NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119611320|gb|EAW90914|]
View 

KIAA0859, isoform CRA_d [Homo sapiens]

Protein Classification

eEF1A lysine and N-terminal methyltransferase( domain architecture ID 20705015)

eEF1A lysine and N-terminal methyltransferase is a dual methyltransferase that catalyzes methylation of elongation factor 1-alpha (EEF1A1 and EEF1A2) at two different positions, and is therefore involved in the regulation of mRNA translation

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0016279|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
257-397 1.29e-28

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


:

Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 111.46  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 257 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQS----DRMKVHIADGLDYIAslagggEARPCYDVIMf 332
Cdd:COG0421   43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR------EAEESYDVII- 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119611320 333 dVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLK--DSVLAGLKAVFPLLYV 397
Cdd:COG0421  116 -VDLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 2-64 2.81e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.85  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119611320    2 KECNATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltdeeekTLQQVDRMLAEVGRVL 64
Cdd:pfam13649  37 RERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL-------PDPDLEAALREIARVL 92
 
Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
257-397 1.29e-28

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 111.46  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 257 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQS----DRMKVHIADGLDYIAslagggEARPCYDVIMf 332
Cdd:COG0421   43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR------EAEESYDVII- 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119611320 333 dVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLK--DSVLAGLKAVFPLLYV 397
Cdd:COG0421  116 -VDLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
PRK04457 PRK04457
polyamine aminopropyltransferase;
257-431 1.62e-20

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 90.87  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 257 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVA-TQWFGFSQSDRMKVHIADGLDYIAslagggEARPCYDVIMFD-V 334
Cdd:PRK04457  72 QIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVArNHFELPENGERFEVIEADGAEYIA------VHRHSTDVILVDgF 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 335 DSKDptlgmscPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDlGLKDSVLAGLKAVFP-LLYVRRIEGEVNEILFCQLH 413
Cdd:PRK04457 146 DGEG-------IIDALCTQPFFDDCRNALSSDGIFVVNLWSRD-KRYDRYLERLESSFEgRVLELPAESHGNVAVFAFKS 217

                        170
                 ....*....|....*...
gi 119611320 414 PEQKLATPELLETAQALE 431
Cdd:PRK04457 218 APKELRWDKLRKRAKKLE 235
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 232-393 1.65e-09

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 59.86  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 232 HKAMIAGLALLRNPELLLEIPLallvvgLGGG--SLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFsQSDRMKVHIAD 309
Cdd:NF037959 260 YAAMLDELARLRMGRADFSAFF------IGGGayTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWF-DPASATVLHED 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 310 gldyiASLAGGGEARPCYDVIMFDVdSKDPTLgmscpPPAFVEQSFLQKVKSILTPEGVFILNLV--CRDLGLKDSVLAG 387
Cdd:NF037959 333 -----ARRALRRRPEERFDVIVGDA-FTDIAV-----PAHLVTREFFELVRARLTPDGVYLMNVIdhADRLRALAALVAT 401


                 ....*.
gi 119611320 388 LKAVFP 393
Cdd:NF037959 402 LREVFP 407
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 235-393 3.59e-09

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 56.17  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320  235 MIAGLALLRNPELLLeiplallVVGLGGGSL----PLFVHDhfPKSCIDAVEIDPSMLEVATQWF----GFSQSDRMKVH 306
Cdd:pfam01564   7 MIAHVPLCSHPNPKK-------VLIIGGGDGgvlrEVVKHP--SVEKITLVDIDEKVIDFSKKFLpslaIGFQDPRVKVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320  307 IADGLDYIASLAGGgearpcYDVIMfdVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLKD--SV 384
Cdd:pfam01564  78 IGDGFKFLKDYLNT------FDVII--VDSTDPV----GPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELiiNI 145


                  ....*....
gi 119611320  385 LAGLKAVFP 393
Cdd:pfam01564 146 LKNGKQVFP 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 2-64 2.81e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.85  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119611320    2 KECNATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltdeeekTLQQVDRMLAEVGRVL 64
Cdd:pfam13649  37 RERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL-------PDPDLEAALREIARVL 92
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 6-89 1.00e-02

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 36.51  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320   6 ATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltDEEEKTLQQVDRMLAEVGRVLqgrETEWLFGMDEGRKQLAAS 85
Cdd:COG2226   65 AEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHL--PDPERALAEIARVLKPGGRLV---VVDFSPPDLAELEELLAE 139


                 ....
gi 119611320  86 AGFR 89
Cdd:COG2226  140 AGFE 143
 
Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
257-397 1.29e-28

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 111.46  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 257 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQS----DRMKVHIADGLDYIAslagggEARPCYDVIMf 332
Cdd:COG0421   43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR------EAEESYDVII- 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119611320 333 dVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLK--DSVLAGLKAVFPLLYV 397
Cdd:COG0421  116 -VDLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
PRK04457 PRK04457
polyamine aminopropyltransferase;
257-431 1.62e-20

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 90.87  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 257 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVA-TQWFGFSQSDRMKVHIADGLDYIAslagggEARPCYDVIMFD-V 334
Cdd:PRK04457  72 QIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVArNHFELPENGERFEVIEADGAEYIA------VHRHSTDVILVDgF 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 335 DSKDptlgmscPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDlGLKDSVLAGLKAVFP-LLYVRRIEGEVNEILFCQLH 413
Cdd:PRK04457 146 DGEG-------IIDALCTQPFFDDCRNALSSDGIFVVNLWSRD-KRYDRYLERLESSFEgRVLELPAESHGNVAVFAFKS 217

                        170
                 ....*....|....*...
gi 119611320 414 PEQKLATPELLETAQALE 431
Cdd:PRK04457 218 APKELRWDKLRKRAKKLE 235
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 232-393 1.65e-09

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 59.86  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 232 HKAMIAGLALLRNPELLLEIPLallvvgLGGG--SLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFsQSDRMKVHIAD 309
Cdd:NF037959 260 YAAMLDELARLRMGRADFSAFF------IGGGayTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWF-DPASATVLHED 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 310 gldyiASLAGGGEARPCYDVIMFDVdSKDPTLgmscpPPAFVEQSFLQKVKSILTPEGVFILNLV--CRDLGLKDSVLAG 387
Cdd:NF037959 333 -----ARRALRRRPEERFDVIVGDA-FTDIAV-----PAHLVTREFFELVRARLTPDGVYLMNVIdhADRLRALAALVAT 401


                 ....*.
gi 119611320 388 LKAVFP 393
Cdd:NF037959 402 LREVFP 407
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 235-393 3.59e-09

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 56.17  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320  235 MIAGLALLRNPELLLeiplallVVGLGGGSL----PLFVHDhfPKSCIDAVEIDPSMLEVATQWF----GFSQSDRMKVH 306
Cdd:pfam01564   7 MIAHVPLCSHPNPKK-------VLIIGGGDGgvlrEVVKHP--SVEKITLVDIDEKVIDFSKKFLpslaIGFQDPRVKVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320  307 IADGLDYIASLAGGgearpcYDVIMfdVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLKD--SV 384
Cdd:pfam01564  78 IGDGFKFLKDYLNT------FDVII--VDSTDPV----GPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELiiNI 145


                  ....*....
gi 119611320  385 LAGLKAVFP 393
Cdd:pfam01564 146 LKNGKQVFP 154
PRK00811 PRK00811
polyamine aminopropyltransferase;
278-370 1.78e-08

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 55.55  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 278 IDAVEIDPSMLEVATQWF-----GFSQSDRMKVHIADGLDYIAslagggEARPCYDVIMfdVDSKDPTlGmscppPA--- 349
Cdd:PRK00811 103 ITLVEIDERVVEVCRKYLpeiagGAYDDPRVELVIGDGIKFVA------ETENSFDVII--VDSTDPV-G-----PAegl 168

                         90       100
                 ....*....|....*....|.
gi 119611320 350 FvEQSFLQKVKSILTPEGVFI 370
Cdd:PRK00811 169 F-TKEFYENCKRALKEDGIFV 188
PLN02366 PLN02366
spermidine synthase
 235-368 3.83e-07

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 51.57  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 235 MIAGLAL--LRNPELLLeiplallVVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWF-----GFSQSdRMKVHI 307
Cdd:PLN02366  80 MITHLPLcsIPNPKKVL-------VVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFpdlavGFDDP-RVNLHI 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119611320 308 ADGLDYIASLAGGGearpcYDVIMfdVDSKDPtLGmscPPPAFVEQSFLQKVKSILTPEGV 368
Cdd:PLN02366 152 GDGVEFLKNAPEGT-----YDAII--VDSSDP-VG---PAQELFEKPFFESVARALRPGGV 201
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 278-373 1.53e-06

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 50.25  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 278 IDAVEIDPSMLEVATQWFGFSQ-------SDRMKVHIADGLDYIAslagggEARPCYDVIMFD-VDSKDPTLGmscpppA 349
Cdd:COG4262  313 VTLVDLDPEVTDLAKTNPFLRElnggalnDPRVTVVNADAFQFLR------ETDEKYDVIIVDlPDPSNFSLG------K 380

                         90       100
                 ....*....|....*....|....
gi 119611320 350 FVEQSFLQKVKSILTPEGVFILNL 373
Cdd:COG4262  381 LYSVEFYRLVRRHLAPGGVLVVQA 404
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 258-371 4.68e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 44.75  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320 258 VGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQ-SDRMKVHIADGLDYIASLAGGgearpCYDVIM----- 331
Cdd:COG4123   44 LGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGlEDRITVIHGDLKEFAAELPPG-----SFDLVVsnppy 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119611320 332 FDVDSkdptlGMSCPPP----AFVE-----QSFLQKVKSILTPEGVFIL 371
Cdd:COG4123  119 FKAGS-----GRKSPDEaraiARHEdaltlEDLIRAAARLLKPGGRFAL 162
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 2-64 2.81e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.85  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119611320    2 KECNATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltdeeekTLQQVDRMLAEVGRVL 64
Cdd:pfam13649  37 RERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL-------PDPDLEAALREIARVL 92
PLN03075 PLN03075
nicotianamine synthase; Provisional
 260-330 3.47e-03

nicotianamine synthase; Provisional


Pssm-ID: 178624  Cd Length: 296  Bit Score: 39.27  E-value: 3.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119611320 260 LGGGSLPL----FVHDHFPKSCIDAVEIDPSMLEVATQWFGF--SQSDRMKVHIADGLDYIASLAGggearpcYDVI 330
Cdd:PLN03075 130 VGSGPLPLtsivLAKHHLPTTSFHNFDIDPSANDVARRLVSSdpDLSKRMFFHTADVMDVTESLKE-------YDVV 199
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 6-89 1.00e-02

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 36.51  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119611320   6 ATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltDEEEKTLQQVDRMLAEVGRVLqgrETEWLFGMDEGRKQLAAS 85
Cdd:COG2226   65 AEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHL--PDPERALAEIARVLKPGGRLV---VVDFSPPDLAELEELLAE 139


                 ....
gi 119611320  86 AGFR 89
Cdd:COG2226  140 AGFE 143
 
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