|
Name |
Accession |
Description |
Interval |
E-value |
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
158-407 |
3.03e-21 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; :
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 93.30 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 158 WEAYDPNGDRWLRVPKMTFNEC--FMcsdkeSLAVGTELLVFG-------KEIMSHVIYRYSILTNTWTSGMQMNVPRCL 228
Cdd:COG3055 40 FEVYDPATNTWSELAPLPGPPRhhAA-----AVAQDGKLYVFGgftganpSSTPLNDVYVYDPATNTWTKLAPMPTPRGG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 229 FGSASLGEIAVIAGGCDPRGRiLSSAELYNSETGEWTVIPSMNKARKMCSSVFM-DGNFYCIGGIGEGNSkmllcgevyd 307
Cdd:COG3055 115 ATALLLDGKIYVVGGWDDGGN-VAWVEVYDPATGTWTQLAPLPTPRDHLAAAVLpDGKILVIGGRNGSGF---------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 308 lkKKTWTLIPNMLPERSSGGggdqakeiaaataaseapplVAVVKDELYAA---NYAQQEVKKYDKRLNVWNKVGNLPEr 384
Cdd:COG3055 184 --SNTWTTLAPLPTARAGHA--------------------AAVLGGKILVFggeSGFSDEVEAYDPATNTWTALGELPT- 240
|
250 260
....*....|....*....|...
gi 30699022 385 assmNGWGMAFRACGDQLVVVGG 407
Cdd:COG3055 241 ----PRHGHAAVLTDGKVYVIGG 259
|
|
| F-box_SF super family |
cl45894 |
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ... |
105-139 |
2.91e-04 |
|
F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures. The actual alignment was detected with superfamily member cd22152:
Pssm-ID: 459239 Cd Length: 45 Bit Score: 38.32 E-value: 2.91e-04
10 20 30
....*....|....*....|....*....|....*
gi 30699022 105 LNCLAHCSLSDFGSIASTNRTFRSLIKDSELYRLR 139
Cdd:cd22152 11 LQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
158-407 |
3.03e-21 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 93.30 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 158 WEAYDPNGDRWLRVPKMTFNEC--FMcsdkeSLAVGTELLVFG-------KEIMSHVIYRYSILTNTWTSGMQMNVPRCL 228
Cdd:COG3055 40 FEVYDPATNTWSELAPLPGPPRhhAA-----AVAQDGKLYVFGgftganpSSTPLNDVYVYDPATNTWTKLAPMPTPRGG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 229 FGSASLGEIAVIAGGCDPRGRiLSSAELYNSETGEWTVIPSMNKARKMCSSVFM-DGNFYCIGGIGEGNSkmllcgevyd 307
Cdd:COG3055 115 ATALLLDGKIYVVGGWDDGGN-VAWVEVYDPATGTWTQLAPLPTPRDHLAAAVLpDGKILVIGGRNGSGF---------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 308 lkKKTWTLIPNMLPERSSGGggdqakeiaaataaseapplVAVVKDELYAA---NYAQQEVKKYDKRLNVWNKVGNLPEr 384
Cdd:COG3055 184 --SNTWTTLAPLPTARAGHA--------------------AAVLGGKILVFggeSGFSDEVEAYDPATNTWTALGELPT- 240
|
250 260
....*....|....*....|...
gi 30699022 385 assmNGWGMAFRACGDQLVVVGG 407
Cdd:COG3055 241 ----PRHGHAAVLTDGKVYVIGG 259
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
226-407 |
5.53e-12 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 67.49 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 226 RCLFGSASLGEIAVIAGGCDPRGRILSSAELYNSETGEWTVIPSMNKARKMCSSVFMDGNFYCIGGIGEGNSkmLLCGEV 305
Cdd:PHA03098 285 VYCFGSVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSIS--LNTVES 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 306 YDLKKKTWTLIPNMLPERSSGGggdqakeiaaataaseapplVAVVKDELYAA------NYAQQEVKKYDKRLNVWNKVG 379
Cdd:PHA03098 363 WKPGESKWREEPPLIFPRYNPC--------------------VVNVNNLIYVIggisknDELLKTVECFSLNTNKWSKGS 422
|
170 180
....*....|....*....|....*...
