|
Name |
Accession |
Description |
Interval |
E-value |
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-602 |
0e+00 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 889.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 6 TRIAIVSEDRCKPKKCRQECKKSCPVVKTGKLCIEVGSTSKSAFISEELCIGCGICVKKCPFEAIQIINLPKDLAKDTTH 85
Cdd:COG1245 2 MRIAVVDRDRCQPKKCNYECIKYCPVNRTGKEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEDPVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 86 RYGANGFKLHRLPIPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDWEEILTHFRGSELQSYFIRVVEENLK 165
Cdd:COG1245 82 RYGENGFRLYGLPVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGTELQDYFKKLANGEIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 166 TAIKPQHVDYIKEVVRGNLGKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:COG1245 162 VAHKPQYVDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 246 YLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAYGVVTLPFSVREGINVFLAGFIPTENLRFR 325
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPGVYGVVSKPKSVRVGINQYLDGYLPEENVRIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 326 DESLTFRVSETTQENDGEVKSyaryKYPNMTKQLGDFKLEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGAF-PREEGV 404
Cdd:COG1245 322 DEPIEFEVHAPRREKEEETLV----EYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLkPDEGEV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 405 QSEIpefNVSYKPQGNDSKRECTVRQLLHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPA 484
Cdd:COG1245 398 DEDL---KISYKPQYISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 485 DIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQPAVKCIAHSPQSLLSGMNHFLS 564
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMREGMNRFLK 554
|
570 580 590
....*....|....*....|....*....|....*...
gi 15231301 565 HLNITFRRDPTNFRPRINKLESIKDKEQKTAGSYYYLD 602
Cdd:COG1245 555 ELGITFRRDEETGRPRINKPGSYLDREQKERGEYYYYE 592
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-602 |
0e+00 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 861.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 6 TRIAIVSEDRCKPKKCRQECKKSCPVVKTGKLCIEVGSTSKSAFISEELCIGCGICVKKCPFEAIQIINLPKDLAKDTTH 85
Cdd:PRK13409 2 MRIAVVDYDRCQPKKCNYECIKYCPVVRTGEETIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEEPVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 86 RYGANGFKLHRLPIPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDWEEILTHFRGSELQSYFIRVVEENLK 165
Cdd:PRK13409 82 RYGVNGFKLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTELQNYFKKLYNGEIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 166 TAIKPQHVDYIKEVVRGNLGKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:PRK13409 162 VVHKPQYVDLIPKVFKGKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 246 YLDVRQRLKAAQVIRSLLRhDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAYGVVTLPFSVREGINVFLAGFIPTENLRFR 325
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIAYGEPGAYGVVSKPKGVRVGINEYLKGYLPEENMRIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 326 DESLTFRVSETTQENDGEVKSyaryKYPNMTKQLGDFKLEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGAF-PREEGV 404
Cdd:PRK13409 321 PEPIEFEERPPRDESERETLV----EYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLkPDEGEV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 405 QSEIpefNVSYKPQGNDSKRECTVRQLLhDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPA 484
Cdd:PRK13409 397 DPEL---KISYKPQYIKPDYDGTVEDLL-RSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 485 DIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQPAVKCIAHSPQSLLSGMNHFLS 564
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASGPMDMREGMNRFLK 552
|
570 580 590
....*....|....*....|....*....|....*...
gi 15231301 565 HLNITFRRDPTNFRPRINKLESIKDKEQKTAGSYYYLD 602
Cdd:PRK13409 553 ELGITFRRDEETGRPRVNKPGSYLDREQKERGEYYYAD 590
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-332 |
3.14e-157 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 450.67 E-value: 3.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 78 DLAKDTTHRYGANGFKLHRLPIPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDWEEILTHFRGSELQSYFI 157
Cdd:cd03236 1 ELEDEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 158 RVVEENLKTAIKPQHVDYIKEVVRGNLGKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADI 237
Cdd:cd03236 81 KLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 238 YMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAYGVVTLPFSVREGINVFLAGFI 317
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLDGYL 240
|
250
....*....|....*
gi 15231301 318 PTENLRFRDESLTFR 332
Cdd:cd03236 241 PTENMRFREESIEFE 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
350-596 |
7.52e-146 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 421.43 E-value: 7.52e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQGNDSKRECTVR 429
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-DIEIELDTVSYKPQYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 430 QLLHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIK 509
Cdd:cd03237 80 DLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 510 RFILHAKKTAFIVEHDFIMATYLADRVIVYEGQPAVKCIAHSPQSLLSGMNHFLSHLNITFRRDPTNFRPRINKLESIKD 589
Cdd:cd03237 160 RFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFLKNLDITFRRDPETGRPRINKLGSVKD 239
|
....*..
gi 15231301 590 KEQKTAG 596
Cdd:cd03237 240 REQKESG 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
351-571 |
6.00e-67 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 215.90 E-value: 6.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 351 KYPNMTKQLGDFKLEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQGNDskrectvrq 430
Cdd:cd03222 2 LYPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-NDEWDGITPVYKPQYID--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 431 llhdkirdacahpqfmsdvirplqieqlmdqvvktLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKR 510
Cdd:cd03222 72 -----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 511 FILHAKKTAFIVEHDFIMATYLADRVIVYEGQPAVKCIAHSPQSLLSGMNHFLSHLNITFR 571
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
81-337 |
1.01e-48 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 169.90 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGANGFKLHRLPIP-RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILThfrgselqsyfirv 159
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---------DIEI-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 160 veENLKTAIKPQhvdYIKEVVRGNLGKMLEKLDERGLME-----EICADMELNQVLEREARQVSGGELQRFAIAAVFVKK 234
Cdd:cd03237 59 --ELDTVSYKPQ---YIKADYEGTVRDLLSSITKDFYTHpyfktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 235 ADIYMFDEPSSYLDVRQRLKAAQVIRSL-LRHDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAYGVVTLPFSVREGINVFL 313
Cdd:cd03237 134 ADIYLLDEPSAYLDVEQRLMASKVIRRFaENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFL 213
|
250 260
....*....|....*....|....
gi 15231301 314 AgfipteNLrfrdeSLTFRVSETT 337
Cdd:cd03237 214 K------NL-----DITFRRDPET 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
82-321 |
1.10e-44 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 156.58 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 82 DTTHRYGaNGFKLHRLPIPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppDWEEIlthfrgselqsyfirvve 161
Cdd:cd03222 5 DCVKRYG-VFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----EWDGI------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 162 enlKTAIKPQHVDyikevvrgnlgkmleklderglmeeicadmelnqvlerearqVSGGELQRFAIAAVFVKKADIYMFD 241
Cdd:cd03222 62 ---TPVYKPQYID------------------------------------------LSGGELQRVAIAAALLRNATFYLFD 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 242 EPSSYLDVRQRLKAAQVIRSLLRH-DSYVIVVEHDLSVLDYLSDFVCCLYGKPGAYGVVTLPFSVREGINVFLAGFIPTE 320
Cdd:cd03222 97 EPSAYLDIEQRLNAARAIRRLSEEgKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITF 176
|
.
gi 15231301 321 N 321
Cdd:cd03222 177 R 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
101-542 |
5.75e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.94 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNLGRFNtppdwEEILthFRGSEL--QSYFIR-----VVEENLKTAIKPQHV 173
Cdd:COG1123 30 APGETVALVGESGSGKSTLALALMG-LLPHGGRIS-----GEVL--LDGRDLleLSEALRgrrigMVFQDPMTQLNPVTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 174 -DYIKEVVRgNLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQR 252
Cdd:COG1123 102 gDQIAEALE-NLGLSRAEARAR--VLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 253 LKAAQVIRSLLR-HDSYVIVVEHDLSVLDYLSDFVCCLY-GKPGAYGVVTLPFSVREGINVflagfIPTENLRFRDESLT 330
Cdd:COG1123 179 AEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDdGRIVEDGPPEEILAAPQALAA-----VPRLGAARGRAAPA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 331 FRVSETTQENDGEVKSYARYKyPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIpE 410
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYPVRG-KGGVRAVDDVSLTLRRGE-----TLGLVGESGSGKSTLARLLLGLLRPTSG---SI-L 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 411 FNvsykpqGND--SKRECTVRQLLHD----------------KIRDACAHP----QFMSDVIRPLQIEQLMDQV------ 462
Cdd:COG1123 324 FD------GKDltKLSRRSLRELRRRvqmvfqdpysslnprmTVGDIIAEPlrlhGLLSRAERRERVAELLERVglppdl 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 463 ----VKTLSGGEKQRVAI--TLCLgKPaDIYLIDEPSAHLDseQRITAS--KVIKRfiLHAK--KTAFIVEHDFIMATYL 532
Cdd:COG1123 398 adryPHELSGGQRQRVAIarALAL-EP-KLLILDEPTSALD--VSVQAQilNLLRD--LQRElgLTYLFISHDLAVVRYI 471
|
490
....*....|.
gi 15231301 533 ADRVIV-YEGQ 542
Cdd:COG1123 472 ADRVAVmYDGR 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
373-578 |
6.91e-31 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 121.32 E-value: 6.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 373 DSQIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFN------------------------VSYKPQGND---SKRE 425
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeildefrgselqnyftkllegdvkVIVKPQYVDlipKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 CTVRQLLhDKIRDAcahpQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITAS 505
Cdd:cd03236 105 GKVGELL-KKKDER----GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 506 KVIKRFILHaKKTAFIVEHDFIMATYLADRVIVYEGQPAVKCIAHSPQSLLSGMNHFLSHL----NITFRRDPTNFR 578
Cdd:cd03236 180 RLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLDGYlpteNMRFREESIEFE 255
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
80-286 |
3.47e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 97.71 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGANGFKLHRLPIP-RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNtppdWEEILTHFRGSELQSYFIr 158
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDlYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL----LNGKPIKAKERRKSIGYV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 159 vveenlktaikPQHVDYI--KEVVRGNLGKMLEKLDERGL-MEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKA 235
Cdd:cd03226 77 -----------MQDVDYQlfTDSVREELLLGLKELDAGNEqAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15231301 236 DIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFV 286
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
80-289 |
6.05e-23 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 95.39 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGaNGFKLHRLPI-PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQSYFIR 158
Cdd:cd00267 2 IENLSFRYG-GRTALDNVSLtLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-----------LIDGKDIAKLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 159 VVEenlktaikpQHVDYIKevvrgnlgkmleklderglmeeicadmelnqvlerearQVSGGELQRFAIAAVFVKKADIY 238
Cdd:cd00267 70 ELR---------RRIGYVP--------------------------------------QLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15231301 239 MFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
349-540 |
7.49e-23 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 95.39 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTkQLGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqsEIpEFNvsykpqGNDSKRECtv 428
Cdd:cd00267 6 SFRYGGRT-ALDNVSLTLKAGEIV-----ALVGPNGSGKSTLLRAIAGLLKPTSG---EI-LID------GKDIAKLP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQLLHDKIrdacahpqfmsdvirplqieqlmdQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVI 508
Cdd:cd00267 68 LEELRRRI------------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|..
