NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1693982895|gb|TPR89102|]
View 

alpha/beta hydrolase [Acinetobacter baumannii]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
69-270 1.18e-62

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


:

Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 196.66  E-value: 1.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  69 ILYLHGGGYVVGSSKSHAKLAAQIGHVAQAQVWLPEYRLAPEHPSPAAIEDIIAVYKTLLT----YGQDPKKLVIAGDSA 144
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEqaaeLGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 145 GGGLSLSTVIALRDAGLPLPAALVLLSPWVDL-SLSGNTIKTHAAQDAMLSEDWLTWCAKNYCGQKSATDPTCSPLYA-D 222
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLrTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1693982895 223 LTGLPPVLIHVGTEEVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFQ 270
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
69-270 1.18e-62

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 196.66  E-value: 1.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  69 ILYLHGGGYVVGSSKSHAKLAAQIGHVAQAQVWLPEYRLAPEHPSPAAIEDIIAVYKTLLT----YGQDPKKLVIAGDSA 144
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEqaaeLGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 145 GGGLSLSTVIALRDAGLPLPAALVLLSPWVDL-SLSGNTIKTHAAQDAMLSEDWLTWCAKNYCGQKSATDPTCSPLYA-D 222
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLrTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1693982895 223 LTGLPPVLIHVGTEEVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFQ 270
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
58-295 4.88e-55

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 177.37  E-value: 4.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  58 IRPKTIKSGLG-ILYLHGGGYVVGSSKSHAKLAAQIGHVAQAQVWLPEYRLAPEHPSPAAIEDIIAVYKTLL----TYGQ 132
Cdd:COG0657     4 YRPAGAKGPLPvVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRanaaELGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 133 DPKKLVIAGDSAGGGLSLSTVIALRDAGLPLPAALVLLSPWVDLSLsgntikthaaqdamlsedwltwcaknycgqksat 212
Cdd:COG0657    84 DPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTA---------------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 213 dptcSPLYADLTGLPPVLIHVGTEEVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFQFHAGiLKESNDSIERIRQFIDK 292
Cdd:COG0657   130 ----SPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAG-LPEARAALAEIAAFLRR 204

                  ...
gi 1693982895 293 HTE 295
Cdd:COG0657   205 ALA 207
PRK10162 PRK10162
acetyl esterase;
50-289 1.08e-24

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 100.95  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  50 IAQVPTLHIRPKTiKSGLGILYLHGGGYVVGSSKSHAKLAAQIGHVAQAQVWLPEYRLAPEHPSPAAIEDIIAVYKTLLT 129
Cdd:PRK10162   66 YGQVETRLYYPQP-DSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQ 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 130 ----YGQDPKKLVIAGDSAGGGLSLSTVIALRDAGLPLPAALVLL--SPWVDLSLSGNTIKTHAAQDAMLSEDWLTWcak 203
Cdd:PRK10162  145 haedYGINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKVAGVLlwYGLYGLRDSVSRRLLGGVWDGLTQQDLQMY--- 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 204 nycGQKSATDPTC--SPLYA----DLT-GLPPVLIHVGTEEVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFQFHAGIL 276
Cdd:PRK10162  222 ---EEAYLSNDADreSPYYClfnnDLTrDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMM 298
                         250
                  ....*....|...
gi 1693982895 277 KESNDSIERIRQF 289
Cdd:PRK10162  299 DTADDALRDGAQF 311
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
69-270 1.18e-62

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 196.66  E-value: 1.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  69 ILYLHGGGYVVGSSKSHAKLAAQIGHVAQAQVWLPEYRLAPEHPSPAAIEDIIAVYKTLLT----YGQDPKKLVIAGDSA 144
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEqaaeLGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 145 GGGLSLSTVIALRDAGLPLPAALVLLSPWVDL-SLSGNTIKTHAAQDAMLSEDWLTWCAKNYCGQKSATDPTCSPLYA-D 222
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLrTESPSYLAREFADGPLLTRAAMDWFWRLYLPGADRDDPLASPLFAsD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1693982895 223 LTGLPPVLIHVGTEEVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFQ 270
Cdd:pfam07859 161 LSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
58-295 4.88e-55