gi 30699022 380 NLPeraSSMNGWGMAFRacGDQLVVVGG 407
Cdd:PHA03098 423 PLP---ISHYGGCAIYH--DGKIYVIGG 445
|
|
| Kelch |
smart00612 |
Kelch domain; |
240-284 |
5.89e-08 |
|
Kelch domain;
Pssm-ID: 128874 [Multi-domain] Cd Length: 47 Bit Score: 48.71 E-value: 5.89e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 30699022 240 IAGGCDPrGRILSSAELYNSETGEWTVIPSMNKARKMCSSVFMDG 284
Cdd:smart00612 4 VVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
|
|
| Kelch_1 |
pfam01344 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
225-271 |
6.61e-08 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
Pssm-ID: 396078 [Multi-domain] Cd Length: 46 Bit Score: 48.76 E-value: 6.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30699022 225 PRCLFGSASLGEIAVIAGGCDpRGRILSSAELYNSETGEWTVIPSMN 271
Cdd:pfam01344 1 RRSGAGVVVVGGKIYVIGGFD-GNQSLNSVEVYDPETNTWSKLPSMP 46
|
|
| F-box_AtAFR-like |
cd22152 |
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ... |
105-139 |
2.91e-04 |
|
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and similar proteins; AtAFR, also called SKP1-interacting partner 29 (AtSKIP29), or F-box protein AFR, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It is part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyl elongation in response to red and far-red light exposure. This subfamily also includes many other Arabidopsis thaliana SKP1-interacting partner proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 438923 Cd Length: 45 Bit Score: 38.32 E-value: 2.91e-04
10 20 30
....*....|....*....|....*....|....*
gi 30699022 105 LNCLAHCSLSDFGSIASTNRTFRSLIKDSELYRLR 139
Cdd:cd22152 11 LQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
158-407 |
3.03e-21 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 93.30 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 158 WEAYDPNGDRWLRVPKMTFNEC--FMcsdkeSLAVGTELLVFG-------KEIMSHVIYRYSILTNTWTSGMQMNVPRCL 228
Cdd:COG3055 40 FEVYDPATNTWSELAPLPGPPRhhAA-----AVAQDGKLYVFGgftganpSSTPLNDVYVYDPATNTWTKLAPMPTPRGG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 229 FGSASLGEIAVIAGGCDPRGRiLSSAELYNSETGEWTVIPSMNKARKMCSSVFM-DGNFYCIGGIGEGNSkmllcgevyd 307
Cdd:COG3055 115 ATALLLDGKIYVVGGWDDGGN-VAWVEVYDPATGTWTQLAPLPTPRDHLAAAVLpDGKILVIGGRNGSGF---------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 308 lkKKTWTLIPNMLPERSSGGggdqakeiaaataaseapplVAVVKDELYAA---NYAQQEVKKYDKRLNVWNKVGNLPEr 384
Cdd:COG3055 184 --SNTWTTLAPLPTARAGHA--------------------AAVLGGKILVFggeSGFSDEVEAYDPATNTWTALGELPT- 240
|
250 260
....*....|....*....|...
gi 30699022 385 assmNGWGMAFRACGDQLVVVGG 407
Cdd:COG3055 241 ----PRHGHAAVLTDGKVYVIGG 259
|
|
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
215-407 |
1.95e-17 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 82.13 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 215 TWTSGMQMNVPRCLFGSASLGEIAVIAGGCDPrGRILSSAELYNSETGEWTVIPSMNKARKMCS-SVFMDGNFYCIGGIG 293
Cdd:COG3055 2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSG-GSASNSFEVYDPATNTWSELAPLPGPPRHHAaAVAQDGKLYVFGGFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 294 EGNSKMLLC--GEVYDLKKKTWTLIPNMLPERSSGGggdqakeiaaataaseapplVAVVKDELYAA-----NYAQQEVK 366
Cdd:COG3055 81 GANPSSTPLndVYVYDPATNTWTKLAPMPTPRGGAT--------------------ALLLDGKIYVVggwddGGNVAWVE 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 30699022 367 KYDKRLNVWNKVGNLPERASSMngwgMAFRACGDQLVVVGG 407
Cdd:COG3055 141 VYDPATGTWTQLAPLPTPRDHL----AAAVLPDGKILVIGG 177
|
|
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
159-307 |
4.02e-15 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 75.19 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 159 EAYDPNGDRWLRVPKMTFNECFMCSdkeSLAVGTELLVFGKeimshviYRYSILTNTWTSGMQMNVPRCLFGSASLGEIA 238
Cdd:COG3055 140 EVYDPATGTWTQLAPLPTPRDHLAA---AVLPDGKILVIGG-------RNGSGFSNTWTTLAPLPTARAGHAAAVLGGKI 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30699022 239 VIAGGcdpRGRILSSAELYNSETGEWTVIPSMNKARKMCSSVFMDGNFYCIGGIGEGN--SKMLLCGEVYD 307
Cdd:COG3055 210 LVFGG---ESGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIGGETKPGvrTPLVTSAEVYD 277
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
226-407 |
5.53e-12 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 67.49 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 226 RCLFGSASLGEIAVIAGGCDPRGRILSSAELYNSETGEWTVIPSMNKARKMCSSVFMDGNFYCIGGIGEGNSkmLLCGEV 305
Cdd:PHA03098 285 VYCFGSVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSIS--LNTVES 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 306 YDLKKKTWTLIPNMLPERSSGGggdqakeiaaataaseapplVAVVKDELYAA------NYAQQEVKKYDKRLNVWNKVG 379
Cdd:PHA03098 363 WKPGESKWREEPPLIFPRYNPC--------------------VVNVNNLIYVIggisknDELLKTVECFSLNTNKWSKGS 422
|
170 180
....*....|....*....|....*...
gi 30699022 380 NLPeraSSMNGWGMAFRacGDQLVVVGG 407
Cdd:PHA03098 423 PLP---ISHYGGCAIYH--DGKIYVIGG 445
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
149-321 |
3.64e-09 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 58.63 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 149 IYFSCRLLEWEAYDPNGDRWLRVPKMTFNECFMCSDKeslaVGTELLVFGKEIMSH----VIYRYSILTNTWTSGMQMNV 224
Cdd:PHA03098 351 IYNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVN----VNNLIYVIGGISKNDellkTVECFSLNTNKWSKGSPLPI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 225 PRCLFGSASLGEIAVIAGGCDPRGRI--LSSAELYNSETGEWTVIPSMNKARKMCSSVFMDGNFYCIGGIGEGNSKMLLc 302
Cdd:PHA03098 427 SHYGGCAIYHDGKIYVIGGISYIDNIkvYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEYYINEI- 505
|
170
....*....|....*....
gi 30699022 303 gEVYDLKKKTWTLIPNMLP 321
Cdd:PHA03098 506 -EVYDDKTNTWTLFCKFPK 523
|
|
| Kelch |
smart00612 |
Kelch domain; |
240-284 |
5.89e-08 |
|
Kelch domain;
Pssm-ID: 128874 [Multi-domain] Cd Length: 47 Bit Score: 48.71 E-value: 5.89e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 30699022 240 IAGGCDPrGRILSSAELYNSETGEWTVIPSMNKARKMCSSVFMDG 284
Cdd:smart00612 4 VVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
|
|
| Kelch_1 |
pfam01344 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
225-271 |
6.61e-08 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
Pssm-ID: 396078 [Multi-domain] Cd Length: 46 Bit Score: 48.76 E-value: 6.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30699022 225 PRCLFGSASLGEIAVIAGGCDpRGRILSSAELYNSETGEWTVIPSMN 271