gi 15231301 509 KRFILHaKKTAFIVEHDFIMATYLADRVIVYE 540
Cdd:cd00267 124 RELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
80-276 |
8.83e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 95.58 E-value: 8.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGANgFKLHRLPI-PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEIltHFRGSELQSYfir 158
Cdd:cd03214 2 VENLSVGYGGR-TVLDDLSLsIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG---------EI--LLDGKDLASL--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 159 vveenlktaikpqhvdyikevvrgnlgKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIY 238
Cdd:cd03214 67 ---------------------------SPKELARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 239 MFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDL 276
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDL 158
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
101-284 |
2.22e-22 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 96.47 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-----FNTPPDWEEILTH--FRGSELQSYFIRVVEENLKtaikpqhv 173
Cdd:COG4555 25 KDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgEDVRKEPREARRQigVLPDERGLYDRLTVRENIR-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 174 dYIKEVvRGNLGKMLEKLderglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRL 253
Cdd:COG4555 97 -YFAEL-YGLFDEELKKR-----IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARR 169
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 254 KAAQVIRSLLRHDSYVIVVEHDLSVLDYLSD 284
Cdd:COG4555 170 LLREILRALKKEGKTVLFSSHIMQEVEALCD 200
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
101-289 |
2.79e-22 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 95.23 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYFIRvvEENLKTAIKPQHVDY----- 175
Cdd:cd03225 25 KKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSG---------EVL--VDGKDLTKLSLK--ELRRKVGLVFQNPDDqffgp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 --IKEVVRG--NLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQ 251
Cdd:cd03225 92 tvEEEVAFGleNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 15231301 252 RLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:cd03225 170 RRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
349-538 |
2.90e-22 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 95.23 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPN-MTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQGNDSKRECT 427
Cdd:cd03225 6 SFSYPDgARPALDDISLTIKKGEF-----VLIVGPNGSGKSTLLRLLNGLLGPTSG-EVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 V-----RQLLHDKIRDACA-HPQFM-----------SDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLID 490
Cdd:cd03225 80 VfqnpdDQFFGPTVEEEVAfGLENLglpeeeieervEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 491 EPSAHLDSEQRITASKVIKRfiLHAK-KTAFIVEHDFIMATYLADRVIV 538
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKK--LKAEgKTIIIVTHDLDLLLELADRVIV 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
370-555 |
3.90e-22 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 95.69 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 370 EFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF--NVSYKPQGNDSKRECTVRQ------LLH 433
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsilidgedVRKEPREArrQIGVLPDERGLYDRLTVREniryfaELY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 434 DKIRDACAhpQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFIL 513
Cdd:COG4555 103 GLFDEELK--KRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD----VMARRLLREILR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 514 HAKKTAFIV---EHDFIMATYLADRVI-------VYEGQPAVKCIAHSPQSL 555
Cdd:COG4555 177 ALKKEGKTVlfsSHIMQEVEALCDRVVilhkgkvVAQGSLDELREEIGEENL 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
102-540 |
4.64e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDW------------------EEILTHFRGselqsyfIRVVEEN 163
Cdd:COG0488 23 PGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigylpqeppldddltvlDTVLDGDAE-------LRALEAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 164 LkTAIKPQHVDYIKEVVRgnLGKMLEKLDERGL------MEEICADMELNQV-LEREARQVSGGELQRFAIAAVFVKKAD 236
Cdd:COG0488 96 L-EELEAKLAEPDEDLER--LAELQEEFEALGGweaearAEEILSGLGFPEEdLDRPVSELSGGWRRRVALARALLSEPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 237 IYMFDEPSSYLDvrqrlkaaqvIRS-------LLRHDSYVIVVEHDLSVLDylsdfvcclygkpgayGVVTLPFSV-REG 308
Cdd:COG0488 173 LLLLDEPTNHLD----------LESiewleefLKNYPGTVLVVSHDRYFLD----------------RVATRILELdRGK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 309 INVFLAGFipTENLRFRDESLT----------------------FRV--SETTQeNDGEVKSYA---------RYKYPNM 355
Cdd:COG0488 227 LTLYPGNY--SAYLEQRAERLEqeaaayakqqkkiakeeefirrFRAkaRKAKQ-AQSRIKALEklereepprRDKTVEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 356 ----TKQLG--------------------DFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqsEI--- 408
Cdd:COG0488 304 rfppPERLGkkvleleglsksygdktlldDLSLRIDRGD-----RIGLIGPNGAGKSTLLKLLAGELEPDSG---TVklg 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 409 PEFNVSYKPQ-----------------GNDSKRECTVRQLLHDkirdacahpqFM---SDVirplqieqlmDQVVKTLSG 468
Cdd:COG0488 376 ETVKIGYFDQhqeeldpdktvldelrdGAPGGTEQEVRGYLGR----------FLfsgDDA----------FKPVGVLSG 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 469 GEKQRVAITLCLGKPADIYLIDEPSAHLDseqriTASK-VIKRFILHAKKTAFIVEHD--FIMAtyLADRVIVYE 540
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLD-----IETLeALEEALDDFPGTVLLVSHDryFLDR--VATRILEFE 503
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
101-276 |
1.35e-21 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 94.34 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSY----FIRVVeenlktAIKPQHVDY- 175
Cdd:COG1120 25 PPGEVTALLGPNGSGKSTLLRALAGLLKPSSG---------EVL--LDGRDLASLsrreLARRI------AYVPQEPPAp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 ----IKEVV-------RGNLGKMLEKlDERgLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:COG1120 88 fgltVRELValgryphLGLFGRPSAE-DRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190
....*....|....*....|....*....|...
gi 15231301 245 SYLDVRQRLKAAQVIRSLLRHDSY-VIVVEHDL 276
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLARERGRtVVMVLHDL 198
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
359-538 |
1.41e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 92.11 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqsEIpEFNvsykpqGNDskrectVRQLLHDKIRD 438
Cdd:cd03214 15 LDDLSLSIEAGEIV-----GILGPNGAGKSTLLKTLAGLLKPSSG---EI-LLD------GKD------LASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 439 ACAhpqFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKT 518
Cdd:cd03214 74 KIA---YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKT 150
|
170 180
....*....|....*....|
gi 15231301 519 AFIVEHDFIMATYLADRVIV 538
Cdd:cd03214 151 VVMVLHDLNLAARYADRVIL 170
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
359-538 |
3.15e-21 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 92.32 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQgndSKRECT-VRQLL----H 433
Cdd:cd03301 16 LDDLNLDIADGEF-----VVLLGPSGCGKTTTLRMIAGLEEPTSG-RIYIGGRDVTDLPP---KDRDIAmVFQNYalypH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 434 DKIRDACAHP------------QFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQR 501
Cdd:cd03301 87 MTVYDNIAFGlklrkvpkdeidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 502 ITASKVIKRfiLHAK-KTAFI-VEHDFIMATYLADRVIV 538
Cdd:cd03301 167 VQMRAELKR--LQQRlGTTTIyVTHDQVEAMTMADRIAV 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
359-538 |
6.53e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.42 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEG---------VQSEIPEF--NVSYKPQgndskrECt 427
Cdd:COG4619 16 LSPVSLTLEAGEC-----VAITGPSGSGKSTLLRALADLDPPTSGeiyldgkplSAMPPPEWrrQVAYVPQ------EP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 vrQLLHDKIRDACAHP-QFMSDVIRPLQIEQLMDQV----------VKTLSGGEKQRVAI--TLCLGKpaDIYLIDEPSA 494
Cdd:COG4619 84 --ALWGGTVRDNLPFPfQLRERKFDRERALELLERLglppdildkpVERLSGGERQRLALirALLLQP--DVLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 495 HLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
354-538 |
6.66e-21 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 92.01 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFKLEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF-NVSYKPQGNDSKR 424
Cdd:cd03299 5 NLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkillngkdITNLPPEKrDISYVPQNYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 ECTV--------RQLLHDKIRDacahPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHL 496
Cdd:cd03299 85 HMTVykniayglKKRKVDKKEI----ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15231301 497 DSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAI 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
70-284 |
7.23e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 91.66 E-value: 7.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 70 IQIINLpkdlakdtTHRYGA----NGFKLHrlpIPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-----FNTPPDW 140
Cdd:COG1131 1 IEVRGL--------TKRYGDktalDGVSLT---VE-PGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgEDVARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 141 EEILTHFrGSELQSYFirvVEENLkTAIkpQHVDYIKEvVRGnlgkmLEKLDERGLMEEICADMELNQVLEREARQVSGG 220
Cdd:COG1131 69 AEVRRRI-GYVPQEPA---LYPDL-TVR--ENLRFFAR-LYG-----LPRKEARERIDELLELFGLTDAADRKVGTLSGG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 221 ELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSD 284
Cdd:COG1131 136 MKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCD 199
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
101-245 |
1.11e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 88.86 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNTPPDWEEILTHFRG-----SELQSYFIRV-VEENLKTAIKPQH 172
Cdd:pfam00005 9 NPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilLDGQDLTDDERKSLRKeigyvFQDPQLFPRLtVRENLRLGLLLKG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 173 VDYIKEVVRgnLGKMLEKLDERGLmeeicadmeLNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:pfam00005 89 LSKREKDAR--AEEALEKLGLGDL---------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
354-538 |
1.19e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 91.28 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF--NVSYKP 417
Cdd:COG1131 5 GLTKRYGDKTaldgvsLTVEPGE-----IFGLLGPNGAGKTTTIRMLLGLLRPTSGevrvlgedVARDPAEVrrRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 418 QGNDSKRECTVRQLL--HDKIRDacahpqfMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPADI 486
Cdd:COG1131 80 QEPALYPDLTVRENLrfFARLYG-------LPRKEARERIDELLELFgltdaadrkVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 487 YLIDEPSAHLDSEQRitasKVIKRFILHAK---KTAFIVEHdfIM--ATYLADRVIV 538
Cdd:COG1131 153 LILDEPTSGLDPEAR----RELWELLRELAaegKTVLLSTH--YLeeAERLCDRVAI 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
102-287 |
2.49e-20 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 89.51 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQsyfirvvEENLKTAIKPQH--VDY---- 175
Cdd:cd03235 24 PGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----------RVFGKPLE-------KERKRIGYVPQRrsIDRdfpi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 -IKEVVR-GNLGKM-----LEKLDERgLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:cd03235 86 sVRDVVLmGLYGHKglfrrLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15231301 249 VRQRLKAAQVIRSLLRHDSYVIVVEHDL-SVLDYLSDFVC 287
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLL 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
350-541 |
1.46e-19 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 86.28 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-LGDFKLEVMEGEFTdsqIIVmlGENGTGKTTFIRMLAGAFPREEGvqsEIpEFNvsykpqGNDskrectV 428
Cdd:cd03228 8 FSYPGRPKPvLKDVSLTIKPGEKV---AIV--GPSGSGKSTLLKLLLRLYDPTSG---EI-LID------GVD------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQLLHDKIRDACA----HPQFMSDVIRplqiEQLmdqvvktLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD--SEQRI 502
Cdd:cd03228 67 RDLDLESLRKNIAyvpqDPFLFSGTIR----ENI-------LSGGQRQRIAIARALLRDPPILILDEATSALDpeTEALI 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 503 TasKVIKRfiLHAKKTAFIVEHDFIMATyLADRVIVYEG 541
Cdd:cd03228 136 L--EALRA--LAKGKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
70-291 |
2.40e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 87.18 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 70 IQIINLPKDLAKDTTHRYGANGFKLHrlpIpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNtppdwEEILTHF 147
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFS---I-KKGETLGLVGESGSGKSTLARAILGLLKPTSGSiiFD-----GKDLLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 148 RGSELQSYF--IRVVEENLKTAIKPQHV--DYIKEVVRGNLGKMLEKLDERGLMEEICAdMELN-QVLEREARQVSGGEL 222
Cdd:cd03257 73 SRRLRKIRRkeIQMVFQDPMSSLNPRMTigEQIAEPLRIHGKLSKKEARKEAVLLLLVG-VGLPeEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 223 QRFAIAAVFVKKADIYMFDEPSSYLDVrqrLKAAQVIRsLLR--HDSY---VIVVEHDLSVLDYLSDFVCCLYG 291
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDV---SVQAQILD-LLKklQEELgltLLFITHDLGVVAKIADRVAVMYA 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
359-544 |
2.96e-19 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 87.41 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEG-VQ------SEIP--EF--NVSYKPQGNDSKRECT 427
Cdd:COG1120 17 LDDVSLSLPPGEVT-----ALLGPNGSGKSTLLRALAGLLKPSSGeVLldgrdlASLSrrELarRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQLL------------------HDKIRDAcahpqfmsdvIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLI 489
Cdd:COG1120 92 VRELValgryphlglfgrpsaedREAVEEA----------LERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 490 DEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRV-------IVYEGQPA 544
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLvllkdgrIVAQGPPE 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
101-297 |
5.63e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 86.68 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilthfrgselqsyfIRVVEENLKTAIK-----PQHVDY 175
Cdd:COG1121 30 PPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT-----------------------VRLFGKPPRRARRrigyvPQRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 -------IKEVV------RGNLGKMLEKLDeRGLMEEICADMELnqvLEREARQV---SGGELQRFAIAAVFVKKADIYM 239
Cdd:COG1121 87 dwdfpitVRDVVlmgrygRRGLFRRPSRAD-REAVDEALERVGL---EDLADRPIgelSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 240 FDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAYG 297
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHG 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
354-538 |
7.53e-19 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 84.37 E-value: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIPEFNVSYKPQGNDSKRECT 427
Cdd:cd03230 5 NLSKRYGKKTalddisLTVEKGE-----IYGLLGPNGAGKTTLIKIILGLLKPDSG---EIKVLGKDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VrqlLHDkirdacaHPQFMSDvirpLQIEQLMDqvvktLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKV 507
Cdd:cd03230 77 Y---LPE-------EPSLYEN----LTVRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 508 IKRfILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:cd03230 138 LRE-LKKEGKTILLSSHILEEAERLCDRVAI 167
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
101-280 |
1.13e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 89.43 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNTPPdweeiLTHFRGSELQSYFIRVveenlktaikPQHVDYIKE 178
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSilINGVD-----LSDLDPASWRRQIAWV----------PQNPYLFAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 VVRGNLG---------KMLEKLDERGLMEEIcadMELNQVLERE----ARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:COG4988 426 TIRENLRlgrpdasdeELEAALEAAGLDEFV---AALPDGLDTPlgegGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190
....*....|....*....|....*....|....*..
