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Conserved domains on  [gi|654931924|ref|WP_028382287|]
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AAA family ATPase [Legionella cherrii]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3896 super family cl43976
Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];
2-189 4.53e-30

Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];


The actual alignment was detected with superfamily member COG3896:

Pssm-ID: 443103  Cd Length: 182  Bit Score: 108.85  E-value: 4.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGMLgdkfaelhpdnPQVCIPNDicyahqyADGTYEIIPGALCSK 81
Cdd:COG3896    7 IIILNGASSSGKSSIARALQELLPEPWLHLSIDTFVDML-----------PPRLLRGI-------DGPGGAIDVGPILRR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  82 LYLTIPNVLKLLAEQGFNIIVDSFITTIDEFKSYKEILESYGVLFVYLDASEATIAQREAARGDRLKGSALHWLKR-FDF 160
Cdd:COG3896   69 LIRGMHRAIAAFARAGNNVIVDDVLLEGAWLQDLLRALSGLPVLFVGVRCPLEELERRERARGDRPIGLARSQAERvHAG 148

                        170       180
                 ....*....|....*....|....*....
gi 654931924 161 QEHcDLCINTEEMNTQQIGDEVFRALETR 189
Cdd:COG3896  149 VIY-DLEVDTSALSPEECAERILARLKAR 176
 
Name Accession Description Interval E-value
COG3896 COG3896
Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];
2-189 4.53e-30

Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];


Pssm-ID: 443103  Cd Length: 182  Bit Score: 108.85  E-value: 4.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGMLgdkfaelhpdnPQVCIPNDicyahqyADGTYEIIPGALCSK 81
Cdd:COG3896    7 IIILNGASSSGKSSIARALQELLPEPWLHLSIDTFVDML-----------PPRLLRGI-------DGPGGAIDVGPILRR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  82 LYLTIPNVLKLLAEQGFNIIVDSFITTIDEFKSYKEILESYGVLFVYLDASEATIAQREAARGDRLKGSALHWLKR-FDF 160
Cdd:COG3896   69 LIRGMHRAIAAFARAGNNVIVDDVLLEGAWLQDLLRALSGLPVLFVGVRCPLEELERRERARGDRPIGLARSQAERvHAG 148

                        170       180
                 ....*....|....*....|....*....
gi 654931924 161 QEHcDLCINTEEMNTQQIGDEVFRALETR 189
Cdd:COG3896  149 VIY-DLEVDTSALSPEECAERILARLKAR 176
CPT cd00227
Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary ...
 2-190 7.77e-17

Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary (C-3) hydroxyl of the antibiotic. Related structurally to shikimate kinase II.


Pssm-ID: 238139  Cd Length: 175  Bit Score: 74.09  E-value: 7.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGMLgdkfaelhpdnPQVCIPNDICYAhqyADGTYEIIPGALCSK 81
Cdd:cd00227    4 IIILNGGSSAGKSSIARALQSVLAEPWLHFGVDSFIEAL-----------PLKCQDAEGGIE---FDGDGGVSPGPEFRL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  82 LYLTIPNVLKLLAEQGFNIIVDSFITTIDEFKSYKEILESYGVLFVYLDASEATIAQREAARGDRLKGSALHWLKRFDFQ 161
Cdd:cd00227   70 LEGAWYEAVAAMARAGANVIADDVFLGRAALQDCWRSFVGLDVLWVGVRCPGEVAEGRETARGDRVPGQARKQARVVHAG 149

                        170       180
                 ....*....|....*....|....*....
gi 654931924 162 EHCDLCINTeemnTQQIGDEVFRALETRI 190
Cdd:cd00227  150 VEYDLEVDT----THKTPIECARAIAARV 174
CPT pfam07931
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ...
 1-187 3.64e-11

Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to chloramphenicol 3-O phosphotransferase (CPT) expressed by Streptomyces venezuelae. Chloramphenicol (Cm) is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group to the C-3 hydroxyl group of Cm, CPT inactivates this potentially lethal metabolite.


