIRDaadvrlltYEIG 86
Cdd:PTZ00124   35 IPKCELHCHLDLCFSVDFFLSCIRKYN-LQPNLSDEEIL-DYYLFakggKSLGEFVEKAIRVADIFND--------YEVI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  87 RELSRQRV--RYAELTV------TP-YSSVRRGIPAPAFCEAI----EDARAGARRDFGVELAWCfdipGEAGLPAA--E 151
Cdd:PTZ00124  105 EDLAKHAVfnKYKEGVVlmefrySPtFVAFKHNLDIDLIHQAIvkgiKEAVELLDHKIEVGLLCI----GDTGHDAApiK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 152 ETLRIALEERPDgLISFGLGGPEIgvprpQFKPY---FDKARAAGLHSVPHAGETTGP---ETIWDAIRDLGAERIGHGI 225
Cdd:PTZ00124  181 ESADFCLKHKAD-FVGFDHAGHEV-----DLKPFkdiFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 226 AAAQDERLMAHLAEHGIPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTSLEREYavaAELLALDHA 305
Cdd:PTZ00124  255 RVAESQELIDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDY---EELYTHLNF 331

                         330       340
                  ....*....|....*....|....*.
gi 1270019200 306 GVADLARA---AVRHSFLSPQGRATL 328
Cdd:PTZ00124  332 TLADFMKMnewALEKSFLDKDIKLKI 357
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 2-331 1.12e-25

Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors with sequence similarty to adenosine deaminase.


Pssm-ID: 238646  Cd Length: 345  Bit Score: 105.05  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200   2 SDLTEFITGLPK-AELHVHHVGSASPRIVAELAarhegsspvpadpaaladyfefrdFAHFIEIYLSVVDLIRDAADVRL 80
Cdd:cd01321    15 STLFKIIQKMPKgALLHVHDTAMVSSDWLIKNA------------------------TYRFEQIFDIIDGLLTYLPIFRD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  81 LTYEIGRELSRQRVRYAELTVT---PYSSVRRGIPAPAFCEAIEDARAGARR---DF-GVELAWCfdIPGEAGLPAAEET 153
Cdd:cd01321    71 YYRRLLEELYEDNVQYVELRSSfspLYDLDGREYDYEETVQLLEEVVEKFKKthpDFiGLKIIYA--TLRNFNDSEIKES 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 154 LRIALEER---PDGLISFGLGGPE-IGVPRPQFKPYFD--KARAAGLHSVPHAGETTGPET-----IWDAIRdLGAERIG 222
Cdd:cd01321   149 MEQCLNLKkkfPDFIAGFDLVGQEdAGRPLLDFLPQLLwfPKQCAEIPFFFHAGETNGDGTetdenLVDALL-LNTKRIG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 223 HGIAAAQDERLMAHLAEHGIPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFG-TSLEREYAVAAELLA 301
Cdd:cd01321   228 HGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGaKGLSHDFYQAFMGLA 307

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1270019200 302 LDHAGVADLARAA---VRHSFLSPQGRATLLAE 331
Cdd:cd01321   308 PADAGLRGLKQLAensIRYSALSDQEKDEAVAK 340
adm_rel TIGR01431
adenosine deaminase-related growth factor; Members of this family have been described as ...
 152-330 2.72e-21

adenosine deaminase-related growth factor; Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates.


Pssm-ID: 273620 [Multi-domain]  Cd Length: 479  Bit Score: 94.48  E-value: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 152 ETLRIALEER---PDGLISFGLGGPE-------------IGVPRPQFKPYFDkaraaglhsvpHAGETTGPET-----IW 210
Cdd:TIGR01431 274 EYIKMAMGLRikyPDFVAGFDLVGQEdtghslldykdalLIPSIGVKLPYFF-----------HAGETNWQGTsvdrnLL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 211 DAIRdLGAERIGHGIAAAQDERLMAHLAEHGIPLEVCPTSNLRTRAVADLARHPITTLAAAGVPFSVNSDDPPMFGTS-L 289
Cdd:TIGR01431 343 DALL-LNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISSDDPAFWGAKgL 421

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1270019200 290 EREYAVAAELLALDHAGVA---DLARAAVRHSFLSPQGRATLLA 330
Cdd:TIGR01431 422 SYDFYEAFMGIAGMKADLRtlkQLALNSIKYSALSEEEKNTAMA 465
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 118-318 1.66e-10

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 60.81  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 118 EAIEDARAGARRDFGVELAWCFDIPGEAGLPAAEET---LRIALEERPDGLISFGLGGPEI--GVPRPQFKPYFDKARAA 192
Cdd:cd01292    66 AAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEallLELLRRGLELGAVGLKLAGPYTatGLSDESLRRVLEEARKL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 193 GLHSVPHAGETTGPETIW----DAIRDLGAERIGHGIAAaqDERLMAHLAEHGIPLEVCPTSNLRTRaVADLARHPITTL 268
Cdd:cd01292   146 GLPVVIHAGELPDPTRALedlvALLRLGGRVVIGHVSHL--DPELLELLKEAGVSLEVCPLSNYLLG-RDGEGAEALRRL 222

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270019200 269 AAAGVPFSVNSDDPPMFGTS-LEREYAVAAELLALDhAGVADLARAAVRHS 318
Cdd:cd01292   223 LELGIRVTLGTDGPPHPLGTdLLALLRLLLKVLRLG-LSLEEALRLATINP 272
AMPD cd01319
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ...
 198-323 2.69e-08

AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway.