gi 15231301 246 YLDVR--QRLKAAqvIRSLLRHDSyVIVVEHDLSVLD 280
Cdd:COG4988 503 HLDAEteAEILQA--LRRLAKGRT-VILITHRLALLA 536
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
101-284 |
2.14e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 84.85 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNTPPDWEEILTHFRGSelqsyfIRVVEENLKTAIKPQH-VDY-I 176
Cdd:COG1124 29 APGESFGLVGESGSGKSTLLRALAGLERPWSGEvtFDGRPVTRRRRKAFRRR------VQMVFQDPYASLHPRHtVDRiL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEVVRGnlgkmLEKLDERGLMEEICADMELN-QVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVrqrLKA 255
Cdd:COG1124 103 AEPLRI-----HGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDV---SVQ 174
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 256 AQVIRSL--LRHD---SYVIvVEHDLSVLDYLSD 284
Cdd:COG1124 175 AEILNLLkdLREErglTYLF-VSHDLAVVAHLCD 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-537 |
2.42e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 83.85 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIpEFNVSYKPQGNDSKR----- 424
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGE-----IIALTGKNGAGKTTLAKILAGLIKESSG---SI-LLNGKPIKAKERRKSigyvm 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 --------ECTVRQLLHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAI--TLCLGKpaDIYLIDEPSA 494
Cdd:cd03226 78 qdvdyqlfTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIaaALLSGK--DLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15231301 495 HLDSEQRITASKVIKRfILHAKKTAFIVEHDFIMATYLADRVI 537
Cdd:cd03226 156 GLDYKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
349-538 |
2.82e-18 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 84.31 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKPQGNDSKREC-- 426
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEF-----VAIIGPNGSGKSTLLRLLNGLLKPTSG------EVLVDGKDITKKNLRELrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 ----------------TVRQ----------LLHDKIRDACAhpqfmsDVIRPLQIEQLMDQVVKTLSGGEKQRVAI--TL 478
Cdd:COG1122 76 kvglvfqnpddqlfapTVEEdvafgpenlgLPREEIRERVE------EALELVGLEHLADRPPHELSGGQKQRVAIagVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 479 CLgKPaDIYLIDEPSAHLDSEQRITASKVIKRfiLHAKKTAFI-VEHDFIMATYLADRVIV 538
Cdd:COG1122 150 AM-EP-EVLVLDEPTAGLDPRGRRELLELLKR--LNKEGKTVIiVTHDLDLVAELADRVIV 206
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
100-291 |
3.11e-18 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 84.87 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 100 PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNtppdweeilthFRGSELQSYFIRvvEENLKTAIKPQHVD----- 174
Cdd:TIGR03873 24 APPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-----------LAGVDLHGLSRR--ARARRVALVEQDSDtavpl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 YIKEVV-------RGNLGkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYL 247
Cdd:TIGR03873 91 TVRDVValgriphRSLWA--GDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 248 DVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYG 291
Cdd:TIGR03873 169 DVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDG 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
359-538 |
5.09e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 82.95 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF-NVSYKPQG-----NDSKR 424
Cdd:cd03259 16 LDDLSLTVEPGEFL-----ALLGPSGCGKTTLLRLIAGLERPDSGeilidgrdVTGVPPERrNIGMVFQDyalfpHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 E-----CTVRQLLHDKIRDAcahpqfMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:cd03259 91 EniafgLKLRGVPKAEIRAR------VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 500 QRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAV 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
359-537 |
5.14e-18 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 82.97 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsQIIvmlGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKPQGNDSKR----------EC-- 426
Cdd:cd03235 15 LEDVSFEVKPGEFL--AIV---GPNGAGKSTLLKAILGLLKPTSG------SIRVFGKPLEKERKRigyvpqrrsiDRdf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 --TVRQL----------LHDKIRDACahpqfMSDVIRPLQ---IEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDE 491
Cdd:cd03235 84 piSVRDVvlmglyghkgLFRRLSKAD-----KAKVDEALErvgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 492 PSAHLDSEQRITASKVIKRfiLHAK-KTAFIVEHDFIMATYLADRVI 537
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRE--LRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
359-538 |
7.16e-18 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 81.46 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqsEIpEFNvsykpqGNDSKRECTVRQLLHDKIRD 438
Cdd:cd03229 16 LNDVSLNIEAGEIV-----ALLGPSGSGKSTLLRCIAGLEEPDSG---SI-LID------GEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 439 ACAHPQFMS--DVirplqieqlMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfiLHAK 516
Cdd:cd03229 81 VFQDFALFPhlTV---------LENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKS--LQAQ 149
|
170 180
....*....|....*....|....
gi 15231301 517 --KTAFIVEHDFIMATYLADRVIV 538
Cdd:cd03229 150 lgITVVLVTHDLDEAARLADRVVV 173
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
101-276 |
1.64e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---FNTPpdweeiLTHFRGSELQSyfIRvveenlktAIKPQHVDY-- 175
Cdd:PRK13548 26 RPGEVVAILGPNGAGKSTLLRALSGELSPDSGEvrlNGRP------LADWSPAELAR--RR--------AVLPQHSSLsf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 ---IKEVVRgnLGKM---LEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFV------KKADIYMFDEP 243
Cdd:PRK13548 90 pftVEEVVA--MGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 244 SSYLDVRQRLKAAQVIRSLLRHDSY-VIVVEHDL 276
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLaVIVVLHDL 201
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-544 |
2.96e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEG---VQSEIPEFN---VSYKPQGNDSKRE--CTVRQLL--- 432
Cdd:COG1121 27 LTIPPGEFV-----AIVGPNGAGKSTLLKAILGLLPPTSGtvrLFGKPPRRArrrIGYVPQRAEVDWDfpITVRDVVlmg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 433 ---------------HDKIRDAcahpqfMSDVirplQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD 497
Cdd:COG1121 102 rygrrglfrrpsradREAVDEA------LERV----GLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 498 --SEQRITAskVIKRfiLHAK-KTAFIVEHDFIMATYLADRVI------VYEGQPA 544
Cdd:COG1121 172 aaTEEALYE--LLRE--LRREgKTILVVTHDLGAVREYFDRVLllnrglVAHGPPE 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
349-538 |
3.52e-17 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 85.27 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYP-NMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqsEI-----------PEF---NV 413
Cdd:COG2274 480 SFRYPgDSPPVLDNISLTIKPGER-----VAIVGRSGSGKSTLLKLLLGLYEPTSG---RIlidgidlrqidPASlrrQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 414 SYKPQGNdskrectvrQLLHDKIRD--ACAHPQF-MSDVIRPLQ-------IEQL---MDQVV----KTLSGGEKQRVAI 476
Cdd:COG2274 552 GVVLQDV---------FLFSGTIREniTLGDPDAtDEEIIEAARlaglhdfIEALpmgYDTVVgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 477 TLCLGKPADIYLIDEPSAHLD--SEQRITASkvIKRFIlhAKKTAFIVEHDfiMAT-YLADRVIV 538
Cdd:COG2274 623 ARALLRNPRILILDEATSALDaeTEAIILEN--LRRLL--KGRTVIIIAHR--LSTiRLADRIIV 681
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
101-280 |
6.85e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 84.05 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---FNTPpdweeiLTHFRGSELQSYfIRVVeenlktaikPQHVDYIK 177
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlGGVD------LRDLDEDDLRRR-IAVV---------PQRPHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 178 EVVRGNL---------GKMLEKLDERGLMEEICADME-LNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYL 247
Cdd:COG4987 423 TTLRENLrlarpdatdEELWAALERVGLGDWLAALPDgLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190
....*....|....*....|....*....|....*
gi 15231301 248 DvrqRLKAAQVIRSLLRH--DSYVIVVEHDLSVLD 280
Cdd:COG4987 503 D---AATEQALLADLLEAlaGRTVLLITHRLAGLE 534
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
101-292 |
7.53e-17 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 80.17 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQSY-------------F--IRV-----V 160
Cdd:cd03219 24 RPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-----------LFDGEDITGLppheiarlgigrtFqiPRLfpeltV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 161 EENLKTAIKPQHVDYIkevVRGNLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMF 240
Cdd:cd03219 93 LENVMVAAQARTGSGL---LLARARREEREARER--AEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 241 DEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL-YGK 292
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLdQGR 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
101-289 |
8.10e-17 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 80.07 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQsyfirvvEENLKTAIK-----PQHVDY 175
Cdd:COG1122 25 EKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG---------EVL--VDGKDIT-------KKNLRELRRkvglvFQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 --IKEVVR-----G--NLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:COG1122 87 qlFAPTVEedvafGpeNLGLPREEIRER--VEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15231301 247 LDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:COG1122 165 LDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVL 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
359-542 |
1.00e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 77.10 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFNVSYKPQgndskrectvrqllhdkird 438
Cdd:cd03221 16 LKDISLTINPGD-----RIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 439 acahpqfmsdvirplqieqlmdqvvktLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFILHAKKT 518
Cdd:cd03221 71 ---------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIEALEEALKEYPGT 119
|
170 180
....*....|....*....|....
gi 15231301 519 AFIVEHDFIMATYLADRVIVYEGQ 542
Cdd:cd03221 120 VILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
80-281 |
1.06e-16 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 79.46 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGANGFKLHRLPIP----RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-----FNTPPDWEEILTHFRGS 150
Cdd:cd03255 3 LKNLSKTYGGGGEKVQALKGVslsiEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgTDISKLSEKELAAFRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 151 EL----QSYFI---RVVEENLKTAIKPQHVDyiKEVVRGNLGKMLEKLDerglmeeicadmeLNQVLEREARQVSGGELQ 223
Cdd:cd03255 83 HIgfvfQSFNLlpdLTALENVELPLLLAGVP--KKERRERAEELLERVG-------------LGDRLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 224 RFAIAAVFVKKADIYMFDEPSSYLDVrqrlKAAQVIRSLLR--HDSY---VIVVEHDLSVLDY 281
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDS----ETGKEVMELLRelNKEAgttIVVVTHDPELAEY 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
359-494 |
1.55e-16 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 76.92 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF---NVSYKPQGNDSKRECT 427
Cdd:pfam00005 1 LKNVSLTLNPGE-----ILALVGPNGAGKSTLLKLIAGLLSPTEGtilldgqdLTDDERKSlrkEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 428 VR---------QLLHDKIRDACAHpQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSA 494
Cdd:pfam00005 76 VRenlrlglllKGLSKREKDARAE-EALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
364-525 |
1.84e-16 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 78.29 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF--NVSYKPQGNDSKRECTVRQLLH 433
Cdd:COG4133 23 FTLAAGE-----ALALTGPNGSGKTTLLRILAGLLPPSAGevlwngepIRDAREDYrrRLAYLGHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 434 ------------DKIRDACAHpqfmsdvirpLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQR 501
Cdd:COG4133 98 fwaalyglradrEAIDEALEA----------VGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 15231301 502 ITASKVIKRFiLHAKKTAFIVEHD 525
Cdd:COG4133 168 ALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
81-277 |
1.84e-16 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 78.33 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGA----NGFKLHrlpiPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--------FNTPPDWEEILTHFr 148
Cdd:cd03259 4 KGLSKTYGSvralDDLSLT----VEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvTGVPPERRNIGMVF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 149 gselQSYFI---RVVEENLKTAIKPQHVDyiKEVVRGNLGKMLEKLDERGLmeeicadmelnqvLEREARQVSGGELQRF 225
Cdd:cd03259 79 ----QDYALfphLTVAENIAFGLKLRGVP--KAEIRARVRELLELVGLEGL-------------LNRYPHELSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 226 AIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDLS 277
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQReLGITTIYVTHDQE 192
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
101-286 |
1.86e-16 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 77.44 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilthfrgselqsyfIRVVEENLKTAikpqhvdyiKEVV 180
Cdd:cd03230 24 EKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE-----------------------IKVLGKDIKKE---------PEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNLGKMLEkldERGLMEEICAdmelnqvleREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIR 260
Cdd:cd03230 72 KRRIGYLPE---EPSLYENLTV---------RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR 139
|
170 180
....*....|....*....|....*.
gi 15231301 261 SLLRHDSYVIVVEHDLSVLDYLSDFV 286
Cdd:cd03230 140 ELKKEGKTILLSSHILEEAERLCDRV 165
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
102-280 |
2.84e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.95 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDweeilthfrgselqsyfirvveenlktaIKPQHVDyikevvr 181
Cdd:cd03221 25 PGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------------------------VKIGYFE------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 182 gnlgkmleklderglmeeicadmelnqvlerearQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRlkaAQVIRS 261
Cdd:cd03221 70 ----------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI---EALEEA 112
|
170
....*....|....*....
gi 15231301 262 LLRHDSYVIVVEHDLSVLD 280
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLD 131
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
359-544 |
3.39e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 77.90 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFP------REEGVQSEIPEFNVSYKPQgNDS----KrecTV 428
Cdd:cd03293 20 LEDISLSVEEGEF-----VALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQ-QDAllpwL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQ--LLHDKIrdacahpQFMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLCL-GKPaDIYLIDEPSAHL 496
Cdd:cd03293 91 LDnvALGLEL-------QGVPKAEARERAEELLELVglsgfenayPHQLSGGMRQRVALARALaVDP-DVLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231301 497 DSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQPA 544
Cdd:cd03293 163 DALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPG 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
350-538 |
3.51e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 81.73 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGEFTdsqIIVmlGENGTGKTTFIRMLAGAFPREEGV----QSEIPEF-------NVSYKPQ 418
Cdd:COG4988 344 FSYPGGRPALDGLSLTIPPGERV---ALV--GPSGAGKSTLLNLLLGFLPPYSGSilinGVDLSDLdpaswrrQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 gnDSkrectvrQLLHDKIRD--ACAHPQF-MSDVIRPLQ-------IEQL---MDQVV----KTLSGGEKQRVAITLCLG 481
Cdd:COG4988 419 --NP-------YLFAGTIREnlRLGRPDAsDEELEAALEaagldefVAALpdgLDTPLgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 482 KPADIYLIDEPSAHLD--SEQRITASkvIKRfiLHAKKTAFIVEHDfIMATYLADRVIV 538
Cdd:COG4988 490 RDAPLLLLDEPTAHLDaeTEAEILQA--LRR--LAKGRTVILITHR-LALLAQADRILV 543
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
354-538 |
3.95e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.12 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAG---------AF---------PREEGV----Q 405
Cdd:COG3839 8 NVSKSYGGVEalkdidLDIEDGEF-----LVLLGPSGCGKSTLLRMIAGledptsgeiLIggrdvtdlpPKDRNIamvfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 406 S----------EipefNVSY--KPQGnDSKREctVRQllhdKIRDACAhpqfMsdvirpLQIEQLMDQVVKTLSGGEKQR 473
Cdd:COG3839 83 SyalyphmtvyE----NIAFplKLRK-VPKAE--IDR----RVREAAE----L------LGLEDLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 474 VAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfiLHAK-KTAFI-VEHDFIMATYLADRVIV 538
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKR--LHRRlGTTTIyVTHDQVEAMTLADRIAV 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
103-544 |
4.48e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGklkpnLGRFntPPDWEEILTHFRGSELQSYFIR--VVEENLKT---AIKPQHVDYIK 177
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVLRG-----MDQY--EPTSGRIIYHVALCEKCGYVERpsKVGEPCPVcggTLEPEEVDFWN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 178 --EVVRGNLGK----MLEKL-----DERGL------MEEI--CADMELNQVLE------------REARQVSGGELQRFA 226
Cdd:TIGR03269 99 lsDKLRRRIRKriaiMLQRTfalygDDTVLdnvleaLEEIgyEGKEAVGRAVDliemvqlshritHIARDLSGGEKQRVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 227 IAAVFVKKADIYMFDEPSSYLDVrqrlKAAQVIRSLLR-----HDSYVIVVEHDLSVLDYLSDFVCCLygKPGAYGVVTL 301
Cdd:TIGR03269 179 LARQLAKEPFLFLADEPTGTLDP----QTAKLVHNALEeavkaSGISMVLTSHWPEVIEDLSDKAIWL--ENGEIKEEGT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 302 PFSVregINVFLAGFIPTEnlrfrdesltfRVSETTQEND-GEVKSYARYKYP---NMTKQLGDFKLEVMEGEftdsqII 377
Cdd:TIGR03269 253 PDEV---VAVFMEGVSEVE-----------KECEVEVGEPiIKVRNVSKRYISvdrGVVKAVDNVSLEVKEGE-----IF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 378 VMLGENGTGKTTFIRMLAGAFPREEG-VQSEIPEFNVSYKPQGNDSK-RECTVRQLLHDKIrDACAHPQFMSDVIRPLQI 455
Cdd:TIGR03269 314 GIVGTSGAGKTTLSKIIAGVLEPTSGeVNVRVGDEWVDMTKPGPDGRgRAKRYIGILHQEY-DLYPHRTVLDNLTEAIGL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 456 E-------------------------QLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqrITASKVIKR 510
Cdd:TIGR03269 393 ElpdelarmkavitlkmvgfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP---ITKVDVTHS 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15231301 511 fILHAKK----TAFIVEHDFIMATYLADRV-------IVYEGQPA 544
Cdd:TIGR03269 470 -ILKAREemeqTFIIVSHDMDFVLDVCDRAalmrdgkIVKIGDPE 513
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
102-287 |
4.98e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 77.34 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--------------FNTPPDWEEIlthfrGSELQSYfirvveenlktA 167
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtvlfdsrkkINLPPQQRKI-----GLVFQQY-----------A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 168 IKPqHVDyikevVRGNLG---KMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:cd03297 86 LFP-HLN-----VRENLAfglKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 245 SYLDVRQRLKAAQVIRSLLRH-DSYVIVVEHDLSVLDYLSDFVC 287
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIV 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
97-276 |
6.11e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 97 LPIPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQSYFIRVVEENLktAIKPQH---- 172
Cdd:PRK11231 23 LSLP-TGKITALIGPNGCGKSTLLKCFARLLTPQSGTV-----------FLGDKPISMLSSRQLARRL--ALLPQHhltp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 --------VDYIKEVVRGNLGKMLEklDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:PRK11231 89 egitvrelVAYGRSPWLSLWGRLSA--EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190
....*....|....*....|....*....|..
gi 15231301 245 SYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKTVVTVLHDL 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
351-555 |
8.09e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 76.77 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 351 KYPNMTKQ-LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFP--------REEGVQSEIPEF--NVSYKPQG 419
Cdd:cd03263 9 TYKKGTKPaVDDLSLNVYKGE-----IFGLLGHNGAGKTTTLKMLTGELRptsgtayiNGYSIRTDRKAArqSLGYCPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 420 NDSKRECTVRQLL---------HDKIRDACAHpqfmsDVIRPLQIEQLMDQVVKTLSGGEKQR--VAITLClGKPAdIYL 488
Cdd:cd03263 84 DALFDELTVREHLrfyarlkglPKSEIKEEVE-----LLLRVLGLTDKANKRARTLSGGMKRKlsLAIALI-GGPS-VLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 489 IDEPSAHLDSEQRitasKVIKRFILHAKK--TAFIVEHDFIMATYLADRV-IVYEGQpaVKCIAhSPQSL 555
Cdd:cd03263 157 LDEPTSGLDPASR----RAIWDLILEVRKgrSIILTTHSMDEAEALCDRIaIMSDGK--LRCIG-SPQEL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
359-544 |
9.20e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 77.44 E-value: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqsEI---------PEFNVSYKPQgNDS----Kre 425
Cdd:COG1116 27 LDDVSLTVAAGEF-----VALVGPSGCGKSTLLRLIAGLEKPTSG---EVlvdgkpvtgPGPDRGVVFQ-EPAllpwL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 cTVRQ--LLHDKIRDacahpqfMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAI--TLCLgKPaDIYLIDEP 492
Cdd:COG1116 96 -TVLDnvALGLELRG-------VPKAERRERARELLELVglagfedayPHQLSGGMRQRVAIarALAN-DP-EVLLMDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 493 SAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQPA 544
Cdd:COG1116 166 FGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPG 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
101-279 |
9.31e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 9.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilthfrgselqsyfiRVVEENLKTAIKPQHVDY----- 175
Cdd:NF040873 16 PAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT------------------------VRRAGGARVAYVPQRSEVpdslp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 --IKEVV-------RGNLGKMleKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:NF040873 72 ltVRDLVamgrwarRGLWRRL--TRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 15231301 247 LDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVL 279
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
341-502 |
1.22e-15 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 76.08 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 341 DGEVKSYARykypnmTKQLGDFKLEVMEGeftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEFN 412
Cdd:cd03264 4 ENLTKRYGK------KRALDGVSLTLGPG------MYGLLGPNGAGKTTLMRILATLTPPSSGtiridgqdVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 413 --VSYKPQGNDSKRECTVRQLLhdkirDACAHPQFMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLCL- 480
Cdd:cd03264 72 rrIGYLPQEFGVYPNFTVREFL-----DYIAWLKGIPSKEVKARVDEVLELVnlgdrakkkIGSLSGGMRRRVGIAQALv 146
|
170 180
....*....|....*....|..
gi 15231301 481 GKPaDIYLIDEPSAHLDSEQRI 502
Cdd:cd03264 147 GDP-SILIVDEPTAGLDPEERI 167
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
101-279 |
1.26e-15 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 80.26 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeILthFRGSELQSYFIRVVEENLktAIKPQHVDYIKEVV 180
Cdd:COG2274 499 KPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR---------IL--IDGIDLRQIDPASLRRQI--GVVLQDVFLFSGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNL---------GKMLEKLDERGLMEEICAD-MELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:COG2274 566 RENItlgdpdatdEEIIEAARLAGLHDFIEALpMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAE 645
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 251 QRlkaAQVIRSL--LRHDSYVIVVEHDLSVL 279
Cdd:COG2274 646 TE---AIILENLrrLLKGRTVIIIAHRLSTI 673
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
361-541 |
1.34e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 361 DFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAG------------------AFPREEGV----QSEI--PEFNVS-- 414
Cdd:PRK11000 21 DINLDIHEGEF-----VVFVGPSGCGKSTLLRMIAGleditsgdlfigekrmndVPPAERGVgmvfQSYAlyPHLSVAen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 415 ----YKPQGNDsKRECTVRqllhdkirdacahpqfMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLID 490
Cdd:PRK11000 96 msfgLKLAGAK-KEEINQR----------------VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 491 EPSAHLDS----EQRITASKVIKRFilhaKKTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:PRK11000 159 EPLSNLDAalrvQMRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
101-276 |
1.48e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.69 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---FNTPpdweeiLTHFRGSELQSyfIRvveenlktAIKPQHV---- 173
Cdd:COG4559 25 RPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvrlNGRP------LAAWSPWELAR--RR--------AVLPQHSslaf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 174 DY-IKEVVRgnLGKM---LEKLDERGLMEEICADMELNQVLEREARQVSGGELQR--FA--IAAVFVKKADI--YMF-DE 242
Cdd:COG4559 89 PFtVEEVVA--LGRAphgSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRvqLArvLAQLWEPVDGGprWLFlDE 166
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 243 PSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLARRGGGVVAVLHDL 200
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
101-280 |
1.82e-15 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 74.34 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYFIRVVEENLktAIKPQHV----DYI 176
Cdd:cd03228 26 KPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG---------EIL--IDGVDLRDLDLESLRKNI--AYVPQDPflfsGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEvvrgNLgkmleklderglmeeicadmelnqvlerearqVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQrlkAA 256
Cdd:cd03228 93 RE----NI--------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET---EA 133
|
170 180
....*....|....*....|....*.
gi 15231301 257 QVIRSL--LRHDSYVIVVEHDLSVLD 280
Cdd:cd03228 134 LILEALraLAKGKTVIVIAHRLSTIR 159
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
102-280 |
1.92e-15 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 75.21 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYFIRVveenlktaikPQHVDY------ 175
Cdd:COG4133 27 AGEALALTGPNGSGKTTLLRILAGLLPPSAG---------EVL--WNGEPIRDAREDY----------RRRLAYlghadg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IKEV--VRGNL---GKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:COG4133 86 LKPEltVRENLrfwAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190
....*....|....*....|....*....|
gi 15231301 251 QRLKAAQVIRSLLRHDSYVIVVEHDLSVLD 280
Cdd:COG4133 166 GVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
354-538 |
2.58e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 73.62 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKPQGNDSkrect 427
Cdd:cd03216 5 GITKRFGGVKaldgvsLSVRRGE-----VHALLGENGAGKSTLMKILSGLYKPDSG------EILVDGKEVSFAS----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 vrqllhdkIRDACAHPqfmsdvirplqIEqlmdqVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKV 507
Cdd:cd03216 69 --------PRDARRAG-----------IA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 508 IKRfiLHAKKTAFI-VEHDF--IMAtyLADRVIV 538
Cdd:cd03216 125 IRR--LRAQGVAVIfISHRLdeVFE--IADRVTV 154
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
103-322 |
7.17e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 74.29 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWEEIlthfrGSELQSYFI---RVVEENLKTAIKPQ 171
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditNLPPEKRDI-----SYVPQNYALfphMTVYKNIAYGLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HVDY--IKEVVRgnlgkmleklderglmeEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDV 249
Cdd:cd03299 100 KVDKkeIERKVL-----------------EIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 250 RQRLKaaqvIRSLLR--HDSY---VIVVEHDLSVLDYLSDFVCCLY-GKPGAYGVVTLPFSvrEGINVFLAGFIPTENL 322
Cdd:cd03299 163 RTKEK----LREELKkiRKEFgvtVLHVTHDFEEAWALADKVAIMLnGKLIQVGKPEEVFK--KPKNEFVAEFLGFNNI 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
77-289 |
8.34e-15 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 73.70 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 77 KDLAKDTTHRYGANGFKLhRLpipRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYF 156
Cdd:COG4619 4 EGLSFRVGGKPILSPVSL-TL---EAGECVAITGPSGSGKSTLLRALADLDPPTSG---------EIY--LDGKPLSAMP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 157 I-----RV-------------VEENLKTAIKPQHVDYIKEVVRgnlgKMLEKLderGLMEEIcadmelnqvLEREARQVS 218
Cdd:COG4619 69 PpewrrQVayvpqepalwggtVRDNLPFPFQLRERKFDRERAL----ELLERL---GLPPDI---------LDKPVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 219 GGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLL-RHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
357-544 |
9.68e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 73.48 E-value: 9.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 357 KQLGDFKLEVmegEFT-DSQIIVMLGENGTGKTTFIRMLAGAFPREEG---------VQSEIPEF------NVSYKPQGN 420
Cdd:cd03297 8 KRLPDFTLKI---DFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngtvlFDSRKKINlppqqrKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 421 DSKRECTVRQLLhdkirdACAHPQF--MSDVIRP------LQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEP 492
Cdd:cd03297 85 ALFPHLNVRENL------AFGLKRKrnREDRISVdelldlLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 493 SAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYE-GQPA 544
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEdGRLQ 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-556 |
1.02e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 75.92 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFKLEVMEgEFTDSQIIVMLGENGTGKTTFIRMLAGA---------------FPREEGVQSEIPEFNVSYKPQ 418
Cdd:TIGR02142 4 RFSKRLGDFSLDADF-TLPGQGVTAIFGRSGSGKTTLIRLIAGLtrpdegeivlngrtlFDSRKGIFLPPEKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 GNDSKRECTVRQLLHDKIRDACAHPQFMSD--VIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHL 496
Cdd:TIGR02142 83 EARLFPHLSVRGNLRYGMKRARPSERRISFerVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 497 DSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYE--------------GQPAVKCIAHSPQSLL 556
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEdgrvaaagpiaevwASPDLPWLAREDQGSL 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
80-277 |
1.45e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 73.00 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGaNGFKLHRLPIPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeilthfrgsELQSYFIRV 159
Cdd:cd03264 3 LENLTKRYG-KKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTI----------------RIDGQDVLK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 160 VEENLKTAIK--PQHVDYIKEV-VRGNLGKM--LEKLDERGLMEEICADME---LNQVLEREARQVSGGELQRFAIAAVF 231
Cdd:cd03264 66 QPQKLRRRIGylPQEFGVYPNFtVREFLDYIawLKGIPSKEVKARVDEVLElvnLGDRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 232 VKKADIYMFDEPSSYLDVRQRLKaaqvIRSLLRH---DSYVIVVEHDLS 277
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIR----FRNLLSElgeDRIVILSTHIVE 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
349-555 |
1.48e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 76.48 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKQ-LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIpEFN--------------- 412
Cdd:COG1123 11 SVRYPGGDVPaVDGVSLTIAPGET-----VALVGESGSGKSTLALALMGLLPHGGRISGEV-LLDgrdllelsealrgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 413 VSYKPQGNDSKREC-TVRQLLHDKIRDACAHPQFMSD-VIRPLQ---IEQLMDQVVKTLSGGEKQRVAITLCLGKPADIY 487
Cdd:COG1123 85 IGMVFQDPMTQLNPvTVGDQIAEALENLGLSRAEARArVLELLEavgLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 488 LIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV-YEG----QPAVKCIAHSPQSL 555
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVmDDGriveDGPPEEILAAPQAL 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
352-538 |
1.61e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 76.56 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 352 YPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGVQS----EIPEFN-------VSYKPQG- 419
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGE-----RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvPLADADadswrdqIAWVPQHp 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 420 ---NDSKREcTVR--------QLLHDKIRDACAHpQFMSDviRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYL 488
Cdd:TIGR02857 406 flfAGTIAE-NIRlarpdasdAEIREALERAGLD-EFVAA--LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15231301 489 IDEPSAHLDSEqriTASKVIKRFILHAK-KTAFIVEHDfIMATYLADRVIV 538
Cdd:TIGR02857 482 LDEPTAHLDAE---TEAEVLEALRALAQgRTVLLVTHR-LALAALADRIVV 528
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
373-538 |
1.70e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 72.79 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 373 DSQIIVMLGENGTGKTTFIRMLAGAFPREEGVqSEIPEFNVSYKPQG--------NDSKR---ECTVRQL------LHDK 435
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGF-ATVDGFDVVKEPAEarrrlgfvSDSTGlydRLTARENleyfagLYGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 436 IRDACAhpQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFILHA 515
Cdd:cd03266 109 KGDELT--ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD----VMATRALREFIRQL 182
|
170 180
....*....|....*....|....*.
gi 15231301 516 K---KTAFIVEHDFIMATYLADRVIV 538
Cdd:cd03266 183 RalgKCILFSTHIMQEVERLCDRVVV 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
97-275 |
2.19e-14 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 72.29 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 97 LPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWEEILTHFrgselQSYFI---RVVEENLK 165
Cdd:cd03301 21 LDIAD-GEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRDIAMVF-----QNYALyphMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 166 TAIKPQHV--DYIKEVVRgNLGKMLEklderglmeeicadmeLNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEP 243
Cdd:cd03301 95 FGLKLRKVpkDEIDERVR-EVAELLQ----------------IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|...
gi 15231301 244 SSYLDVRQRLKAAQVIRSLL-RHDSYVIVVEHD 275
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQqRLGTTTIYVTHD 190
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
101-542 |
2.30e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.02 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNlgrfntpPDWE-EIltHFRGSELQSYFIRVVEENlKTAIKPQHVDYIKEV 179
Cdd:TIGR02633 25 RPGECVGLCGENGAGKSTLMKILSG-VYPH-------GTWDgEI--YWSGSPLKASNIRDTERA-GIVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 -VRGNLGKMLEKLDERGLM---------EEICADMELNQV-LEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:TIGR02633 94 sVAENIFLGNEITLPGGRMaynamylraKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 249 VRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLygKPGAYgVVTLPFSV--REGINVFLAG-----FIPTEN 321
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI--RDGQH-VATKDMSTmsEDDIITMMVGreitsLYPHEP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 322 LRFRDESLtfrvsettqendgEVKSYARYKYPN-MTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFP- 399
Cdd:TIGR02633 251 HEIGDVIL-------------EARNLTCWDVINpHRKRVDDVSFSLRRGE-----ILGVAGLVGAGRTELVQALFGAYPg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 400 REEG--------VQSEIP----EFNVSYKPQgnDSKRECTVRQLLHDK--------------IRDACAHPQFMSDVIRPL 453
Cdd:TIGR02633 313 KFEGnvfingkpVDIRNPaqaiRAGIAMVPE--DRKRHGIVPILGVGKnitlsvlksfcfkmRIDAAAELQIIGSAIQRL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 454 QIEQLM-DQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIkrFILHAKKTAFIV-EHDFIMATY 531
Cdd:TIGR02633 391 KVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLI--NQLAQEGVAIIVvSSELAEVLG 468
|
490
....*....|..
gi 15231301 532 LADRVIV-YEGQ 542
Cdd:TIGR02633 469 LSDRVLViGEGK 480
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
364-537 |
6.03e-14 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 71.37 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQGNDSK----------------RECT 427
Cdd:cd03255 25 LSIEKGEFV-----AIVGPSGSGKSTLLNILGGLDRPTSG-EVRVDGTDISKLSEKELAAfrrrhigfvfqsfnllPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQ-----LLHDKIRDACAHPQFMsDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEqri 502
Cdd:cd03255 99 ALEnvelpLLLAGVPKKERRERAE-ELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE--- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 15231301 503 TASKVIKRFI-LHAK--KTAFIVEHDFIMATYlADRVI 537
Cdd:cd03255 175 TGKEVMELLReLNKEagTTIVVVTHDPELAEY-ADRII 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
101-279 |
6.33e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 74.63 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFN---------TPPDWEEILTH-------FRGSelqsyfirvVEENL 164
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladaDADSWRDQIAWvpqhpflFAGT---------IAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 165 KTAIKPQHVDYIKEVVRgnLGKMLEKLDERGLMeeicadmeLNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:TIGR02857 417 RLARPDASDAEIREALE--RAGLDEFVAALPQG--------LDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|....*..
gi 15231301 245 SYLDvrqRLKAAQVIRSLLRHDS--YVIVVEHDLSVL 279
Cdd:TIGR02857 487 AHLD---AETEAEVLEALRALAQgrTVLLVTHRLALA 520
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
80-291 |
7.31e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 72.15 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGANGF--KLHRLPI-------PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLG--RFNTPPdweeiLTHFR 148
Cdd:TIGR02769 5 VRDVTHTYRTGGLfgAKQRAPVltnvslsIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGtvSFRGQD-----LYQLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 149 GSELQSYF--IRVVEENLKTAIKPQHVdyIKEVVRGNLgKMLEKLDERGLMEEICADMEL----NQVLEREARQVSGGEL 222
Cdd:TIGR02769 80 RKQRRAFRrdVQLVFQDSPSAVNPRMT--VRQIIGEPL-RHLTSLDESEQKARIAELLDMvglrSEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 223 QRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHD--SYVIVVeHDLSVLDYLSDFVCCLYG 291
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFIT-HDLRLVQSFCQRVAVMDK 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
350-540 |
8.58e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 69.65 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSyKPQGNDSKRECTV 428
Cdd:cd03247 8 FSYPEQEQQvLKNLSLELKQGEK-----IALLGRSGSGKSTLLQLLTGDLKPQQG-EITLDGVPVS-DLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQLLHdkirdacahpqfmsdvirpLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqRITASKVI 508
Cdd:cd03247 81 NQRPY-------------------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD---PITERQLL 138
|
170 180 190
....*....|....*....|....*....|...
gi 15231301 509 KRFILHAK-KTAFIVEHDFIMATYlADRVIVYE 540
Cdd:cd03247 139 SLIFEVLKdKTLIWITHHLTGIEH-MDKILFLE 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
77-284 |
9.36e-14 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 69.52 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 77 KDLAKDTTHRYGANGFKLHrlpIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYF 156
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLN---IEA-GEIVALLGPSGSGKSTLLRCIAGLEEPDSG---------SIL--IDGEDLTDLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 157 IRVVEENLKTAIKPQHvdyikevvrGNLGKMLEKLDERGLmeeicadmelnqvlerearQVSGGELQRFAIAAVFVKKAD 236
Cdd:cd03229 69 DELPPLRRRIGMVFQD---------FALFPHLTVLENIAL-------------------GLSGGQQQRVALARALAMDPD 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 237 IYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSY-VIVVEHDLSVLDYLSD 284
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGItVVLVTHDLDEAARLAD 169
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
80-281 |
1.24e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.46 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGANGFKLHRLPIP----RPGQVLGLVGTNGIGKSTALKILAGKLKP----------NLGRFNtppdwEEILT 145
Cdd:COG1136 7 LRNLTKSYGTGEGEVTALRGVslsiEAGEFVAIVGPSGSGKSTLLNILGGLDRPtsgevlidgqDISSLS-----ERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 146 HFRGSEL----QSYF-IRV--VEENLKTAIKPQHVDyiKEVVRGNLGKMLEKLDerglmeeicadmeLNQVLEREARQVS 218
Cdd:COG1136 82 RLRRRHIgfvfQFFNlLPEltALENVALPLLLAGVS--RKERRERARELLERVG-------------LGDRLDHRPSQLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 219 GGELQRFAIAAVFVKKADIYMFDEPSSYLDvrqrLKAAQVIRSLLR--HDSY---VIVVEHDLSVLDY 281
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLD----SKTGEEVLELLRelNRELgttIVMVTHDPELAAR 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
101-287 |
1.32e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 70.23 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQSYfIRVVEENLktAIKPQHvD------ 174
Cdd:cd03263 26 YKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-----------YINGYSIRTD-RKAARQSL--GYCPQF-Dalfdel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 ------YIKEVVRGnlgkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:cd03263 91 tvrehlRFYARLKG-----LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 249 VRQRLKAAQVIRSlLRHDSYVIVVEHDLSVLDYLSDFVC 287
Cdd:cd03263 166 PASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIA 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
350-541 |
1.66e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.18 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIPEFNVSYKPQGNDSKRE--- 425
Cdd:PRK13632 15 FSYPNSENNaLKNVSFEINEGEY-----VAILGHNGSGKSTISKILTGLLKPQSG---EIKIDGITISKENLKEIRKkig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 ------------CTVRQLLHDKIRDACAHPQFMSDVIRPL----QIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLI 489
Cdd:PRK13632 87 iifqnpdnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLakkvGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 490 DEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATyLADRVIVYEG 541
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSE 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-538 |
1.67e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 70.45 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAG---------AFPREEGVQSEIPEFNVSYKPQ 418
Cdd:cd03296 7 NVSKRFGDFValddvsLDIPSGE-----LVALLGPSGSGKTTLLRLIAGlerpdsgtiLFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 GNDSKRECTVRQ-----LlhdKIRDACAHP------QFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIY 487
Cdd:cd03296 82 HYALFRHMTVFDnvafgL---RVKPRSERPpeaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 488 LIDEPSAHLDSEQRitasKVIKRFI--LHAKK--TAFIVEHDFIMATYLADRVIV 538
Cdd:cd03296 159 LLDEPFGALDAKVR----KELRRWLrrLHDELhvTTVFVTHDQEEALEVADRVVV 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
80-303 |
1.78e-13 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 69.81 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGANGFKLHRL-PIP---RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---FNTP-----PDweeilthf 147
Cdd:cd03293 3 VRNVSKTYGGGGGAVTALeDISlsvEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEvlvDGEPvtgpgPD-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 148 RGSELQSYFI---RVVEENLKTAIKPQHVDY--IKEVVRgnlgKMLEKLderGLMEeicadmelnqVLEREARQVSGGEL 222
Cdd:cd03293 75 RGYVFQQDALlpwLTVLDNVALGLELQGVPKaeARERAE----ELLELV---GLSG----------FENAYPHQLSGGMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 223 QRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAY-GVVT 300
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLLVTHDIDEAVFLADRVVVLSARPGRIvAEVE 217
|
...
gi 15231301 301 LPF 303
Cdd:cd03293 218 VDL 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
101-281 |
2.30e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 68.49 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYfirvvEENLKTAIK--PQHVDYIKE 178
Cdd:cd03247 26 KQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG---------EIT--LDGVPVSDL-----EKALSSLISvlNQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 VVRGNLGkmleklderglmeeicadmelnqvlereaRQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQV 258
Cdd:cd03247 90 TLRNNLG-----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180
....*....|....*....|...
gi 15231301 259 IRSLLRhDSYVIVVEHDLSVLDY 281
Cdd:cd03247 141 IFEVLK-DKTLIWITHHLTGIEH 162
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-538 |
3.04e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 71.29 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFKLEVmEGEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEG---VQSEI---PEFNVSYKPQgndsKREC- 426
Cdd:COG4148 6 DFRLRRGGFTLDV-DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGrirLGGEVlqdSARGIFLPPH----RRRIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 ------------TVRQLLHDKIRDACA---HPQFmSDVIRPLQIEQLMDQVVKTLSGGEKQRVAI--TLcLGKPaDIYLI 489
Cdd:COG4148 81 yvfqearlfphlSVRGNLLYGRKRAPRaerRISF-DEVVELLGIGHLLDRRPATLSGGERQRVAIgrAL-LSSP-RLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 490 DEPSAHLDsEQRitaskviKRFILH-----AKKTA---FIVEHDFIMATYLADRVIV 538
Cdd:COG4148 158 DEPLAALD-LAR-------KAEILPylerlRDELDipiLYVSHSLDEVARLADHVVL 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
102-294 |
4.32e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF---NTPPDW---------EEILTHFRGSElQSYFIRVVEENLKTAIK 169
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqGKPLDYskrgllalrQQVATVFQDPE-QQIFYTDIDSDIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 170 pqhvdyikevvrgNLGKMLEKLDERglmeeicADMELNQVLEREARQ-----VSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:PRK13638 105 -------------NLGVPEAEITRR-------VDEALTLVDAQHFRHqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 245 SYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL-------YGKPG 294
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLrqgqiltHGAPG 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
354-543 |
4.34e-13 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 68.94 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF--NVSYKP 417
Cdd:cd03265 5 NLVKKYGDFEavrgvsFRVRRGE-----IFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREVrrRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 418 QGNDSKRECTVRQ--LLHDKIrdacahpQFMSDVIRPLQIEQLM---------DQVVKTLSGGEKQRVAITLCLGKPADI 486
Cdd:cd03265 80 QDLSVDDELTGWEnlYIHARL-------YGVPGAERRERIDELLdfvglleaaDRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 487 YLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRV-------IVYEGQP 543
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVaiidhgrIIAEGTP 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
354-538 |
5.14e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.51 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPE--------- 410
Cdd:COG3842 10 NVSKRYGDVTalddvsLSIEPGEF-----VALLGPSGCGKTTLLRMIAGFETPDSGrilldgrdVTGLPPEkrnvgmvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 411 ----F-------NVSY--KPQGNdSKREctvrqlLHDKIRDACAHpqfmsdvirpLQIEQLMDQVVKTLSGGEKQRVAI- 476
Cdd:COG3842 85 dyalFphltvaeNVAFglRMRGV-PKAE------IRARVAELLEL----------VGLEGLADRYPHQLSGGQQQRVALa 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 477 -TLCLgKPaDIYLIDEPSAHLDSEQRITASKVIKRfILHAKKTAFI-VEHDFIMATYLADRVIV 538
Cdd:COG3842 148 rALAP-EP-RVLLLDEPLSALDAKLREEMREELRR-LQRELGITFIyVTHDQEEALALADRIAV 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
352-544 |
5.66e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 68.75 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 352 YPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqseipefNVSYKPQGNDSKRECTVRQL 431
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEF-----VALIGPSGAGKSTLLRCLNGLVEPTSG--------SVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 432 LHdkiRDACAHPQF--------MSDV----------IRPL-------QIE---QLMDQV---------VKTLSGGEKQRV 474
Cdd:cd03256 77 RR---QIGMIFQQFnlierlsvLENVlsgrlgrrstWRSLfglfpkeEKQralAALERVglldkayqrADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 475 AITLCLGKPADIYLIDEPSAHLDSeqrITASKVI---KRFILHAKKTAFIVEHDFIMATYLADRV-------IVYEGQPA 544
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDP---ASSRQVMdllKRINREEGITVIVSLHQVDLAREYADRIvglkdgrIVFDGPPA 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
92-277 |
6.07e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.33 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 92 FKLHRlpiprpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNT------PPDweeiLTHFRGSELqsyfirVVEENLk 165
Cdd:cd03220 43 FEVPR------GERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvssLLG----LGGGFNPEL------TGRENI- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 166 taikpqhvdYIKEVVRGNLGKmleklDERGLMEEICADMELNQVLEREARQVSGGELQR--FAIAAVFvkKADIYMFDEP 243
Cdd:cd03220 106 ---------YLNGRLLGLSRK-----EIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARlaFAIATAL--EPDILLIDEV 169
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 244 SSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLS 277
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS 203
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
101-280 |
6.40e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 68.39 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeILthFRGSELQSYFIRVVEENLKTAikPQHVDYIKEVV 180
Cdd:cd03245 28 RAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGS---------VL--LDGTDIRQLDPADLRRNIGYV--PQDVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNLG-KMLEKLDERGL--MEEICAD---------MELnQVLEReARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:cd03245 95 RDNITlGAPLADDERILraAELAGVTdfvnkhpngLDL-QIGER-GRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 249 VR--QRLKAAqvIRSLLRHDSyVIVVEHDLSVLD 280
Cdd:cd03245 173 MNseERLKER--LRQLLGDKT-LIIITHRPSLLD 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
101-292 |
6.75e-13 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 68.68 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---FNTPpdweeiLTHFRGSELQSYFIRV--------------VEEN 163
Cdd:cd03261 24 RRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvliDGED------ISGLSEAELYRLRRRMgmlfqsgalfdsltVFEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 164 LKTAIKpQHVDYIKEVVRgnlGKMLEKLDERGlmeeicadmeLNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEP 243
Cdd:cd03261 98 VAFPLR-EHTRLSEEEIR---EIVLEKLEAVG----------LRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 244 SSYLDVRQRLKAAQVIRSLlrHDSY---VIVVEHDLSVLDYLSDFVCCLYGK 292
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSL--KKELgltSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
80-284 |
6.95e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGAN------GFKLHrlpiprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILTHFRGSELQ 153
Cdd:PRK11701 9 VRGLTKLYGPRkgcrdvSFDLY------PGEVLGIVGESGSGKTTLLNALSARLAPDAG---------EVHYRMRDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 154 SYF----------IR----VVEENLKTAIKPQhvdyikeVVRG-NLGKMLEKLDER--GLMEEICADMeLNQV------L 210
Cdd:PRK11701 74 DLYalseaerrrlLRtewgFVHQHPRDGLRMQ-------VSAGgNIGERLMAVGARhyGDIRATAGDW-LERVeidaarI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 211 EREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRH-DSYVIVVEHDLSVLDYLSD 284
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAH 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
82-274 |
7.60e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 67.90 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 82 DTTHRYGANGFKLHrLPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWEEILTHFRGSELQ 153
Cdd:cd03298 5 KIRFSYGEQPMHFD-LTFAQ-GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtAAPPADRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 154 SYFirVVEENLKTAIKPqhvdyikevvrgNLgkmleKLDE--RGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVF 231
Cdd:cd03298 83 AHL--TVEQNVGLGLSP------------GL-----KLTAedRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 232 VKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSY-VIVVEH 274
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMtVLMVTH 187
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
379-541 |
8.35e-13 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 68.69 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 379 MLGENGTGKTTFIRMLAGAFPREEG-----------VQSEIPEFNVSYKPQGNDSKRECTVRQLL------H------DK 435
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPDAGtvdlagvdlhgLSRRARARRVALVEQDSDTAVPLTVRDVValgripHrslwagDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 436 IRDACAHPQFMSDVirplQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD-SEQRITASKVikRFILH 514
Cdd:TIGR03873 112 PHDAAVVDRALART----ELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvRAQLETLALV--RELAA 185
|
170 180
....*....|....*....|....*..
gi 15231301 515 AKKTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:TIGR03873 186 TGVTVVAALHDLNLAASYCDHVVVLDG 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
351-538 |
8.35e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.11 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 351 KYPNMTKQLGDFKLEVMEGeftdsQIIVMLGENGTGKTTFIRMLAG---------AFPREEGVQSEIPEFNVSYKPQGND 421
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSG-----QMVALLGPSGSGKTTLLRIIAGlehqtsghiRFHGTDVSRLHARDRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 422 SKRECTV--------RQLLHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPS 493
Cdd:PRK10851 85 LFRHMTVfdniafglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 494 AHLDSEQRitasKVIKRFI--LHA--KKTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK10851 165 GALDAQVR----KELRRWLrqLHEelKFTSVFVTHDQEEAMEVADRVVV 209
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
354-537 |
8.99e-13 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 67.64 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLG------DFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIPEFNVSYKPQGNDSKREC- 426
Cdd:TIGR03608 3 NISKKFGdkvildDLNLTIEKGKM-----YAIIGESGSGKSTLLNIIGLLEKFDSG---QVYLNGQETPPLNSKKASKFr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 -----------------TVRQLLH----DKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPAD 485
Cdd:TIGR03608 75 reklgylfqnfalieneTVEENLDlglkYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 486 IYLIDEPSAHLDSEQRitaSKVIKRF--ILHAKKTAFIVEHDFIMATyLADRVI 537
Cdd:TIGR03608 155 LILADEPTGSLDPKNR---DEVLDLLleLNDEGKTIIIVTHDPEVAK-QADRVI 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
364-544 |
8.99e-13 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 67.84 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGV------------QSEIPEFNVSYKPQGNDSKRECTVRQ- 430
Cdd:cd03224 21 LTVPEGE-----IVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrditglpPHERARAGIGYVPEGRRIFPELTVEEn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 431 -LLHDKIRDACAHPQFMSDVIR--PLqIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLdseqritASKV 507
Cdd:cd03224 96 lLLGAYARRRAKRKARLERVYElfPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL-------APKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15231301 508 IKRFI-----LHAKKTA-FIVEHDFIMATYLADRV-------IVYEGQPA 544
Cdd:cd03224 168 VEEIFeaireLRDEGVTiLLVEQNARFALEIADRAyvlergrVVLEGTAA 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
349-538 |
1.15e-12 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 70.57 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKQ-LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipefnvSYKPQGNDskrect 427
Cdd:COG4987 340 SFRYPGAGRPvLDGLSLTLPPGE-----RVAIVGPSGSGKSTLLALLLRFLDPQSG----------SITLGGVD------ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQLLHDKIRDACA----HPQFMSDVIR-----------PLQIEQLMDQV-----VK---------------TLSGGEKQ 472
Cdd:COG4987 399 LRDLDEDDLRRRIAvvpqRPHLFDTTLRenlrlarpdatDEELWAALERVglgdwLAalpdgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 473 RVAITLCLGKPADIYLIDEPSAHLDseqRITASKVIKRFILHAK-KTAFIVEHDFIMATyLADRVIV 538
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLD---AATEQALLADLLEALAgRTVLLITHRLAGLE-RMDRILV 541
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
350-544 |
1.24e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 68.23 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSykpqGNDSKRECTV 428
Cdd:TIGR04520 8 FSYPESEKPaLKNVSLSIEKGEF-----VAIIGHNGSGKSTLAKLLNGLLLPTSG------KVTVD----GLDTLDEENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQllhdkIRDACA----HP--QFMS-----DV--------IRPLQIEQLMDQVVKT-------------LSGGEKQRVAI 476
Cdd:TIGR04520 73 WE-----IRKKVGmvfqNPdnQFVGatvedDVafglenlgVPREEMRKRVDEALKLvgmedfrdrephlLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 477 --TLCLgKPaDIYLIDEPSAHLDSEQRITASKVIKRfiLHAK--KTAFIVEHDFIMATyLADRVIV-------YEGQPA 544
Cdd:TIGR04520 148 agVLAM-RP-DIIILDEATSMLDPKGRKEVLETIRK--LNKEegITVISITHDMEEAV-LADRVIVmnkgkivAEGTPR 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
101-289 |
1.41e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 67.46 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG--RFN------TPPdwEEILThfRG----SELQSYFIRV-VEENLKTA 167
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsiRFDgrditgLPP--HERAR--AGigyvPEGRRIFPELtVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 168 IKPQHvdyiKEVVRGNLGKMLE---KLDERglmeeicadmelnqvLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:cd03224 100 AYARR----RAKRKARLERVYElfpRLKER---------------RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 245 SYL--DVRQRLkaAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:cd03224 161 EGLapKIVEEI--FEAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
97-290 |
1.60e-12 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 67.21 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 97 LPIPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntpPDWEEILthFRGSELQSYFIRVVEENLKTAIKPQHVDYI 176
Cdd:cd03260 21 LDIP-KGEITALIGPSGCGKSTLLRLLNRLNDLIPGA----PDEGEVL--LDGKDIYDLDVDVLELRRRVGMVFQKPNPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEVVRGN------LGKMLEKLDERGLMEEICADMEL-NQVLER-EARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:cd03260 94 PGSIYDNvayglrLHGIKLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15231301 249 VRQRLKAAQVIRSlLRHDSYVIVVEHDLSVLDYLSDFVCCLY 290
Cdd:cd03260 174 PISTAKIEELIAE-LKKEYTIVIVTHNMQQAARVADRTAFLL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
371-540 |
1.68e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 66.75 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 371 FTDSQIIVMLGENGTGKTTFIRMLAGaFPREEGVQSEIPEFNVSYKP----------QGNDSKRECTVRQ----LLHDKI 436
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAG-FETPQSGRVLINGVDVTAAPpadrpvsmlfQENNLFAHLTVEQnvglGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 437 RDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAK 516
Cdd:cd03298 100 KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETK 179
|
170 180
....*....|....*....|....
gi 15231301 517 KTAFIVEHDFIMATYLADRVIVYE 540
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
349-541 |
1.84e-12 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 66.84 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNM-TKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGV-------QSEIPEF----NVSYK 416
Cdd:cd03245 9 SFSYPNQeIPALDNVSLTIRAGEK-----VAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtdIRQLDPAdlrrNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 417 PQgnDSkrectvrQLLHDKIRD--ACAHP----QFMSDVIRPLQIEQLMD--------QVVK---TLSGGEKQRVAIT-L 478
Cdd:cd03245 84 PQ--DV-------TLFYGTLRDniTLGAPladdERILRAAELAGVTDFVNkhpngldlQIGErgrGLSGGQRQAVALArA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 479 CLGKPAdIYLIDEPSAHLD--SEQRITasKVIKRFILHakKTAFIVEHDFIMATyLADRVIVYEG 541
Cdd:cd03245 155 LLNDPP-ILLLDEPTSAMDmnSEERLK--ERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
103-274 |
3.47e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.59 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNtppdWEEILTHFRGSELQSYFIRVveenlktaikpQHVDYIKEV--V 180
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL----LNGGPLDFQRDSIARGLLYL-----------GHAPGIKTTlsV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNLgKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIR 260
Cdd:cd03231 91 LENL-RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....
