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Conserved domains on  [gi|2527312827|ref|WP_288338265|]
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ThiF family adenylyltransferase [uncultured Gordonia sp.]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK07877 super family cl35627
Rv1355c family protein;
9-338 1.31e-79

Rv1355c family protein;


The actual alignment was detected with superfamily member PRK07877:

Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 256.84  E-value: 1.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827   9 KDRGRVTQLTA-GHVRIVDTWPdavneyAAMAALDSGLPAIDSDNPDAHTRWIHFPWRATLVRLPDSGMFHRLRTGRNRY 87
Cdd:PRK07877   22 ADRLVLARLRAdPGIEFVDRID------EQLAELRRLRPPPDPELLAEPGRWVYYPWRRTVVHLLGPREFRAVRLDRNRN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  88 LITDTEQQQWAEATIAVAGLSVGASLLHTCVLTG-GRRFRIADCDTLGLTNLNRLTGSVCDLGMEKSLLAHRRMLETDPY 166
Cdd:PRK07877   96 KITAEEQERLGRLRIGVVGLSVGHAIAHTLAAEGlCGELRLADFDTLELSNLNRVPAGVFDLGVNKAVVAARRIAELDPY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 167 LSVDVFSSGVTPSTAREFVSGGEgvpragVVLEEVDDLPTKVELRRQARAAGAPLVMVTDDGDnvIVDVERYDLDPDYPA 246
Cdd:PRK07877  176 LPVEVFTDGLTEDNVDAFLDGLD------VVVEECDSLDVKVLLREAARARRIPVLMATSDRG--LLDVERFDLEPDRPI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 247 FHGSVGDIESwceADLR--DPRHRMRLVGSIVG-DDISSRVSEALAVVGRRIPSWPQLGTASTVAGAVGACVARRIVCGD 323
Cdd:PRK07877  248 LHGLLGDIDA---AKLAglSTKDKVPHVLRILDaEALSARMAASLVEVDQTLSTWPQLASDVVLGAAAVAEAVRRIGLGE 324
                         330
                  ....*....|....*
gi 2527312827 324 TVLSGRARVRIDELL 338
Cdd:PRK07877  325 PLESGRVRVDLDELL 339
 
Name Accession Description Interval E-value
PRK07877 PRK07877
Rv1355c family protein;
9-338 1.31e-79

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 256.84  E-value: 1.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827   9 KDRGRVTQLTA-GHVRIVDTWPdavneyAAMAALDSGLPAIDSDNPDAHTRWIHFPWRATLVRLPDSGMFHRLRTGRNRY 87
Cdd:PRK07877   22 ADRLVLARLRAdPGIEFVDRID------EQLAELRRLRPPPDPELLAEPGRWVYYPWRRTVVHLLGPREFRAVRLDRNRN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  88 LITDTEQQQWAEATIAVAGLSVGASLLHTCVLTG-GRRFRIADCDTLGLTNLNRLTGSVCDLGMEKSLLAHRRMLETDPY 166
Cdd:PRK07877   96 KITAEEQERLGRLRIGVVGLSVGHAIAHTLAAEGlCGELRLADFDTLELSNLNRVPAGVFDLGVNKAVVAARRIAELDPY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 167 LSVDVFSSGVTPSTAREFVSGGEgvpragVVLEEVDDLPTKVELRRQARAAGAPLVMVTDDGDnvIVDVERYDLDPDYPA 246
Cdd:PRK07877  176 LPVEVFTDGLTEDNVDAFLDGLD------VVVEECDSLDVKVLLREAARARRIPVLMATSDRG--LLDVERFDLEPDRPI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 247 FHGSVGDIESwceADLR--DPRHRMRLVGSIVG-DDISSRVSEALAVVGRRIPSWPQLGTASTVAGAVGACVARRIVCGD 323
Cdd:PRK07877  248 LHGLLGDIDA---AKLAglSTKDKVPHVLRILDaEALSARMAASLVEVDQTLSTWPQLASDVVLGAAAVAEAVRRIGLGE 324
                         330
                  ....*....|....*
gi 2527312827 324 TVLSGRARVRIDELL 338
Cdd:PRK07877  325 PLESGRVRVDLDELL 339
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
101-224 3.92e-13

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 65.75  E-value: 3.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 101 TIAVAGLS-VGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTG-SVCDLGMEKSLLAHRRMLETDPYLSVDVFSSGVTP 178
Cdd:cd01483     1 RVLLVGLGgLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLaRQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2527312827 179 STAREFVSGgegvprAGVVLEEVDDLPTKVELRRQARAAGAPLVMV 224
Cdd:cd01483    81 DNLDDFLDG------VDLVIDAIDNIAVRRALNRACKELGIPVIDA 120
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
89-222 5.83e-11