Pssm-ID: 238644  Cd Length: 496  Bit Score: 55.07  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 198 PHAGETTGPETIWDAIrdLGAERIGHGIAAAQDERL--MAHLAEhgIPLEVCPTSNlrTRAVADLARHPITTLAAAGVPF 275
Cdd:cd01319   331 PHCGEAGDIDHLASAF--LLAHGISHGINLRKVPVLqyLYYLTQ--IGIAMSPLSN--NSLFLSYEKNPFPEFFKRGLNV 404

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270019200 276 SVNSDDPPMFGTSLE---REYAVAAELLALDHAGVADLARAAVRHSFLSPQ 323
Cdd:cd01319   405 SLSTDDPLQFHFTKEplmEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHS 455
PLN03055 PLN03055
AMP deaminase; Provisional
 198-318 4.54e-06

AMP deaminase; Provisional


Pssm-ID: 178613  Cd Length: 602  Bit Score: 48.32  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 198 PHAGETTGPETIWDAIrdLGAERIGHGIAAAQDERL--MAHLAEhgIPLEVCPTSNlrTRAVADLARHPITTLAAAGVPF 275
Cdd:PLN03055  421 PHAGEAGDIDHLAAAF--LLAHNIAHGNNLRKSPGLqyLYYLAQ--IGLAMSPLSN--NSLFLDYHRNPFPMFFARGLNV 494

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1270019200 276 SVNSDDPPMFGTSLE---REYAVAAELLALDHAGVADLARAAVRHS 318
Cdd:PLN03055  495 SLSTDDPLQIHLTKEplvEEYSIAAQVWKLSSCDLCEIARNSVLQS 540
AMP_deaminase pfam19326
AMP deaminase;
198-323 3.81e-05

AMP deaminase;


Pssm-ID: 437158 [Multi-domain]  Cd Length: 622  Bit Score: 45.53  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 198 PHAGETTGPETIWDAIrdLGAERIGHGIAAAQDERL--MAHLAEhgIPLEVCPTSNlrTRAVADLARHPITTLAAAGVPF 275
Cdd:pfam19326 448 PHCGEAGDIDHLVSAF--LLAHGISHGILLRKSPVLqyLYYLAQ--IGIAMSPLSN--NSLFLEYHKNPFPEFFKRGLNV 521

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270019200 276 SVNSDDPPMFGTSLE---REYAVAAELLALDHAGVADLARAAVRHSFLSPQ 323
Cdd:pfam19326 522 SLSTDDPLQFHFTKEplmEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQ 572
AMP_deaminase TIGR01429
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ...
 190-323 1.50e-04

AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.


Pssm-ID: 273618 [Multi-domain]  Cd Length: 611  Bit Score: 43.68  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200 190 RAAGLHSV---PHAGETTGPETIWDAIrdLGAERIGHGIAAAQDERL--MAHLAEhgIPLEVCPTSNlrTRAVADLARHP 264
Cdd:TIGR01429 432 RERGLNTFllrPHCGEAGSVDHLVSAF--LTSHGINHGILLRKVPVLqyLYYLTQ--IPIAMSPLSN--NSLFLEYSKNP 505

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270019200 265 ITTLAAAGVPFSVNSDDPPMFGTSLE---REYAVAAELLALDHAGVADLARAAVRHSFLSPQ 323
Cdd:TIGR01429 506 LPEYLHKGLNVSLSTDDPLQFHYTKEalmEEYAIAAQVWKLSTCDMCELARNSVLQSGFEHQ 567
PTZ00310 PTZ00310
AMP deaminase; Provisional
 198-318 7.66e-04

AMP deaminase; Provisional


Pssm-ID: 240354 [Multi-domain]  Cd Length: 1453  Bit Score: 41.33  E-value: 7.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270019200  198 PHAGETTGPETIWDAIrdLGAERIGHGIAAAQDERL--MAHLAEHGipLEVCPTSNlrTRAVADLARHPITTLAAAGVPF 275
Cdd:PTZ00310  1114 PHCGESGSMDHLYGAF--LCANSICHGINLRNDPPMqyLYYLAQIG--LHVSPLSN--NALFLAFLENPFPVFFHRGLNV 1187

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1270019200  276 SVNSDDPPMFGTSLE---REYAVAAELLALDHAGVADLARAAVRHS 318
Cdd:PTZ00310  1188 SLSTDDPLMFHQTQEpliEEYSIAARVWGLSLNDLCEIARNSVLQS 1233
 
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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