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Conserved domains on  [gi|190194372|ref|NP_694950|]
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purine nucleoside phosphorylase LACC1 isoform 1 [Homo sapiens]

Protein Classification

polyphenol oxidase family protein( domain architecture ID 10495413)

polyphenol oxidase family protein such as peptidoglycan editing factor PgeF involved in the maintenance of bacterial peptide composition

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cu-oxidase_4 pfam02578
Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able ...
195-426 2.03e-82

Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able to oxidize a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms.


:

Pssm-ID: 460601 [Multi-domain]  Cd Length: 232  Bit Score: 252.79  E-value: 2.03e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  195 TTRTGGISYIP--------TlssfnlfssskRRDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIM-----GRKE 261
Cdd:pfam02578   1 TTRLGGVSEGPyaslnlglH-----------VGDDPEAVAENRRRLAAALGLPPERLVWLRQVHGTDVRVVteddaGAAR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  262 PDSYDGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYGCSLEDIVVVLGPSVGPC 341
Cdd:pfam02578  70 EEDADALVTDEPGVALAVLTADCVPVLLADPVGGVVAAAHAGWRGTVAGILEATVEAMEELGGARPEDILAAIGPSIGPC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  342 CFTLPRESAEAFHNLHPACVQLFDSPN-PCIDIRKATRILLEQGGILPQNIqdqnQDLNLCTSCHPDKFFSHVRDGLNFG 420
Cdd:pfam02578 150 CYEVGEEVAEAFAAADPDAAFPATRAGkYLLDLWAANRLQLEAAGVPPENI----EVSGLCTYCEPDRFFSYRRDGGKTG 225

                  ....*.
gi 190194372  421 TQIGFI 426
Cdd:pfam02578 226 RMASLI 231
 
Name Accession Description Interval E-value
Cu-oxidase_4 pfam02578
Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able ...
195-426 2.03e-82

Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able to oxidize a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms.


Pssm-ID: 460601 [Multi-domain]  Cd Length: 232  Bit Score: 252.79  E-value: 2.03e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  195 TTRTGGISYIP--------TlssfnlfssskRRDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIM-----GRKE 261
Cdd:pfam02578   1 TTRLGGVSEGPyaslnlglH-----------VGDDPEAVAENRRRLAAALGLPPERLVWLRQVHGTDVRVVteddaGAAR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  262 PDSYDGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYGCSLEDIVVVLGPSVGPC 341
Cdd:pfam02578  70 EEDADALVTDEPGVALAVLTADCVPVLLADPVGGVVAAAHAGWRGTVAGILEATVEAMEELGGARPEDILAAIGPSIGPC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  342 CFTLPRESAEAFHNLHPACVQLFDSPN-PCIDIRKATRILLEQGGILPQNIqdqnQDLNLCTSCHPDKFFSHVRDGLNFG 420
Cdd:pfam02578 150 CYEVGEEVAEAFAAADPDAAFPATRAGkYLLDLWAANRLQLEAAGVPPENI----EVSGLCTYCEPDRFFSYRRDGGKTG 225

                  ....*.
gi 190194372  421 TQIGFI 426
Cdd:pfam02578 226 RMASLI 231
YfiH cd16833
protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function ...
250-427 3.32e-61

protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function from Shigella flexneri, E. coli, and many similar proteins which collectively are often called DUF152. The structure of YfiH reveals a distant homology to Rho-activating toxins cytotoxic necrotizing factor 1 (CNF1) as well as chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs), all having an invariant Cys-His pair forming a catalytic dyad, and is required by the CNF-1 toxins for deamidation activity.


Pssm-ID: 319354  Cd Length: 185  Bit Score: 196.65  E-value: 3.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 250 HSNDI----WIMGRKEPDSYDGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYgC 325
Cdd:cd16833    9 HGVRVvdvdDAGGGTAIPEADALITNEPGVALAVLTADCVPVLLYDPKGGVIAAAHAGWRGTVAGIVEKTVEAMKELG-S 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 326 SLEDIVVVLGPSVGPCCFTLPRESAEAFHNLHPACVQLFDSPNPCIDIRKATRILLEQGGILPQNIqdqnQDLNLCTSCH 405
Cdd:cd16833   88 DPEDILAAIGPSIGPCCYEVGEEVAEAFPAAFPEAAAFFKPGKYYLDLWAANRLQLLEAGVPEENI----EVSGLCTYCN 163
                        170       180
                 ....*....|....*....|..
gi 190194372 406 PDKFFSHVRDGLNFGTQIGFIS 427
Cdd:cd16833  164 DDRFFSYRRDGGKTGRMAAVIG 185
YfiH COG1496
Copper oxidase (laccase) domain [Inorganic ion transport and metabolism];
187-428 7.88e-60

Copper oxidase (laccase) domain [Inorganic ion transport and metabolism];


Pssm-ID: 441105 [Multi-domain]  Cd Length: 246  Bit Score: 195.01  E-value: 7.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 187 PDIFIHGFTTRTGGISYIP-------TlssfnlfsssKRRDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIMGR 259
Cdd:COG1496    9 PPGVRHGFTTRLGGVSQGPydslnlgL----------HVGDDPEAVAENRRRLAAALGLPPDRLVWLNQVHGTRVVVVDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 260 KEPDSY----DGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYgCSLEDIVVVLG 335
Cdd:COG1496   79 PDPDGAipeaDALVTNEPGVALAVLTADCVPVLFADPEGGVVAAAHAGWRGTVAGILEKTVEAMEALG-ARPEDILAWIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 336 PSVGPCCFTLPRESAEAFHNLHPACVQLFdSPNPC----IDIRKATRILLEQGGIlpQNIqdqnQDLNLCTSCHPDKFFS 411
Cdd:COG1496  158 PAIGPCCYEVGEEVAEAFLAADPDAARAF-RPGAGgkylLDLPGLARLRLLAAGV--PNI----EGGGLCTYCDPDRFFS 230
                        250
                 ....*....|....*..
gi 190194372 412 HVRDGlNFGTQIGFISI 428
Cdd:COG1496  231 YRRDG-KTGRMASLIWL 246
TIGR00726 TIGR00726
YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized ...
220-428 9.46e-30

YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized bacterial proteins and shows no significant similarity to any characterized protein. No completed genome to date has two members. Members of the family have been crystallized but the function is unknown. [Unknown function, General]


Pssm-ID: 273235 [Multi-domain]  Cd Length: 221  Bit Score: 115.18  E-value: 9.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  220 DPKVVVQENLRRLANAAGFnVEKFYRIKTHHSNDIwimgRKEPDSY------DGITTNQRGVTIAALGADCIPIVFADPV 293
Cdd:TIGR00726  18 DNKAFVLANRERLIAYFNL-PNKIVWLKQVHGDRV----LKVTDKDstlpeaDGLITNTPNLVLAVYTADCVPVLFYDRV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  294 KKACGVAHAGWKGTLLGVAMATVNAMIAEyGCSLEDIVVVLGPSVGPCCFTLPRESAEAFHNLHPACVQLFDSPNPC-ID 372
Cdd:TIGR00726  93 GKIVAAVHAGWRGLKNGIIAKTVKMFKKF-GSKPKDLIAVIGPAIGGCCYEVDKEVYEAFRAVLPNASLPFIPDGKYlFD 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 190194372  373 IRKATRILLEQGGIlpqniqdqNQDLN--LCTSCHPDKFFSHVRDGLNFGTQIGFISI 428
Cdd:TIGR00726 172 LRAIARLQLRELGV--------KQIFVsdRCTYTEPETFFSYRRDKTKTGRMASVIWL 221
PRK10723 PRK10723
polyphenol oxidase;
195-416 3.75e-19

polyphenol oxidase;


Pssm-ID: 182677  Cd Length: 243  Bit Score: 86.23  E-value: 3.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 195 TTRTGGISYIPTLSSFNLFSSSkrrDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIMGrKEPDSY--DGITTNQ 272
Cdd:PRK10723  20 STRIGGVSLPPYDSLNLGAHCG---DNPDHVEENRKRLFAAANLPSKPVWLEQVHGTDVLRLTG-EPYASKraDASYSNT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 273 RGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEygcsLEDIVVVLGPSVGPCCFTLPRESAEA 352
Cdd:PRK10723  96 PGTVCAVMTADCLPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVACFAAK----PENILAWLGPAIGPQAFEVGPEVREA 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190194372 353 FHNLHPACVQLFDSPNP--CIDIRKATRILLEQGGIlpQNIQDQNQdlnlCTSCHPDKFFSHVRDG 416
Cdd:PRK10723 172 FMAKDAKASAAFIPHGDkyLADIYQLARQRLANVGV--EQIFGGDR----CTVTENETFFSYRRDG 231
 
Name Accession Description Interval E-value
Cu-oxidase_4 pfam02578
Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able ...
195-426 2.03e-82

Multi-copper polyphenol oxidoreductase laccase; Laccases are multi-copper oxidoreductases able to oxidize a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms.


Pssm-ID: 460601 [Multi-domain]  Cd Length: 232  Bit Score: 252.79  E-value: 2.03e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  195 TTRTGGISYIP--------TlssfnlfssskRRDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIM-----GRKE 261
Cdd:pfam02578   1 TTRLGGVSEGPyaslnlglH-----------VGDDPEAVAENRRRLAAALGLPPERLVWLRQVHGTDVRVVteddaGAAR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  262 PDSYDGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYGCSLEDIVVVLGPSVGPC 341
Cdd:pfam02578  70 EEDADALVTDEPGVALAVLTADCVPVLLADPVGGVVAAAHAGWRGTVAGILEATVEAMEELGGARPEDILAAIGPSIGPC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  342 CFTLPRESAEAFHNLHPACVQLFDSPN-PCIDIRKATRILLEQGGILPQNIqdqnQDLNLCTSCHPDKFFSHVRDGLNFG 420
Cdd:pfam02578 150 CYEVGEEVAEAFAAADPDAAFPATRAGkYLLDLWAANRLQLEAAGVPPENI----EVSGLCTYCEPDRFFSYRRDGGKTG 225

                  ....*.
gi 190194372  421 TQIGFI 426
Cdd:pfam02578 226 RMASLI 231
YfiH cd16833
protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function ...
250-427 3.32e-61

protein of unknown function YfiH; This subfamily contains YfiH, a protein of unknown function from Shigella flexneri, E. coli, and many similar proteins which collectively are often called DUF152. The structure of YfiH reveals a distant homology to Rho-activating toxins cytotoxic necrotizing factor 1 (CNF1) as well as chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs), all having an invariant Cys-His pair forming a catalytic dyad, and is required by the CNF-1 toxins for deamidation activity.


Pssm-ID: 319354  Cd Length: 185  Bit Score: 196.65  E-value: 3.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 250 HSNDI----WIMGRKEPDSYDGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYgC 325
Cdd:cd16833    9 HGVRVvdvdDAGGGTAIPEADALITNEPGVALAVLTADCVPVLLYDPKGGVIAAAHAGWRGTVAGIVEKTVEAMKELG-S 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 326 SLEDIVVVLGPSVGPCCFTLPRESAEAFHNLHPACVQLFDSPNPCIDIRKATRILLEQGGILPQNIqdqnQDLNLCTSCH 405
Cdd:cd16833   88 DPEDILAAIGPSIGPCCYEVGEEVAEAFPAAFPEAAAFFKPGKYYLDLWAANRLQLLEAGVPEENI----EVSGLCTYCN 163
                        170       180
                 ....*....|....*....|..
gi 190194372 406 PDKFFSHVRDGLNFGTQIGFIS 427
Cdd:cd16833  164 DDRFFSYRRDGGKTGRMAAVIG 185
YfiH COG1496
Copper oxidase (laccase) domain [Inorganic ion transport and metabolism];
187-428 7.88e-60

Copper oxidase (laccase) domain [Inorganic ion transport and metabolism];


Pssm-ID: 441105 [Multi-domain]  Cd Length: 246  Bit Score: 195.01  E-value: 7.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 187 PDIFIHGFTTRTGGISYIP-------TlssfnlfsssKRRDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIMGR 259
Cdd:COG1496    9 PPGVRHGFTTRLGGVSQGPydslnlgL----------HVGDDPEAVAENRRRLAAALGLPPDRLVWLNQVHGTRVVVVDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 260 KEPDSY----DGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYgCSLEDIVVVLG 335
Cdd:COG1496   79 PDPDGAipeaDALVTNEPGVALAVLTADCVPVLFADPEGGVVAAAHAGWRGTVAGILEKTVEAMEALG-ARPEDILAWIG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 336 PSVGPCCFTLPRESAEAFHNLHPACVQLFdSPNPC----IDIRKATRILLEQGGIlpQNIqdqnQDLNLCTSCHPDKFFS 411
Cdd:COG1496  158 PAIGPCCYEVGEEVAEAFLAADPDAARAF-RPGAGgkylLDLPGLARLRLLAAGV--PNI----EGGGLCTYCDPDRFFS 230
                        250
                 ....*....|....*..
gi 190194372 412 HVRDGlNFGTQIGFISI 428
Cdd:COG1496  231 YRRDG-KTGRMASLIWL 246
TIGR00726 TIGR00726
YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized ...
220-428 9.46e-30

YfiH family protein; PSI-BLAST converges on members of this family of uncharacterized bacterial proteins and shows no significant similarity to any characterized protein. No completed genome to date has two members. Members of the family have been crystallized but the function is unknown. [Unknown function, General]


Pssm-ID: 273235 [Multi-domain]  Cd Length: 221  Bit Score: 115.18  E-value: 9.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  220 DPKVVVQENLRRLANAAGFnVEKFYRIKTHHSNDIwimgRKEPDSY------DGITTNQRGVTIAALGADCIPIVFADPV 293
Cdd:TIGR00726  18 DNKAFVLANRERLIAYFNL-PNKIVWLKQVHGDRV----LKVTDKDstlpeaDGLITNTPNLVLAVYTADCVPVLFYDRV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372  294 KKACGVAHAGWKGTLLGVAMATVNAMIAEyGCSLEDIVVVLGPSVGPCCFTLPRESAEAFHNLHPACVQLFDSPNPC-ID 372
Cdd:TIGR00726  93 GKIVAAVHAGWRGLKNGIIAKTVKMFKKF-GSKPKDLIAVIGPAIGGCCYEVDKEVYEAFRAVLPNASLPFIPDGKYlFD 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 190194372  373 IRKATRILLEQGGIlpqniqdqNQDLN--LCTSCHPDKFFSHVRDGLNFGTQIGFISI 428
Cdd:TIGR00726 172 LRAIARLQLRELGV--------KQIFVsdRCTYTEPETFFSYRRDKTKTGRMASVIWL 221
PRK10723 PRK10723
polyphenol oxidase;
195-416 3.75e-19

polyphenol oxidase;


Pssm-ID: 182677  Cd Length: 243  Bit Score: 86.23  E-value: 3.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 195 TTRTGGISYIPTLSSFNLFSSSkrrDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIMGrKEPDSY--DGITTNQ 272
Cdd:PRK10723  20 STRIGGVSLPPYDSLNLGAHCG---DNPDHVEENRKRLFAAANLPSKPVWLEQVHGTDVLRLTG-EPYASKraDASYSNT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 273 RGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEygcsLEDIVVVLGPSVGPCCFTLPRESAEA 352
Cdd:PRK10723  96 PGTVCAVMTADCLPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVACFAAK----PENILAWLGPAIGPQAFEVGPEVREA 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190194372 353 FHNLHPACVQLFDSPNP--CIDIRKATRILLEQGGIlpQNIQDQNQdlnlCTSCHPDKFFSHVRDG 416
Cdd:PRK10723 172 FMAKDAKASAAFIPHGDkyLADIYQLARQRLANVGV--EQIFGGDR----CTVTENETFFSYRRDG 231
CNF1_CheD_YfiH-like cd16832
cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and YfiH (DUF152) are distant ...
266-340 1.38e-05

cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and YfiH (DUF152) are distant homologs; This family contains distant homologs that include cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and a protein of unknown function YfiH. CNF-1 along with dermonecrotic toxin (DNT) from Bordetella species, and Burkholderia Lethal Factor 1 (BLF1, also known as BPSL1549) are Rho-activating toxins. The bacterial chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). YfiH, a domain of unknown function, also included in this family reveals a structure with a distant homology between to the CNF1, and CheD, all having an invariant Cys-His pair forming a catalytic dyad that is required by the CNF-1 toxins for deamidation activity.


Pssm-ID: 319353  Cd Length: 145  Bit Score: 44.70  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194372 266 DGITTNQRGVTIAALG-ADCIPIVFADPVKKACGVAHAGWKGTLLGV--------AMATVNAMIAEYGCSLEDIVVVLGP 336
Cdd:cd16832   12 NGIVIKLKPVIITSGNlSGCTTVVARDPGAKYIAKAHTGTTKSLAGFtsttgvdkAVEVLVLLTKEPGASENFEDSLITY 91

                 ....
gi 190194372 337 SVGP 340
Cdd:cd16832   92 SSSE 95
 
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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