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 61.68  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  89 ITDTEQQQWAEATIAVAGLS-VGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTG-SVCDLGMEKSLLAHRRMLETDPY 166
Cdd:COG0476    17 IGEEGQEKLKAARVLVVGAGgLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILyTEADVGRPKVEAAAERLRALNPD 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2527312827 167 LSVDVFSSGVTPSTAREFVSGgegvprAGVVLEEVDDLPTKVELRRQARAAGAPLV 222
Cdd:COG0476    97 VEVEAIPERLTEENALELLAG------ADLVLDCTDNFATRYLLNDACVKLGIPLV 146
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
94-222 1.60e-09

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 57.65  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  94 QQQWAEATIAVAGL-SVGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTG-SVCDLGMEKSLLAHRRMLETDPYLSVDV 171
Cdd:pfam00899  15 QEKLRNSRVLIVGAgGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLfREADIGKPKAEVAAERLREINPDVEVEA 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2527312827 172 FSSGVTPSTAREFVSGgegvprAGVVLEEVDDLPTKVELRRQARAAGAPLV 222
Cdd:pfam00899  95 YTERLTPENAEELIKS------FDIVVDATDNFAARYLVNDACVKLGKPLI 139
 
Name Accession Description Interval E-value
PRK07877 PRK07877
Rv1355c family protein;
9-338 1.31e-79

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 256.84  E-value: 1.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827   9 KDRGRVTQLTA-GHVRIVDTWPdavneyAAMAALDSGLPAIDSDNPDAHTRWIHFPWRATLVRLPDSGMFHRLRTGRNRY 87
Cdd:PRK07877   22 ADRLVLARLRAdPGIEFVDRID------EQLAELRRLRPPPDPELLAEPGRWVYYPWRRTVVHLLGPREFRAVRLDRNRN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  88 LITDTEQQQWAEATIAVAGLSVGASLLHTCVLTG-GRRFRIADCDTLGLTNLNRLTGSVCDLGMEKSLLAHRRMLETDPY 166
Cdd:PRK07877   96 KITAEEQERLGRLRIGVVGLSVGHAIAHTLAAEGlCGELRLADFDTLELSNLNRVPAGVFDLGVNKAVVAARRIAELDPY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 167 LSVDVFSSGVTPSTAREFVSGGEgvpragVVLEEVDDLPTKVELRRQARAAGAPLVMVTDDGDnvIVDVERYDLDPDYPA 246
Cdd:PRK07877  176 LPVEVFTDGLTEDNVDAFLDGLD------VVVEECDSLDVKVLLREAARARRIPVLMATSDRG--LLDVERFDLEPDRPI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 247 FHGSVGDIESwceADLR--DPRHRMRLVGSIVG-DDISSRVSEALAVVGRRIPSWPQLGTASTVAGAVGACVARRIVCGD 323
Cdd:PRK07877  248 LHGLLGDIDA---AKLAglSTKDKVPHVLRILDaEALSARMAASLVEVDQTLSTWPQLASDVVLGAAAVAEAVRRIGLGE 324
                         330
                  ....*....|....*
gi 2527312827 324 TVLSGRARVRIDELL 338
Cdd:PRK07877  325 PLESGRVRVDLDELL 339
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
101-224 3.92e-13

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 65.75  E-value: 3.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 101 TIAVAGLS-VGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTG-SVCDLGMEKSLLAHRRMLETDPYLSVDVFSSGVTP 178
Cdd:cd01483     1 RVLLVGLGgLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLaRQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2527312827 179 STAREFVSGgegvprAGVVLEEVDDLPTKVELRRQARAAGAPLVMV 224
Cdd:cd01483    81 DNLDDFLDG------VDLVIDAIDNIAVRRALNRACKELGIPVIDA 120
PRK14851 PRK14851
hypothetical protein; Provisional
84-222 6.77e-12

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 66.42  E-value: 6.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  84 RNRYLITDTEQQQWAEATIAVAGLS-VGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTGS-VCDLGMEKSLLAHRRML 161
Cdd:PRK14851   28 RNIGLFTPGEQERLAEAKVAIPGMGgVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGArVPSFGRPKLAVMKEQAL 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527312827 162 ETDPYLSVDVFSSGVTPSTAREFVSGgegvprAGVVLEEVDDLptKVELRRQ----ARAAGAPLV 222
Cdd:PRK14851  108 SINPFLEITPFPAGINADNMDAFLDG------VDVVLDGLDFF--QFEIRRTlfnmAREKGIPVI 164
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
89-222 5.83e-11

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 61.68  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  89 ITDTEQQQWAEATIAVAGLS-VGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTG-SVCDLGMEKSLLAHRRMLETDPY 166
Cdd:COG0476    17 IGEEGQEKLKAARVLVVGAGgLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILyTEADVGRPKVEAAAERLRALNPD 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2527312827 167 LSVDVFSSGVTPSTAREFVSGgegvprAGVVLEEVDDLPTKVELRRQARAAGAPLV 222
Cdd:COG0476    97 VEVEAIPERLTEENALELLAG------ADLVLDCTDNFATRYLLNDACVKLGIPLV 146
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
94-222 1.60e-09

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 57.65  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  94 QQQWAEATIAVAGL-SVGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTG-SVCDLGMEKSLLAHRRMLETDPYLSVDV 171
Cdd:pfam00899  15 QEKLRNSRVLIVGAgGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLfREADIGKPKAEVAAERLREINPDVEVEA 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2527312827 172 FSSGVTPSTAREFVSGgegvprAGVVLEEVDDLPTKVELRRQARAAGAPLV 222
Cdd:pfam00899  95 YTERLTPENAEELIKS------FDIVVDATDNFAARYLVNDACVKLGKPLI 139
PRK08223 PRK08223
hypothetical protein; Validated
84-187 1.19e-08

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 55.46  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  84 RNRYLITDTEQQQWAEATIAVAGL-SVGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTGSVCD-LGMEKSLLAHRRML 161
Cdd:PRK08223   12 RNLGWITPTEQQRLRNSRVAIAGLgGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMStLGRPKAEVLAEMVR 91
                          90       100
                  ....*....|....*....|....*.
gi 2527312827 162 ETDPYLSVDVFSSGVTPSTAREFVSG 187
Cdd:PRK08223   92 DINPELEIRAFPEGIGKENADAFLDG 117
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
98-225 1.38e-07

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 51.45  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  98 AEATIAVAGL-SVGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTGSVC-DLGMEKSLLAHRRMLETDPYLSVDVFSSG 175
Cdd:cd00755    10 RNAHVAVVGLgGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLsTVGKPKVEVMAERIRDINPECEVDAVEEF 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2527312827 176 VTPSTAREFVSGGegvprAGVVLEEVDDLPTKVELRRQARAAGAPLVMVT 225
Cdd:cd00755    90 LTPDNSEDLLGGD-----PDFVVDAIDSIRAKVALIAYCRKRKIPVISSM 134
PRK14852 PRK14852
hypothetical protein; Provisional
68-185 1.34e-06

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 50.08  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827  68 LVRLPDSGMFHRLRTGRNRYLITDTEQQQWAEATIAVAGLS-VGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTG-SV 145
Cdd:PRK14852  301 MLKLETRDAYTDIAFSRNLGLVDYAGQRRLLRSRVAIAGLGgVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGaSI 380
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2527312827 146 CDLGMEKSLLAHRRMLETDPYLSVDVFSSGVTPSTAREFV 185
Cdd:PRK14852  381 ASFGRGKLDVMTERALSVNPFLDIRSFPEGVAAETIDAFL 420
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
100-224 1.70e-04

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 42.15  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 100 ATIAVAGL----SVGASLLhtcVLTGGRRFRIADCDTLGLTNLNRLTGSVCDLGMEKSLLAHRRMLETDPYLSVDVFSSG 175
Cdd:PRK08644   29 AKVGIAGAgglgSNIAVAL---ARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEK 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2527312827 176 VTPSTAREFVSGGEgvpragVVLEEVDDLPTKVELRRQA-RAAGAPLVMV 224
Cdd:PRK08644  106 IDEDNIEELFKDCD------IVVEAFDNAETKAMLVETVlEHPGKKLVAA 149
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
101-223 2.80e-04

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 41.21  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527312827 101 TIAVAGLS-VGASLLHTCVLTGGRRFRIADCDTLGLTNLNRLTGSVCDLGMEKSLLAHRRMLETDPYLSVDVFSSGVTPS 179
Cdd:cd01487     1 KVGIAGAGgLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDEN 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2527312827 180 TAREFVSGGEgvpragVVLEEVDDLPTKVELRRQAR-AAGAPLVM 223
Cdd:cd01487    81 NLEGLFGDCD------IVVEAFDNAETKAMLAESLLgNKNKPVVC 119
 
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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