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 177.37  E-value: 4.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  58 IRPKTIKSGLG-ILYLHGGGYVVGSSKSHAKLAAQIGHVAQAQVWLPEYRLAPEHPSPAAIEDIIAVYKTLL----TYGQ 132
Cdd:COG0657     4 YRPAGAKGPLPvVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRanaaELGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 133 DPKKLVIAGDSAGGGLSLSTVIALRDAGLPLPAALVLLSPWVDLSLsgntikthaaqdamlsedwltwcaknycgqksat 212
Cdd:COG0657    84 DPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTA---------------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 213 dptcSPLYADLTGLPPVLIHVGTEEVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFQFHAGiLKESNDSIERIRQFIDK 292
Cdd:COG0657   130 ----SPLRADLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAG-LPEARAALAEIAAFLRR 204

                  ...
gi 1693982895 293 HTE 295
Cdd:COG0657   205 ALA 207
PRK10162 PRK10162
acetyl esterase;
50-289 1.08e-24

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 100.95  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  50 IAQVPTLHIRPKTiKSGLGILYLHGGGYVVGSSKSHAKLAAQIGHVAQAQVWLPEYRLAPEHPSPAAIEDIIAVYKTLLT 129
Cdd:PRK10162   66 YGQVETRLYYPQP-DSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQ 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 130 ----YGQDPKKLVIAGDSAGGGLSLSTVIALRDAGLPLPAALVLL--SPWVDLSLSGNTIKTHAAQDAMLSEDWLTWcak 203
Cdd:PRK10162  145 haedYGINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKVAGVLlwYGLYGLRDSVSRRLLGGVWDGLTQQDLQMY--- 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 204 nycGQKSATDPTC--SPLYA----DLT-GLPPVLIHVGTEEVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFQFHAGIL 276
Cdd:PRK10162  222 ---EEAYLSNDADreSPYYClfnnDLTrDVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMM 298
                         250
                  ....*....|...
gi 1693982895 277 KESNDSIERIRQF 289
Cdd:PRK10162  299 DTADDALRDGAQF 311
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
69-150 3.22e-10

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 58.73  E-value: 3.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  69 ILYLHGGGYVVGSSKSHAKLAAQIGH-VAQAQ--VWLPEYRLAPEHPSPAAIED----IIAVYKTLLTYGQDPKKLVIAG 141
Cdd:pfam20434  16 VIWIHGGGWNSGDKEADMGFMTNTVKaLLKAGyaVASINYRLSTDAKFPAQIQDvkaaIRFLRANAAKYGIDTNKIALMG 95

                  ....*....
gi 1693982895 142 DSAGGGLSL 150
Cdd:pfam20434  96 FSAGGHLAL 104
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
52-293 6.99e-10

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 58.10  E-value: 6.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  52 QVPTLHIRPKTIKSGLGILYLHGGGYVVGSSKSH-AKLAAQIGHVaqaqVWLPEYR---LAPEHPSPAAIEDIIAVYKTL 127
Cdd:COG1506     9 TLPGWLYLPADGKKYPVVVYVHGGPGSRDDSFLPlAQALASRGYA----VLAPDYRgygESAGDWGGDEVDDVLAAIDYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 128 LTYGQ-DPKKLVIAGDSAGGGLSLstVIALRD-----AGlplpaalVLLSPWVDLSLSGNTIKTHAAQDAMLSEDWLTWC 201
Cdd:COG1506    85 AARPYvDPDRIGIYGHSYGGYMAL--LAAARHpdrfkAA-------VALAGVSDLRSYYGTTREYTERLMGGPWEDPEAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 202 AKNycgqksatdptcSPL-YAD-LTGlpPVLIHVGTEE--VLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVFqfhagILK 277
Cdd:COG1506   156 AAR------------SPLaYADkLKT--PLLLIHGEADdrVPPEQAERLYEALKKAGKPVELLVYPGEGHGF-----SGA 216
                         250
                  ....*....|....*.
gi 1693982895 278 ESNDSIERIRQFIDKH 293
Cdd:COG1506   217 GAPDYLERILDFLDRH 232
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
69-289 9.01e-07

Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.