Pssm-ID: 400334  Cd Length: 172  Bit Score: 59.00  E-value: 3.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924    1 MIIIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGML-------GDKFaELHPDNPQVCIPndicyahQYADGTYEI 73
Cdd:pfam07931   2 RIILLNGGSSSGKSSIARALQDVLDGPWMHFGVDAFVEAMppkrqnsGGGL-EWSTDGPGPEFP-------LFEAAFYEA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   74 IPGalcsklyltipnvlklLAEQGFNIIVDS-FITTIDEFKSYKEILESYGVLFVYLDASEATIAQREAARGDRLKGSAL 152
Cdd:pfam07931  74 VAA----------------MARAGNNVIADDvILSREWLQDRLQRLLSGLDVLFVGVRCPGEVLERREIERGDRVPGMAA 137

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 654931924  153 HWLKRFDFQEHCDLCINTEEMNTQQIGDEVFRALE 187
Cdd:pfam07931 138 YQAKAVHRGVEYDLEVDTSHQPPEECARAIRSHLE 172
PRK06762 PRK06762
hypothetical protein; Provisional
 2-29 1.81e-03

hypothetical protein; Provisional


Pssm-ID: 235858  Cd Length: 166  Bit Score: 37.26  E-value: 1.81e-03
                         10        20
                 ....*....|....*....|....*...
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWL 29
Cdd:PRK06762   4 LIIIRGNSGSGKTTIAKQLQERLGRGTL 31
 
Name Accession Description Interval E-value
COG3896 COG3896
Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];
2-189 4.53e-30

Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];


Pssm-ID: 443103  Cd Length: 182  Bit Score: 108.85  E-value: 4.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGMLgdkfaelhpdnPQVCIPNDicyahqyADGTYEIIPGALCSK 81
Cdd:COG3896    7 IIILNGASSSGKSSIARALQELLPEPWLHLSIDTFVDML-----------PPRLLRGI-------DGPGGAIDVGPILRR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  82 LYLTIPNVLKLLAEQGFNIIVDSFITTIDEFKSYKEILESYGVLFVYLDASEATIAQREAARGDRLKGSALHWLKR-FDF 160
Cdd:COG3896   69 LIRGMHRAIAAFARAGNNVIVDDVLLEGAWLQDLLRALSGLPVLFVGVRCPLEELERRERARGDRPIGLARSQAERvHAG 148

                        170       180
                 ....*....|....*....|....*....
gi 654931924 161 QEHcDLCINTEEMNTQQIGDEVFRALETR 189
Cdd:COG3896  149 VIY-DLEVDTSALSPEECAERILARLKAR 176
CPT cd00227
Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary ...
 2-190 7.77e-17

Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary (C-3) hydroxyl of the antibiotic. Related structurally to shikimate kinase II.


Pssm-ID: 238139  Cd Length: 175  Bit Score: 74.09  E-value: 7.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGMLgdkfaelhpdnPQVCIPNDICYAhqyADGTYEIIPGALCSK 81
Cdd:cd00227    4 IIILNGGSSAGKSSIARALQSVLAEPWLHFGVDSFIEAL-----------PLKCQDAEGGIE---FDGDGGVSPGPEFRL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  82 LYLTIPNVLKLLAEQGFNIIVDSFITTIDEFKSYKEILESYGVLFVYLDASEATIAQREAARGDRLKGSALHWLKRFDFQ 161
Cdd:cd00227   70 LEGAWYEAVAAMARAGANVIADDVFLGRAALQDCWRSFVGLDVLWVGVRCPGEVAEGRETARGDRVPGQARKQARVVHAG 149

                        170       180
                 ....*....|....*....|....*....
gi 654931924 162 EHCDLCINTeemnTQQIGDEVFRALETRI 190
Cdd:cd00227  150 VEYDLEVDT----THKTPIECARAIAARV 174
CPT pfam07931
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ...
 1-187 3.64e-11

Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to chloramphenicol 3-O phosphotransferase (CPT) expressed by Streptomyces venezuelae. Chloramphenicol (Cm) is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group to the C-3 hydroxyl group of Cm, CPT inactivates this potentially lethal metabolite.


Pssm-ID: 400334  Cd Length: 172  Bit Score: 59.00  E-value: 3.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924    1 MIIIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGML-------GDKFaELHPDNPQVCIPndicyahQYADGTYEI 73
Cdd:pfam07931   2 RIILLNGGSSSGKSSIARALQDVLDGPWMHFGVDAFVEAMppkrqnsGGGL-EWSTDGPGPEFP-------LFEAAFYEA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   74 IPGalcsklyltipnvlklLAEQGFNIIVDS-FITTIDEFKSYKEILESYGVLFVYLDASEATIAQREAARGDRLKGSAL 152
Cdd:pfam07931  74 VAA----------------MARAGNNVIADDvILSREWLQDRLQRLLSGLDVLFVGVRCPGEVLERREIERGDRVPGMAA 137

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 654931924  153 HWLKRFDFQEHCDLCINTEEMNTQQIGDEVFRALE 187
Cdd:pfam07931 138 YQAKAVHRGVEYDLEVDTSHQPPEECARAIRSHLE 172
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
2-163 9.87e-11

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 57.62  E-value: 9.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLG------DGWLSFITDGYLgmlgdkfaELHPDNPQVcipNDICYAHQYAdgtyeiip 75
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERLGavrlrsDVVRKRLFGAGL--------APLERSPEA---TARTYARLLA-------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  76 galcsklyltipnVLKLLAEQGFNIIVDSFITTIDEFKSYKEILESYGV--LFVYLDASEATIAQREAARGDRLKGSALH 153
Cdd:COG0645   62 -------------LARELLAAGRSVILDATFLRRAQREAFRALAEEAGApfVLIWLDAPEEVLRERLEARNAEGGDSDAT 128

                        170
                 ....*....|
gi 654931924 154 WlKRFDFQEH 163
Cdd:COG0645  129 W-EVLERQLA 137
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 3-146 1.08e-09

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 54.24  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924    3 IIVCGTSSSGKSTLCHELQSRLGDGWLSfiTDGYLGMLgdkfaelhpdnpqvcipndicYAHQYADGTYeiiPGALCSKL 82
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVRLS--SDDERKRL---------------------FGEGRPSISY---YTDATDRT 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654931924   83 YLTIPNVLKLLAEQGFNIIVDSFITTIDEFKSYKEILESYGVLF--VYLDASEATIAQREAARGDR 146
Cdd:pfam13671  56 YERLHELARIALRAGRPVILDATNLRRDERARLLALAREYGVPVriVVFEAPEEVLRERLAARARA 121
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 1-145 1.89e-06

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 45.89  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   1 MIIIVCGTSSSGKSTLCHELQSRLGdgwLSFItDgylgmlGDkfaELHpdnPQVCI-------P-------------NDI 60
Cdd:COG3265    2 MVIVVMGVSGSGKSTVGQALAERLG---WPFI-D------GD---DFH---PPANIakmaagiPltdedrapwlealADA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  61 CYAHQYADGTyeiipGAL-CSklyltipnVLKllaeqgfniivdsfittidefKSYKEIL--ESYGVLFVYLDASEATIA 137
Cdd:COG3265   66 IAAHLAAGEG-----AVLaCS--------ALK---------------------RSYRDRLreGNPDVRFVYLDGSRELIA 111


                 ....*...
gi 654931924 138 QREAARGD 145
Cdd:COG3265  112 ERLAARKG 119
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 117-188 2.71e-05

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 42.42  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924 117 EILESYGVLfVYLDASEATIAQREAARGDR--LKGSAL------HWLKRFDF-QEHCDLCINTEEMNTQQIGDEVFRALE 187
Cdd:COG0703   86 ELLKEHGTV-VYLDASPETLLERLRRDDNRplLQGEDPrerleeLLAEREPLyREVADITVDTDGRSPEEVVDEILEALE 164


                 .
gi 654931924 188 T 188
Cdd:COG0703  165 E 165
AAA_18 pfam13238
AAA domain;
3-146 6.49e-05

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.87  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924    3 IIVCGTSSSGKSTLCHELQSRLGDGWLSFITDGYLGMLGDKFAELHPDNPQVcipndiCYAHQYADGTYEIIPgalcskl 82
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETRESKRLD------EDKLDRLLDLLEENA------- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654931924   83 yltipnvlklLAEQGFNIIVDSFITtiDEFKSYKEILEsygvlFVYLDASEATIAQREAARGDR 146
Cdd:pfam13238  68 ----------ALEEGGNLIIDGHLA--ELEPERAKDLV-----GIVLRASPEELLERLEKRGYE 114
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
 2-143 9.84e-04

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.


Pssm-ID: 428926  Cd Length: 192  Bit Score: 38.50  E-value: 9.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924    2 IIIVCGTSSSGKSTLCHELQSRLGDgwlsfiTDGYLGMLGDKFAELHPDNPqvcipndicyAHQYADG-TYEIIPGALCS 80
Cdd:pfam06414  13 AILLGGQPGAGKTELARALLDELGR------QGNVVRIDPDDFRELHPHYR----------ELQAADPkTASEYTQPDAS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654931924   81 KLyltIPNVLKLLAEQGFNIIVDSFITTIDEFKSYKEILES--YGVLFVYLDASEATIAQREAAR 143
Cdd:pfam06414  77 RW---VEKLLQHAIENGYNIILEGTLRSPDVAKKIARALKAagYRVEVAAVAAPPELSWLGVLDR 138
PRK06762 PRK06762
hypothetical protein; Provisional
 2-29 1.81e-03

hypothetical protein; Provisional


Pssm-ID: 235858  Cd Length: 166  Bit Score: 37.26  E-value: 1.81e-03
                         10        20
                 ....*....|....*....|....*...
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWL 29
Cdd:PRK06762   4 LIIIRGNSGSGKTTIAKQLQERLGRGTL 31
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 2-36 3.17e-03

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 36.76  E-value: 3.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 654931924   2 IIIVCGTSSSGKSTLCHELQSRLGDGWLSFIT-DGY 36
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISqDSY 36
PRK04182 PRK04182
cytidylate kinase; Provisional
 1-50 5.53e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 35.94  E-value: 5.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654931924   1 MIIIVCGTSSSGKSTLCHELQSRLGdgwLSFITDGYL--------GM----LGdKFAELHPD 50
Cdd:PRK04182   1 MIITISGPPGSGKTTVARLLAEKLG---LKHVSAGEIfrelakerGMsleeFN-KYAEEDPE 58
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-36 6.18e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 35.97  E-value: 6.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 654931924   1 MIIIVCGTSSSGKSTLCHELQSRLGDGWLSFI-TDGY 36
Cdd:COG0572    8 RIIGIAGPSGSGKTTFARRLAEQLGADKVVVIsLDDY 44
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
1-189 8.78e-03

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 35.57  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924   1 MIIIVCGTSSSGKSTLCHELQSRLGdgwLSFItDGYL--------GMLGDKFAELHPDNPQVcipndicYAHQYADGtye 72
Cdd:COG1102    1 MVITISREPGSGGTTIAKRLAEKLG---LPLY-DGEIlreaakerGLSEEEFEKLDEKAPSL-------LYRDTAEE--- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654931924  73 iipgalcSKLYLTIPNVLKLLAEQGfNIIVDS----FITTidefksykeilESYGVLFVYLDASEATIAQREAARGDRLK 148
Cdd:COG1102   67 -------DEIDRALDKVIRELARKG-NCVIVGrladWILR-----------DRPNVLKVFLTAPLEVRVKRIAEREGISE 127

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 654931924 149 GSALHWLKRFDFQEHC----------------DLCINTEEMNTQQIGDEVFRALETR 189
Cdd:COG1102  128 EEAEKEIKKRDKSRAKyykyyygidwgdpsnyDLVINTSRLGIEEAVDLILAAIEAR 184
 
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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