Cdd:pfam01344 1 RRSGAGVVVVGGKIYVIGGFD-GNQSLNSVEVYDPETNTWSKLPSMP 46
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
160-382 |
1.23e-06 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 50.54 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 160 AYDPNGDRWLRVPKMTFN--ECFMCSDKESL-AVGTEllvfGKEIMSHVIYRYSILTNTWTSGMQMNVPRCLFGSASLGE 236
Cdd:PHA03098 315 SYDTKTKSWNKVPELIYPrkNPGVTVFNNRIyVIGGI----YNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNN 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699022 237 IAVIAGGCDPRGRILSSAELYNSETGEWTVIPSMNKARKMCSSVFMDGNFYCIGGIG-EGNSKMLLCGEVYDLKKKTWTL 315
Cdd:PHA03098 391 LIYVIGGISKNDELLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGISyIDNIKVYNIVESYNPVTNKWTE 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30699022 316 IPNMLPERSSggggdqakeiaaataaseapPLVAVVKDELYA-----ANYAQQEVKKYDKRLNVWNKVGNLP 382
Cdd:PHA03098 471 LSSLNFPRIN--------------------ASLCIFNNKIYVvggdkYEYYINEIEVYDDKTNTWTLFCKFP 522
|
|
| Kelch_1 |
pfam01344 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
273-319 |
1.41e-06 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
Pssm-ID: 396078 [Multi-domain] Cd Length: 46 Bit Score: 44.91 E-value: 1.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30699022 273 ARKMCSSVFMDGNFYCIGGIGEGNSkmLLCGEVYDLKKKTWTLIPNM 319
Cdd:pfam01344 1 RRSGAGVVVVGGKIYVIGGFDGNQS--LNSVEVYDPETNTWSKLPSM 45
|
|
| F-box_AtAFR-like |
cd22152 |
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ... |
105-139 |
2.91e-04 |
|
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and similar proteins; AtAFR, also called SKP1-interacting partner 29 (AtSKIP29), or F-box protein AFR, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It is part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyl elongation in response to red and far-red light exposure. This subfamily also includes many other Arabidopsis thaliana SKP1-interacting partner proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.
Pssm-ID: 438923 Cd Length: 45 Bit Score: 38.32 E-value: 2.91e-04
10 20 30
....*....|....*....|....*....|....*
gi 30699022 105 LNCLAHCSLSDFGSIASTNRTFRSLIKDSELYRLR 139
Cdd:cd22152 11 LQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
|
|
| Kelch_4 |
pfam13418 |
Galactose oxidase, central domain; |
225-270 |
3.11e-04 |
|
Galactose oxidase, central domain;
Pssm-ID: 433191 [Multi-domain] Cd Length: 49 Bit Score: 38.36 E-value: 3.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30699022 225 PRCLFGSASLGE-IAVIAGGCDPRGRILSSAELYNSETGEWTVIPSM 270
Cdd:pfam13418 1 PRAYHTSTSIPDdTIYLFGGEGEDGTLLSDLWVFDLSTNEWTRLGSL 47
|
|
| Kelch_6 |
pfam13964 |
Kelch motif; |
225-274 |
3.35e-04 |
|
Kelch motif;
Pssm-ID: 404790 [Multi-domain] Cd Length: 50 Bit Score: 38.47 E-value: 3.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 30699022 225 PRCLFGSASLGEIAVIAGGCDPRGRILSSAELYNSETGEWTVIPSMNKAR 274
Cdd:pfam13964 1 PRTFHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPLPTPR 50
|
|
| Kelch_6 |
pfam13964 |
Kelch motif; |
273-319 |
3.46e-03 |
|
Kelch motif;
Pssm-ID: 404790 [Multi-domain] Cd Length: 50 Bit Score: 35.39 E-value: 3.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30699022 273 ARKMCSSVFMDGNFYCIGGIGEGNSKmLLCGEVYDLKKKTWTLIPNM 319
Cdd:pfam13964 1 PRTFHSVVSVGGYIYVFGGYTNASPA-LNKLEVYNPLTKSWEELPPL 46
|
|
| Kelch_3 |
pfam13415 |
Galactose oxidase, central domain; |
235-280 |
6.43e-03 |
|
Galactose oxidase, central domain;
Pssm-ID: 433188 [Multi-domain] Cd Length: 49 Bit Score: 34.57 E-value: 6.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 30699022 235 GEIAVIAGGCDPRGRILSSAELYNSETGEWTVIPSMNKARkMCSSV 280
Cdd:pfam13415 2 DKLYIFGGLGFDGQTRLNDLYVYDLDTNTWTQIGDLPPPR-SGHSA 46
|
|
|