Pssm-ID: 313549  Cd Length: 374  Bit Score: 49.83  E-value: 9.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  69 ILYLHGGGYVVGSSKSHAKLAAQIG-HVAQAQVWLPEYRLAPEHPS----PAAIEDIIAVYKtLLTYGQDPKKLVIAGDS 143
Cdd:pfam10340 125 LLYYHGGGFALKLIPVTLVFLNNLGkYFPDMAILVSDYTVTANCPQsytyPLQVLQCLAVYD-YLTLTKGCKNVTLMGDS 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 144 AGGGLSLSTVIALRDAGLPLP-AALVLLSPWVDLSLSGNTIKTHAAQDA---MLSEDWLTWCAKNYCGQKsatDPTCSPL 219
Cdd:pfam10340 204 AGGNLVLNILLYLHKCNKVVLpKKAIAISPWLNLTDRNEKEKEYMKANDkldGLCYKGLNMFGKLYVPNV---EPEESLF 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 220 YADLTGLP---------------PVLIHVGTEEVLLDDAKRLAEQ-----TEKYGIPTNLRVYDQVGH---VFQFHAGIL 276
Cdd:pfam10340 281 TDPFVNIEmnfdietwskilekcKLLITYGDDEILSDQIKSFIDKiselkAYNHFTPNNVLIDKQGIHigpILPYMTNLD 360
                         250
                  ....*....|....
gi 1693982895 277 KESN-DSIERIRQF 289
Cdd:pfam10340 361 KWSKkFSVKSILTF 374
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
51-269 8.61e-05

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.03  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  51 AQVPTLHIRPKTIKSGLGILYLHGGGYVVGSSKSHAKLAAQIGHVA--------QAQVWLPE--YRLAPEHPSPAAIEDI 120
Cdd:COG0412    14 VTLPGYLARPAGGGPRPGVVVLHEIFGLNPHIRDVARRLAAAGYVVlapdlygrGGPGDDPDeaRALMGALDPELLAADL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 121 IAVYKTLLTYGQ-DPKKLVIAGDSAGGGLSLstvialrdaglplpaalvllspwvDLSLSGNTIKTHAAqdamlsedwlt 199
Cdd:COG0412    94 RAALDWLKAQPEvDAGRVGVVGFCFGGGLAL------------------------LAAARGPDLAAAVS----------- 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693982895 200 wcaknYCGqkSATDPTCSPLYADLTGlpPVLIHVGTE--EVLLDDAKRLAEQTEKYGIPTNLRVYDQVGHVF 269
Cdd:COG0412   139 -----FYG--GLPADDLLDLAARIKA--PVLLLYGEKdpLVPPEQVAALEAALAAAGVDVELHVYPGAGHGF 201
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
117-293 2.15e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 38.75  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 117 IEDIIAVYKTLLTYGQ-DPKKLVIAGDSAGGGLSLSTV----------IAlrdaglplpaalvlLSPWVDLslsgntIKT 185
Cdd:pfam00326  45 FDDFIAAAEYLIEQGYtDPDRLAIWGGSYGGYLTGAALnqrpdlfkaaVA--------------HVPVVDW------LAY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 186 HAAQDAMLSEDWLTWCA-----KNYCGQKSATDPTCSPLYadltglPPVLIHVGTEE--VLLDDAKRLAEQTEKYGIPTN 258
Cdd:pfam00326 105 MSDTSLPFTERYMEWGNpwdneEGYDYLSPYSPADNVKVY------PPLLLIHGLLDdrVPPWQSLKLVAALQRKGVPFL 178
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1693982895 259 LRVYDQVGHVFQFHagilkesNDSIERIRQ---FIDKH 293
Cdd:pfam00326 179 LLIFPDEGHGIGKP-------RNKVEEYARelaFLLEY 209
YpfH COG0400
Predicted esterase [General function prediction only];
69-293 8.49e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 36.81  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895  69 ILYLHGGGyvvGSSKSHAKLAAQIGhvaqaqvwLPEYR-LAPEHPSP------------------------AAIEDIIAV 123
Cdd:COG0400     8 VVLLHGYG---GDEEDLLPLAPELA--------LPGAAvLAPRAPVPegpggrawfdlsflegredeeglaAAAEALAAF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 124 YKTLL-TYGQDPKKLVIAGDSAGGGLSLSTVIALRD--AGLplpaalvllspwvdLSLSGntikthaaqdaMLsedwltw 200
Cdd:COG0400    77 IDELEaRYGIDPERIVLAGFSQGAAMALSLALRRPEllAGV--------------VALSG-----------YL------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693982895 201 caknycgqksATDPTCSPLYADLTGlPPVLIHVGTE-EVL-LDDAKRLAEQTEKYGIPTNLRVYDqVGHvfqfhaGIlke 278
Cdd:COG0400   125 ----------PGEEALPAPEAALAG-TPVFLAHGTQdPVIpVERAREAAEALEAAGADVTYREYP-GGH------EI--- 183
                         250
                  ....*....|....*
gi 1693982895 279 SNDSIERIRQFIDKH 293
Cdd:COG0400   184 SPEELADARAWLAER 198
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH