|
Name |
Accession |
Description |
Interval |
E-value |
| DsbD |
COG4232 |
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ... |
200-668 |
3.23e-130 |
|
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443376 [Multi-domain] Cd Length: 416 Bit Score: 390.32 E-value: 3.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 200 TIFFISFLSGFAALLTPCVFPMIPMTVSYFTKQS-KTKAKGVKNAVIYGISIIVIYVLLGSAITAIFGADALNALASNFW 278
Cdd:COG4232 4 LILLLAFLGGLLLNLTPCVLPMLPIKSSIIVGQGgKSRRRAFLLSLAYVLGMALTYTLLGLLAALLGGAVGWGFQLQSPW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 279 FNLIFFLILVVFAISFLGAFEITLPSSWSTKVDAQADRSGFVGIFFMALALAIVSFSCTGPIVGTLLVQAASEGG-IAPI 357
Cdd:COG4232 84 VLGALALLFVLLALSMFGLFELQLPSSLQNRLAALSNGGGLLGAFFMGVLAALVATPCTAPFLGGALGYALQTGDaLLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 358 IGMFGFSLAIALPFALFAAFPGWLHSLPKSGGWMNTVKVVLGFLELALAFKFLSNADLvlqyHWIEREVFIAIWIAVFAA 437
Cdd:COG4232 164 LALFALGLGMALPLLLLGLFPGLLKLLPKPGAWMETVKQVFGFLLLATAIWLLSVLLP----QAGLDAVALLLWALLLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 438 LSLYLFGKIRLPHDDATDRISVgRLLLGLVTLSFTVYM-IPGLWGAplnliNAFPPPQhysespygvgytagggstnvde 516
Cdd:COG4232 240 LALWLLGALRLPHDSSGRRLSV-RKGLGLLLLLAGLALlLGALSGA-----DPLQPLA---------------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 517 galPEGAHLFKPHNIVTFDDYEKGLAYAKQVNKPVMLDFTGWSCVNCRKMEQNVWPNPQVLDALRNEVVLISLYVDDKRE 596
Cdd:COG4232 292 ---AGAAAAAAAAGLAWQADLEAALAEARAEGKPVFVDFTADWCVTCKENERTVFSDPEVQAALADDVVLLKADVTDNDP 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2732283776 597 lpesevkpsqiregkmiktigqKWSEFQTlKYKANTQPFYVLMNHQGENLvAPIGYTLdtdDPDEFYQWIKQ 668
Cdd:COG4232 369 ----------------------EITALLK-RFGRFGVPTYVFYDPDGEEL-PRLGFML---TADEFLAALEK 413
|
|
| dipZ |
PRK00293 |
thiol:disulfide interchange protein precursor; Provisional |
100-586 |
6.55e-38 |
|
thiol:disulfide interchange protein precursor; Provisional
Pssm-ID: 234717 [Multi-domain] Cd Length: 571 Bit Score: 148.82 E-value: 6.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 100 YFYRQAVFKQRIKL---LGEVTSMSiKAEVEFMSCDDSN-CLPPDSVDLEffLSGIAAANqgatpqftfgnnteenntvp 175
Cdd:PRK00293 90 FFGEVEVYRDRLDLpvpLNQAAAGA-TLTVTYQGCADAGfCYPPETRTVP--LSAVAANS-------------------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 176 attvSQTTAPKAPVQTPISHQGLWTIFFISFLSGFAALLTPCVFPMIPMTVSYF--TKQSKTKAKGVKNAVIYGISIIVI 253
Cdd:PRK00293 147 ----APAPAPAPAGQATASLASLPWSLLWFFLIGIGLAFTPCVLPMYPILSGIVlgGKQRLSTARALLLSFVYVQGMALT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 254 YVLLGsAITAIFGADALNALASNfWFnLIFFLIL-VVFAISFLGAFEITLPSSWSTKVDAQADR--SG-FVGIFFM-ALA 328
Cdd:PRK00293 223 YTLLG-LVVAAAGLQFQAALQHP-YV-LIGLSILfVLLALSMFGLFTLQLPSSLQTRLTLLSNRqqGGsLGGVFVMgAIS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 329 LAIVSFSCTGPIVGTLLVQAAS----EGGIApiigMFGFSLAIALPFALFAAFPGWLhsLPKSGGWMNTVKVVLGFLELA 404
Cdd:PRK00293 300 GLICSPCTTAPLSGALLYIAQSgdllLGGLT----LYLLALGMGLPLILITTFGNKL--LPKSGPWMNQVKTAFGFVLLA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 405 LAFKFLSNadlVLQYHWIerevfIAIWIAVFAALSLYLFGKIRLPHddATDRISVGRLLLglvtlsftVYMIPGLWGAPL 484
Cdd:PRK00293 374 LPVFLLER---VLPGVWG-----LRLWSLLGVAFFGWAFIQSLKAK--RGWMRLLGQILL--------LAALLASVRPLQ 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 485 NLinAFPPPQHysespygvgytagggstnvdeGALPEGAHLFKPhnIVTFDDYEKGLAYAKQVNKPVMLDF-TGWsCVNC 563
Cdd:PRK00293 436 DW--AFGGAAA---------------------GAQTQAHLNFQR--IKTVAELDQALAEAKGKGKPVMLDLyADW-CVAC 489
|
490 500
....*....|....*....|...
gi 2732283776 564 RKMEQNVWPNPQVLDALRNEVVL 586
Cdd:PRK00293 490 KEFEKYTFSDPQVQQALADTVLL 512
|
|
| DsbD |
pfam02683 |
Cytochrome C biogenesis protein transmembrane region; This family consists of the ... |
205-379 |
1.03e-17 |
|
Cytochrome C biogenesis protein transmembrane region; This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family.
Pssm-ID: 280792 [Multi-domain] Cd Length: 213 Bit Score: 82.45 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 205 SFLSGFAALLTPCVFPMIPMTVSYFT-------KQSKTKAKGVKNAVIYGISIIVIYVLLGsaitaiFGADALNALASNF 277
Cdd:pfam02683 1 AFLAGLLSFLSPCILPLIPAYLSYISgvsvgdrKQGKKRVRVLLKSLLFVLGLSLVFVLLG------LSAAFLGQLFGDF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 278 --WFNLIFFLILVVFAISFLGAFEIT------LPSSWSTKVDAQadrsgFVGIFFMALALAIVSFSCTGPIVGTLLVQAA 349
Cdd:pfam02683 75 kgWVRIIAGLIVILFGLHFLGVFRIPflyklrLVHKTKKKISLP-----VLGAFLLGMTFALGWTPCIGPILASVLALAA 149
|
170 180 190
....*....|....*....|....*....|.
gi 2732283776 350 SEGGIAPIIG-MFGFSLAIALPFALFAAFPG 379
Cdd:pfam02683 150 STGSLLLGAGlMVVYVLGLAAPFLLASLFFG 180
|
|
| DsbDgamma |
cd02953 |
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ... |
541-587 |
2.76e-09 |
|
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.
Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 54.92 E-value: 2.76e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2732283776 541 LAYAKQVNKPVMLDFTG-WsCVNCRKMEQNVWPNPQVLDALRNEVVLI 587
Cdd:cd02953 4 LAQALAQGKPVFVDFTAdW-CVTCKVNEKVVFSDPEVQAALKKDVVLL 50
|
|
| DsbC |
pfam11412 |
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ... |
40-140 |
2.66e-05 |
|
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD.
Pssm-ID: 463273 [Multi-domain] Cd Length: 115 Bit Score: 43.88 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 40 LVATASIEAGWKLYGQNIppngpvptSFKyAQTPAFELVGKTEESKPIVKHDKVFDMEIAYfYRQAVFKQRIKLLGEVTs 119
Cdd:pfam11412 21 LGLRWEIAPGYYLYWDKP--------GFE-WTPPDGVTLGELQLPAPERKPDEFFGEVEVY-EGEVTLPLPLAAAAGAT- 89
|
90 100
....*....|....*....|..
gi 2732283776 120 msIKAEVEFMSCDDSN-CLPPD 140
Cdd:pfam11412 90 --LKLEVTYQGCAEAGiCYPPE 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DsbD |
COG4232 |
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ... |
200-668 |
3.23e-130 |
|
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443376 [Multi-domain] Cd Length: 416 Bit Score: 390.32 E-value: 3.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 200 TIFFISFLSGFAALLTPCVFPMIPMTVSYFTKQS-KTKAKGVKNAVIYGISIIVIYVLLGSAITAIFGADALNALASNFW 278
Cdd:COG4232 4 LILLLAFLGGLLLNLTPCVLPMLPIKSSIIVGQGgKSRRRAFLLSLAYVLGMALTYTLLGLLAALLGGAVGWGFQLQSPW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 279 FNLIFFLILVVFAISFLGAFEITLPSSWSTKVDAQADRSGFVGIFFMALALAIVSFSCTGPIVGTLLVQAASEGG-IAPI 357
Cdd:COG4232 84 VLGALALLFVLLALSMFGLFELQLPSSLQNRLAALSNGGGLLGAFFMGVLAALVATPCTAPFLGGALGYALQTGDaLLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 358 IGMFGFSLAIALPFALFAAFPGWLHSLPKSGGWMNTVKVVLGFLELALAFKFLSNADLvlqyHWIEREVFIAIWIAVFAA 437
Cdd:COG4232 164 LALFALGLGMALPLLLLGLFPGLLKLLPKPGAWMETVKQVFGFLLLATAIWLLSVLLP----QAGLDAVALLLWALLLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 438 LSLYLFGKIRLPHDDATDRISVgRLLLGLVTLSFTVYM-IPGLWGAplnliNAFPPPQhysespygvgytagggstnvde 516
Cdd:COG4232 240 LALWLLGALRLPHDSSGRRLSV-RKGLGLLLLLAGLALlLGALSGA-----DPLQPLA---------------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 517 galPEGAHLFKPHNIVTFDDYEKGLAYAKQVNKPVMLDFTGWSCVNCRKMEQNVWPNPQVLDALRNEVVLISLYVDDKRE 596
Cdd:COG4232 292 ---AGAAAAAAAAGLAWQADLEAALAEARAEGKPVFVDFTADWCVTCKENERTVFSDPEVQAALADDVVLLKADVTDNDP 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2732283776 597 lpesevkpsqiregkmiktigqKWSEFQTlKYKANTQPFYVLMNHQGENLvAPIGYTLdtdDPDEFYQWIKQ 668
Cdd:COG4232 369 ----------------------EITALLK-RFGRFGVPTYVFYDPDGEEL-PRLGFML---TADEFLAALEK 413
|
|
| dipZ |
PRK00293 |
thiol:disulfide interchange protein precursor; Provisional |
100-586 |
6.55e-38 |
|
thiol:disulfide interchange protein precursor; Provisional
Pssm-ID: 234717 [Multi-domain] Cd Length: 571 Bit Score: 148.82 E-value: 6.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 100 YFYRQAVFKQRIKL---LGEVTSMSiKAEVEFMSCDDSN-CLPPDSVDLEffLSGIAAANqgatpqftfgnnteenntvp 175
Cdd:PRK00293 90 FFGEVEVYRDRLDLpvpLNQAAAGA-TLTVTYQGCADAGfCYPPETRTVP--LSAVAANS-------------------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 176 attvSQTTAPKAPVQTPISHQGLWTIFFISFLSGFAALLTPCVFPMIPMTVSYF--TKQSKTKAKGVKNAVIYGISIIVI 253
Cdd:PRK00293 147 ----APAPAPAPAGQATASLASLPWSLLWFFLIGIGLAFTPCVLPMYPILSGIVlgGKQRLSTARALLLSFVYVQGMALT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 254 YVLLGsAITAIFGADALNALASNfWFnLIFFLIL-VVFAISFLGAFEITLPSSWSTKVDAQADR--SG-FVGIFFM-ALA 328
Cdd:PRK00293 223 YTLLG-LVVAAAGLQFQAALQHP-YV-LIGLSILfVLLALSMFGLFTLQLPSSLQTRLTLLSNRqqGGsLGGVFVMgAIS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 329 LAIVSFSCTGPIVGTLLVQAAS----EGGIApiigMFGFSLAIALPFALFAAFPGWLhsLPKSGGWMNTVKVVLGFLELA 404
Cdd:PRK00293 300 GLICSPCTTAPLSGALLYIAQSgdllLGGLT----LYLLALGMGLPLILITTFGNKL--LPKSGPWMNQVKTAFGFVLLA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 405 LAFKFLSNadlVLQYHWIerevfIAIWIAVFAALSLYLFGKIRLPHddATDRISVGRLLLglvtlsftVYMIPGLWGAPL 484
Cdd:PRK00293 374 LPVFLLER---VLPGVWG-----LRLWSLLGVAFFGWAFIQSLKAK--RGWMRLLGQILL--------LAALLASVRPLQ 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 485 NLinAFPPPQHysespygvgytagggstnvdeGALPEGAHLFKPhnIVTFDDYEKGLAYAKQVNKPVMLDF-TGWsCVNC 563
Cdd:PRK00293 436 DW--AFGGAAA---------------------GAQTQAHLNFQR--IKTVAELDQALAEAKGKGKPVMLDLyADW-CVAC 489
|
490 500
....*....|....*....|...
gi 2732283776 564 RKMEQNVWPNPQVLDALRNEVVL 586
Cdd:PRK00293 490 KEFEKYTFSDPQVQQALADTVLL 512
|
|
| CcdA |
COG0785 |
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ... |
202-384 |
5.53e-26 |
|
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440548 [Multi-domain] Cd Length: 193 Bit Score: 105.70 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 202 FFISFLSGFAALLTPCVFPMIPMTVSYFTKQSKT-KAKGVKNAVIYGISIIVIYVLLGSAITAIFGAdalnALASNFWFN 280
Cdd:COG0785 5 LLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLSRAsRRRALLRALLFVLGFSLVFVLLGALASALGSL----LGQYQDLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 281 LIFFLILVVFAISFLGAFEITLpSSWSTKVDAqADRSGFVGIFFMALALAIVSFSCTGPIVGTLLVQAASEGGIAPIIG- 359
Cdd:COG0785 81 IVAGVLLILFGLVLLGLLKIPF-LQREARINL-RRKAGLLGAFLLGLAFGLGWTPCIGPILGAILALAATSGSVLRGALl 158
|
170 180
....*....|....*....|....*
gi 2732283776 360 MFGFSLAIALPFALFAAFPGWLHSL 384
Cdd:COG0785 159 LLAYALGLGLPFLLLALFAGRLLGR 183
|
|
| DsbD |
pfam02683 |
Cytochrome C biogenesis protein transmembrane region; This family consists of the ... |
205-379 |
1.03e-17 |
|
Cytochrome C biogenesis protein transmembrane region; This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family.
Pssm-ID: 280792 [Multi-domain] Cd Length: 213 Bit Score: 82.45 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 205 SFLSGFAALLTPCVFPMIPMTVSYFT-------KQSKTKAKGVKNAVIYGISIIVIYVLLGsaitaiFGADALNALASNF 277
Cdd:pfam02683 1 AFLAGLLSFLSPCILPLIPAYLSYISgvsvgdrKQGKKRVRVLLKSLLFVLGLSLVFVLLG------LSAAFLGQLFGDF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 278 --WFNLIFFLILVVFAISFLGAFEIT------LPSSWSTKVDAQadrsgFVGIFFMALALAIVSFSCTGPIVGTLLVQAA 349
Cdd:pfam02683 75 kgWVRIIAGLIVILFGLHFLGVFRIPflyklrLVHKTKKKISLP-----VLGAFLLGMTFALGWTPCIGPILASVLALAA 149
|
170 180 190
....*....|....*....|....*....|.
gi 2732283776 350 SEGGIAPIIG-MFGFSLAIALPFALFAAFPG 379
Cdd:pfam02683 150 STGSLLLGAGlMVVYVLGLAAPFLLASLFFG 180
|
|
| SoxW |
COG2143 |
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ... |
534-667 |
4.69e-11 |
|
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441746 [Multi-domain] Cd Length: 146 Bit Score: 61.07 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 534 FDDYEKGLAYAKQVNKPVMLDFTGWSCVNCRKMEQNVWPNPQVLDALRNEVVLISLYVDDKRELPESEvkpsqiregkmi 613
Cdd:COG2143 26 LLDLEEDLALAKAEGKPILLFFESDWCPYCKKLHKEVFSDPEVAAYLKENFVVVQLDAEGDKEVTDFD------------ 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2732283776 614 ktiGQKWSEFQ-TLKYKANTQPFYVLMNHQGeNLVAPI-GYTldtdDPDEFYQWIK 667
Cdd:COG2143 94 ---GETLTEKElARKYGVRGTPTLVFFDAEG-KEIARIpGYL----KPETFLALLK 141
|
|
| Thioredoxin_7 |
pfam13899 |
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
535-604 |
2.48e-09 |
|
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.
Pssm-ID: 433567 [Multi-domain] Cd Length: 84 Bit Score: 54.29 E-value: 2.48e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 535 DDYEKGLAYAKQVNKPVMLDFTGWSCVNCRKMEQNVWPNPQVLDALRNEVVLisLYVDDKRELPESEVKP 604
Cdd:pfam13899 4 SDLEEALAAAAERGKPVLVDFGADWCFTCQVLERDFLSHEEVKAALAKNFVL--LRLDWTSRDANITRAF 71
|
|
| DsbDgamma |
cd02953 |
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ... |
541-587 |
2.76e-09 |
|
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.
Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 54.92 E-value: 2.76e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2732283776 541 LAYAKQVNKPVMLDFTG-WsCVNCRKMEQNVWPNPQVLDALRNEVVLI 587
Cdd:cd02953 4 LAQALAQGKPVFVDFTAdW-CVTCKVNEKVVFSDPEVQAALKKDVVLL 50
|
|
| Thioredoxin_2 |
pfam13098 |
Thioredoxin-like domain; |
548-666 |
6.41e-07 |
|
Thioredoxin-like domain;
Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 48.19 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 548 NKPVMLDFTGWSCVNCRKMEQNVWPNPQVLDALRNEVVLISLYVDDKRElpesevKPSQIREGKMIKTIGQkwsefqtlK 627
Cdd:pfam13098 4 GKPVLVVFTDPDCPYCKKLKKELLEDPDVTVYLGPNFVFIAVNIWCAKE------VAKAFTDILENKELGR--------K 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 2732283776 628 YKANTQPFYVLMNHQGENLVAPiGYTldtdDPDEFYQWI 666
Cdd:pfam13098 70 YGVRGTPTIVFFDGKGELLRLP-GYV----PAEEFLALL 103
|
|
| DsbC |
pfam11412 |
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ... |
40-140 |
2.66e-05 |
|
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD.
Pssm-ID: 463273 [Multi-domain] Cd Length: 115 Bit Score: 43.88 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 40 LVATASIEAGWKLYGQNIppngpvptSFKyAQTPAFELVGKTEESKPIVKHDKVFDMEIAYfYRQAVFKQRIKLLGEVTs 119
Cdd:pfam11412 21 LGLRWEIAPGYYLYWDKP--------GFE-WTPPDGVTLGELQLPAPERKPDEFFGEVEVY-EGEVTLPLPLAAAAGAT- 89
|
90 100
....*....|....*....|..
gi 2732283776 120 msIKAEVEFMSCDDSN-CLPPD 140
Cdd:pfam11412 90 --LKLEVTYQGCAEAGiCYPPE 109
|
|
| AraJ |
COG2814 |
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; |
255-487 |
4.15e-05 |
|
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
Pssm-ID: 442063 [Multi-domain] Cd Length: 348 Bit Score: 46.12 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 255 VLLGSAITAIFGAdALNALASNFWFnliffLILVVFAISFLGAFEITLPSSWSTKVDAQADRSGFVGIFFMALALAIVSf 334
Cdd:COG2814 77 VLLLGLLLFALGS-LLCALAPSLWL-----LLAARFLQGLGAGALFPAALALIADLVPPERRGRALGLLGAGLGLGPAL- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 335 sctGPIVGTLLVQAASEGGIapiigmFGFSLAIALPFALFAAF--------------PGWLHSLPKSGGWMNTVKVVLGF 400
Cdd:COG2814 150 ---GPLLGGLLADLFGWRWV------FLVNAVLALLALLLLLRllpesrpaararlrGSLRELLRRPRLLLLLLLAFLLG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 401 LELALAFKFLSNAdLVLQYHWIEREV-FIAIWIAVFAALSLYLFGKIrlphddaTDRISVGRLLLGLVTLSFTVYMIPGL 479
Cdd:COG2814 221 FGFFALFTYLPLY-LQEVLGLSASAAgLLLALFGLGGVLGALLAGRL-------ADRFGRRRLLLIGLLLLALGLLLLAL 292
|
....*...
gi 2732283776 480 WGAPLNLI 487
Cdd:COG2814 293 AGSLWLLL 300
|
|
| ProP |
COG0477 |
MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and ... |
196-407 |
5.68e-04 |
|
MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and metabolism, Amino acid transport and metabolism, Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440245 [Multi-domain] Cd Length: 295 Bit Score: 42.49 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 196 QGLWTIFFISFLSGF-AALLTPCVFPMIpmtVSYFTKQSKTKAkgvknaviygISIIVIYVLLGSAITAIFGAdalnALA 274
Cdd:COG0477 100 PSPELLIAARALQGIgAGGLMPGALALI---AELFPARERGRA----------LGLWGAAIGLGLALGPLLGG----LLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 275 SNFWFNLIFFLILVVFAISFLGAFeiTLPSSWSTKVDAQADRSGFVGIFFMALALAIVSFSCTGPIVGTLLVQAASEGGI 354
Cdd:COG0477 163 AALGWRWIFLINAPLGLLALVLRL--RLPESRGLLLALLALALAALLLAALALALLALLLLLLLLLLALLALLLAGAALL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2732283776 355 APIIGMFGFSLAIALPFALFAAFPGWLHSLPKSGGWMNTVKVVLGFLELALAF 407
Cdd:COG0477 241 LLLALLLLALLLLLALLLLAALLLLLLLLLLLALLLALLLLLLLLLLLLLLAL 293
|
|
| MFS_NepI_like |
cd17324 |
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator ... |
255-487 |
7.03e-04 |
|
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily; This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340882 [Multi-domain] Cd Length: 370 Bit Score: 42.54 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 255 VLLGSAITAIFGAdALNALASNFWFnLIFFLILVVFAISflGAFEITLPssWSTKVDAQADRSGFVGIFFMALALAIVsf 334
Cdd:cd17324 66 LLLVLLLLFILGN-LLAALAPSFAL-LLLARALAGLAHG--GFWAIAAA--YAADLVPPEKRGRAIGLVFSGLTLGLV-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 335 scTGPIVGTLLVQAASEGGIAPIIGMFGFSLAIALPFALfaafPGWLHSLPKSGGWMNTVKVVLGF--LELALAFKFLSN 412
Cdd:cd17324 138 --LGRPLGGLLGQLLGWRAAFLAIAVLALLAALLLWRLL----PSLPPKKPGSLGLLSSLLLLLRNprLRLAYLITFLLF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 413 ADLVLQYHWIE---------REVFIAIWIAVF---AALSLYLFGKIrlphddaTDRISVGRLLLGLVTLSFTVYMIPGLW 480
Cdd:cd17324 212 GGFFALYTYLApfltdvpgfSSSAIIGLLLLFgvaGVVGSPLAGRL-------ADRGGRRALLIALLLLAAALLLLTLLG 284
|
....*..
gi 2732283776 481 GAPLNLI 487
Cdd:cd17324 285 PSPLLLL 291
|
|
| MFS_SV2_like |
cd17316 |
Metazoan Synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters of the ... |
256-377 |
1.30e-03 |
|
Metazoan Synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters of the Major Facilitator Superfamily; This family is composed of metazoan synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters including those that transport inorganic phosphate (Pht), aromatic compounds (PcaK and related proteins), proline/betaine (ProP), alpha-ketoglutarate (KgtP), citrate (CitA), shikimate (ShiA), and cis,cis-muconate (MucK), among others. SV2 is a transporter-like protein that serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. Also included in this family is synaptic vesicle 2 (SV2)-related protein (SVOP) and similar proteins. SVOP is a transporter-like nucleotide binding protein that localizes to neurotransmitter-containing vesicles. The SV2-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340874 [Multi-domain] Cd Length: 353 Bit Score: 41.43 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 256 LLGSAITAIFGADALNALASNFWFNLIFFLILVVFAISFLGAFEITLPSSWSTKVDAQAdrsgfVGIFFmalALAIVSFS 335
Cdd:cd17316 247 VIGLILSGILALPLFYLLSGSPTLLLLLLFILSFFVGGVWGALYAYLAELFPTEVRATG-----VGLSY---NLGRLGGG 318
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2732283776 336 CTGPIVGTLLVQaaseggiAPIIGMFGFSLAIALPFALFAAF 377
Cdd:cd17316 319 GAPPLIALLLAS-------TGGTGVPALILALLAIVALIVAL 353
|
|
| MFS_MdtG_SLC18_like |
cd17325 |
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ... |
169-375 |
1.88e-03 |
|
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters; This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340883 [Multi-domain] Cd Length: 375 Bit Score: 41.02 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 169 EENNTVPATTVSQTTAPKAPVQTPISHQGLWTIFFISFLSGFAALLtpcVFPMIPMTVsyftkQSKTKAKGVKNAVIYGI 248
Cdd:cd17325 172 PEPRPPPNKRAVSAARLRSGLRLLLRDRRLLALFLAIFVLAFAFGA---LEPFLPLYA-----AELGGLSPAQIGLLFGA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 249 SIIV------------------IYVLLGSAITAIFGAdaLNALASNFWFnLIFFLILVVFAISFLGAfeitlpsSWSTKV 310
Cdd:cd17325 244 QGLAsalsqppagklsdrigrkPLILIGLLLSAVALL--LLPLATSFWL-LLLLLALLGLGLGLVFP-------ATLALL 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2732283776 311 DAQADRSGF---VGIFFMALALAIVsfscTGPIVGTLLVQAAseGGIAPIIGMFGFSLAIALPFALFA 375
Cdd:cd17325 314 ADIVPPEGRgtaMGLFNTAFSLGMV----LGPLLGGFLYDAF--GFATPFLAAAALLLLAAVLFLLLR 375
|
|
| SoxW |
cd02951 |
SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, ... |
544-668 |
2.11e-03 |
|
SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, encoded by a genetic locus (sox operon) involved in thiosulfate oxidation. Sulfur bacteria oxidize sulfur compounds to provide reducing equivalents for carbon dioxide fixation during autotrophic growth and the respiratory electron transport chain. It is unclear what the role of SoxW is, since it has been found to be dispensable in the oxidation of thiosulfate to sulfate. SoxW is specifically kept in the reduced state by SoxV, which is essential in thiosulfate oxidation.
Pssm-ID: 239249 [Multi-domain] Cd Length: 125 Bit Score: 38.45 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 544 AKQVNKPVMLDFTGWSCVNCRKMEQNVWPNPQVLDALRNEVVLISLYVDDKRELPESevkpsqiregKMIKTIGQKWSEf 623
Cdd:cd02951 10 AADGKKPLLLLFSQPGCPYCDKLKRDYLNDPAVQAYIRAHFVVVYINIDGDKEVTDF----------DGEALSEKELAR- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2732283776 624 qtlKYKANTQPFYVLMNHQGENLVAPI-GYTLdtddPDEFYQWIKQ 668
Cdd:cd02951 79 ---KYRVRFTPTVIFLDPEGGKEIARLpGYLP----PDEFLAYLEY 117
|
|
| MFS_1 |
pfam07690 |
Major Facilitator Superfamily; |
196-400 |
2.14e-03 |
|
Major Facilitator Superfamily;
Pssm-ID: 429598 [Multi-domain] Cd Length: 344 Bit Score: 40.86 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 196 QGLWTIFFISFLSGFA-ALLTPcvfPMIPMTVSYFTKQSKTKAkgvknaviygISIIVIYVLLGSAITAIFGAdalnALA 274
Cdd:pfam07690 83 SSLWLLLVLRVLQGLGaGALFP---AALALIADWFPPEERGRA----------LGLVSAGFGLGAALGPLLGG----LLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 275 SNFWFNLIFFLILVVFAISFLGAF----EITLPSSWSTKVDAQADRSGFVGIFFMALALAIVSFSCTGPIVGTLL----- 345
Cdd:pfam07690 146 SLFGWRAAFLILAILSLLAAVLLLlprpPPESKRPKPAEEARLSLIVAWKALLRDPVLWLLLALLLFGFAFFGLLtylpl 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2732283776 346 ---------VQAASEGGIAPIIGMFGFSLA--------------IALPFALFAAFPGWLHSLPKSGGWMNTVKVVLGF 400
Cdd:pfam07690 226 yqevlglsaLLAGLLLGLGGLLGAIGRLLLgrlsdrlgrrrrllLALLLLILAALGLLLLSLTLSSLWLLLALLLLGF 303
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
549-670 |
2.51e-03 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 38.90 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 549 KPVMLDFTGWSCVNCRKMEqnvwpnpQVLDALRNE---VVLISLYVDDKRELPEsevkpSQIREGKMIKTIGQKWSEFQT 625
Cdd:COG0526 29 KPVLVNFWATWCPPCRAEM-------PVLKELAEEyggVVFVGVDVDENPEAVK-----AFLKELGLPYPVLLDPDGELA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2732283776 626 LKYKANTQPFYVLMNHQGENLVAPIGYTldtdDPDEFYQWIKQGI 670
Cdd:COG0526 97 KAYGVRGIPTTVLIDKDGKIVARHVGPL----SPEELEEALEKLL 137
|
|
| TauE |
COG0730 |
Sulfite exporter TauE/SafE/YfcA and related permeases, UPF0721 family [Inorganic ion transport ... |
251-382 |
4.81e-03 |
|
Sulfite exporter TauE/SafE/YfcA and related permeases, UPF0721 family [Inorganic ion transport and metabolism];
Pssm-ID: 440494 Cd Length: 250 Bit Score: 39.41 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 251 IVIYVLLGSAITAIFGAdALNALASNFWFNLIFFLILVVFAISFLgafeitLPSSWSTKVDAQADRSGFVGIFFMALALA 330
Cdd:COG0730 72 LLLPLALGALIGALLGA-LLLLLLPADVLKLLFGVLLLLVALLML------LRPKPGAEPERRLPRRSPLLLLLLGFVIG 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2732283776 331 IVSFScTGPIVGTLLVQAASEGGIAPIIGMFGFSLAIALPFALFAAFPGWLH 382
Cdd:COG0730 145 FLSGL-FGIGGGFLLVPALVLLLGLPLKRAVATSLALIFVTALAGLIGFALL 195
|
|
| DUF4153 |
pfam13687 |
Domain of unknown function (DUF4153); Members of this family are annotated as putative inner ... |
317-473 |
5.29e-03 |
|
Domain of unknown function (DUF4153); Members of this family are annotated as putative inner membrane proteins.
Pssm-ID: 463956 Cd Length: 371 Bit Score: 39.61 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 317 SGFVGIFFMALALAIVSFSCTGPIVGTLLVQAASEGGIAPIIGMFGFslaIALPFALFAAFPGWLHSLPKSGGWMNTVKV 396
Cdd:pfam13687 16 NPWLIVLNLLAILLLGLLALLQFAGGRTWRLILLGLLLLPLLFGFAL---IGLPFLLLAGFRKIRGSKRKRLFGYVLLGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 397 VLGFLELALAFKFLSNADLVLQyHWIER--------EVFIAIWIAVFAALSLYLFG----KIRLPHDDATDRISVGRLLL 464
Cdd:pfam13687 93 LIALPLLLVFLALLASADAAFA-SLLGRlfpdifpgLLFGLLWLLLALLLGFLLFGalyfLALPPKPDEELEPERPSLPR 171
|
....*....
gi 2732283776 465 GLVTLSFTV 473
Cdd:pfam13687 172 VEVITVLGL 180
|
|
| AraJ |
COG2814 |
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; |
196-381 |
5.59e-03 |
|
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
Pssm-ID: 442063 [Multi-domain] Cd Length: 348 Bit Score: 39.57 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 196 QGLWTIFFISFLSGFA-ALLTPCVFPMIpmtVSYFTKQSKTKAkgvknaviygISIIVIYVLLGSAITAIFGAdalnALA 274
Cdd:COG2814 96 PSLWLLLAARFLQGLGaGALFPAALALI---ADLVPPERRGRA----------LGLLGAGLGLGPALGPLLGG----LLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732283776 275 SNFWFNLIFFLILVVFAISFLGAFeITLPSSWSTKVDAQADRSGFV---GIFFMALALAIVSFSCTGPIVGTLLVQAASE 351
Cdd:COG2814 159 DLFGWRWVFLVNAVLALLALLLLL-RLLPESRPAARARLRGSLRELlrrPRLLLLLLLAFLLGFGFFALFTYLPLYLQEV 237
|
170 180 190
....*....|....*....|....*....|.
gi 2732283776 352 GGIAPiiGMFGFSLAIALPFALFAAFP-GWL 381
Cdd:COG2814 238 LGLSA--SAAGLLLALFGLGGVLGALLaGRL 266
|
|
| |