gi 15231301 261 SLLRHDSYVIVVEH 274
Cdd:cd03231 170 GHCARGGMVVLTTH 183
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
101-276 |
4.47e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.54 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--NTPPDWEeilthFRGSELqSYFIRVVEENlktaikpQHVdyIKE 178
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtlDGVPVSS-----LDQDEV-RRRVSVCAQD-------AHL--FDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 VVRGNL---------GKMLEKLDERGLMEEICADME-LNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:TIGR02868 424 TVRENLrlarpdatdEELWAALERVGLADWLRALPDgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180 190
....*....|....*....|....*....|
gi 15231301 249 VrqrLKAAQVIRSLLRHDS--YVIVVEHDL 276
Cdd:TIGR02868 504 A---ETADELLEDLLAALSgrTVVLITHHL 530
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
101-286 |
4.64e-12 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 65.85 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-----FNTPPDWEEIlthfRGSelqsyfIRVVEENLktAIKPQHVDY 175
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvagHDVVREPREV----RRR------IGIVFQDL--SVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IKEVVRGNL-GKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLK 254
Cdd:cd03265 92 ENLYIHARLyGVPGAERRER--IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190
....*....|....*....|....*....|...
gi 15231301 255 AAQVIRSLLR-HDSYVIVVEHDLSVLDYLSDFV 286
Cdd:cd03265 170 VWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRV 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
361-541 |
5.94e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 361 DFKLEVMEGeftdsQIIVMLGENGTGKTTFIRMLAGAFPREEGV-QSEIPEfnvsykpqgNDSKRECTvrqllhdkIRDA 439
Cdd:COG2401 48 DLNLEIEPG-----EIVLIVGASGSGKSTLLRLLAGALKGTPVAgCVDVPD---------NQFGREAS--------LIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 440 CAHPQFMSDVIRPLQIEQLMDQV-----VKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQ-RITASKViKRFIL 513
Cdd:COG2401 106 IGRKGDFKDAVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTaKRVARNL-QKLAR 184
|
170 180
....*....|....*....|....*...
gi 15231301 514 HAKKTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:COG2401 185 RAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
101-275 |
6.75e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNtppdweeilthfRGSELQ-SYFirvveenlktaikPQHVDYIKEv 179
Cdd:COG0488 339 DRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK------------LGETVKiGYF-------------DQHQEELDP- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 vrgnlgkmlekldERGLMEEICADMELNQvlEREARQV------------------SGGELQRFAIAAVFVKKADIYMFD 241
Cdd:COG0488 393 -------------DKTVLDELRDGAPGGT--EQEVRGYlgrflfsgddafkpvgvlSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 242 EPSSYLDV--RQRLKAAqvirsLLRHDSYVIVVEHD 275
Cdd:COG0488 458 EPTNHLDIetLEALEEA-----LDDFPGTVLLVSHD 488
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
101-286 |
8.09e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNT--PPDWEEI----------LTHFRGSELQSYFI---RVVEENLK 165
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVDMtkpgpdgrgrAKRYIGILHQEYDLyphRTVLDNLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 166 TAIKpqhVDYIKEVVRgnlGKMLEKLDERGLMEEicadmELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:TIGR03269 388 EAIG---LELPDELAR---MKAVITLKMVGFDEE-----KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15231301 246 YLDVRQRLKAAQVI-RSLLRHDSYVIVVEHDLsvldylsDFV 286
Cdd:TIGR03269 457 TMDPITKVDVTHSIlKAREEMEQTFIIVSHDM-------DFV 491
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
102-286 |
9.48e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 64.70 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTppdwEEILTHFRGSELQSYfIRVVEENlkTAIkpqhvdYIKEVVR 181
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV----DGFDVVKEPAEARRR-LGFVSDS--TGL------YDRLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 182 GNLGKM-----LEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAA 256
Cdd:cd03266 97 ENLEYFaglygLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176
|
170 180 190
....*....|....*....|....*....|
gi 15231301 257 QVIRSLLRHDSYVIVVEHDLSVLDYLSDFV 286
Cdd:cd03266 177 EFIRQLRALGKCILFSTHIMQEVERLCDRV 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
359-541 |
9.53e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.41 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqIIVmlGENGTGKTTFIRMLAGAFPREEGvQSEIPEfNVSYKPQG----NDskrecTVRQ-LLH 433
Cdd:cd03250 21 LKDINLEVPKGELV---AIV--GPVGSGKSSLLSALLGELEKLSG-SVSVPG-SIAYVSQEpwiqNG-----TIREnILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 434 DKIRDacahPQFMSDVIRPLQIEQLMDQVVK-----------TLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEqri 502
Cdd:cd03250 89 GKPFD----EERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH--- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 503 TASKVIKRFILHA---KKTAFIVEH--DFIMAtylADRVIVYEG 541
Cdd:cd03250 162 VGRHIFENCILGLllnNKTRILVTHqlQLLPH---ADQIVVLDN 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
101-289 |
9.64e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.17 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilTHFRGSELQSYFIRVVEENLKTAikPQHVDY----- 175
Cdd:PRK09536 27 REGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT-----------VLVAGDDVEALSARAASRRVASV--PQDTSLsfefd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IKEVV-------RGNLGKMLEklDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:PRK09536 94 VRQVVemgrtphRSRFDTWTE--TDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15231301 249 VRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
348-499 |
1.06e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 67.39 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 348 ARYKYPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQGNDSKRECT 427
Cdd:TIGR02868 340 LSAGYPGAPPVLDGVSLDLPPGER-----VAILGPSGSGKSTLLATLAGLLDPLQG-EVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQLLH-------DKIRDAC--AHPQFMSDVIRPLQIEQL-------MDQVV----KTLSGGEKQRVAITLCLGKPADIY 487
Cdd:TIGR02868 414 CAQDAHlfdttvrENLRLARpdATDEELWAALERVGLADWlralpdgLDTVLgeggARLSGGERQRLALARALLADAPIL 493
|
170
....*....|..
gi 15231301 488 LIDEPSAHLDSE 499
Cdd:TIGR02868 494 LLDEPTEHLDAE 505
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
351-542 |
1.19e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 65.01 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 351 KYPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGV-------QSEIPEF----NVSYK--- 416
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEF-----LVLIGPSGSGKTTTMKMINRLIEPTSGEifidgedIREQDPVelrrKIGYViqq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 417 ----PQGNDSKRECTVRQLLH---DKIRDACAhpQFMSDVirPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLI 489
Cdd:cd03295 84 iglfPHMTVEENIALVPKLLKwpkEKIRERAD--ELLALV--GLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 490 DEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADR-VIVYEGQ 542
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRiAIMKNGE 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
322-540 |
1.22e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 64.48 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 322 LRFRDESLTFRVSETTQENDGEVKSYARYKYPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPRE 401
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGE-----RIGLIGRNGAGKSTLLRLLAGIYPPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 402 EG-VQ-----SEIPEFNVSYKPqgndskrECTVRQ------LLHDKIRDACAhpQFMSDVIRPLQIEQLMDQVVKTLSGG 469
Cdd:cd03220 76 SGtVTvrgrvSSLLGLGGGFNP-------ELTGREniylngRLLGLSRKEID--EKIDEIIEFSELGDFIDLPVKTYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 470 EKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAkKTAFIVEHDFIMATYLADRVIVYE 540
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLE 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
349-542 |
1.51e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 64.60 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKqlgDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVS-------------Y 415
Cdd:TIGR04406 10 SYKKRKVVN---DVSLSVKSGE-----IVGLLGPNGAGKTTSFYMIVGLVRPDAG-KILIDGQDIThlpmherarlgigY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 416 KPQGNDSKRECTVRQ-----LLHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLID 490
Cdd:TIGR04406 81 LPQEASIFRKLTVEEnimavLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 491 EPSAHLDSeqriTASKVIKRFILHAKKTA---FIVEHDFIMATYLADRV-IVYEGQ 542
Cdd:TIGR04406 161 EPFAGVDP----IAVGDIKKIIKHLKERGigvLITDHNVRETLDICDRAyIISDGK 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
352-544 |
1.60e-11 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 64.63 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 352 YPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEG-------------------VQSEI---- 408
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEF-----VAIIGPSGAGKSTLLRCINRLVEPSSGsillegtditklrgkklrkLRRRIgmif 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 409 PEFN---------------VSYKPqgndskrecTVRQLL-----HDKIRdacahpqfMSDVIRPLQIEQLMDQVVKTLSG 468
Cdd:TIGR02315 86 QHYNlierltvlenvlhgrLGYKP---------TWRSLLgrfseEDKER--------ALSALERVGLADKAYQRADQLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 469 GEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRV-------IVYEG 541
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIvglkageIVFDG 228
|
...
gi 15231301 542 QPA 544
Cdd:TIGR02315 229 APS 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
369-537 |
1.74e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.41 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 369 GEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFNVSYKPQGNDSKRE--CTVRQL-----------LHDK 435
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLvamgrwarrglWRRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 436 IRDACAhpqFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD--SEQRITAskVIKRfIL 513
Cdd:NF040873 93 TRDDRA---AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDaeSRERIIA--LLAE-EH 166
|
170 180
....*....|....*....|....
gi 15231301 514 HAKKTAFIVEHDFIMATyLADRVI 537
Cdd:NF040873 167 ARGATVVVVTHDLELVR-RADPCV 189
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
101-276 |
1.78e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNLGR--FNTPPdweeiLTHFRGSEL---QSYFirvveenlktaikPQHVD- 174
Cdd:COG4138 20 NAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEilLNGRP-----LSDWSAAELarhRAYL-------------SQQQSp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 --------YIKEVVRGNLgkMLEKLDerGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVK-------KADIYM 239
Cdd:COG4138 81 pfampvfqYLALHQPAGA--SSEAVE--QLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 15231301 240 FDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
349-538 |
1.82e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 66.73 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKQLGDFKLEVMEGEFTdsqIIVmlGENGTGKTTFIRMLAGAFPREEGV------------QSEIPEfNVSYK 416
Cdd:COG1132 346 SFSYPGDRPVLKDISLTIPPGETV---ALV--GPSGSGKSTLVNLLLRFYDPTSGRilidgvdirdltLESLRR-QIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 417 PQgnDSkrectvrQLLHDKIRD--ACAHPQF-MSDVIRPLQ-------IEQL---MDQVV----KTLSGGEKQRVAI--T 477
Cdd:COG1132 420 PQ--DT-------FLFSGTIREniRYGRPDAtDEEVEEAAKaaqahefIEALpdgYDTVVgergVNLSGGQRQRIAIarA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 478 LClgKPADIYLIDEPSAHLD--SEQRITASkvIKRfiLHAKKTAFIVEHDF--IMAtylADRVIV 538
Cdd:COG1132 491 LL--KDPPILILDEATSALDteTEALIQEA--LER--LMKGRTTIVIAHRLstIRN---ADRILV 546
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
101-286 |
2.09e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFN--TPPDWEEILthfrGSELQSYFIRVVEENLKTAIKPQHV--DYI 176
Cdd:PRK10418 27 QRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAgrVLLDGKPVA----PCALRGRKIATIMQNPRSAFNPLHTmhTHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEVVR-----GNLGKMLEKLDERGLmeeicADMElnQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQ 251
Cdd:PRK10418 103 RETCLalgkpADDATLTAALEAVGL-----ENAA--RVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 252 RLKAAQVIRSLLR-HDSYVIVVEHDLSVLDYLSDFV 286
Cdd:PRK10418 176 QARILDLLESIVQkRALGMLLVTHDMGVVARLADDV 211
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
9-72 |
2.24e-11 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 59.67 E-value: 2.24e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 9 AIVSEDRCKpkKCRqECKKSCPVvktgkLCIEVGStsKSAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG4231 17 YVIDEDKCT--GCG-ACVKVCPA-----DAIEEGD--GKAVIDPDLCIGCGSCVQVCPVDAIKL 70
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
350-544 |
2.62e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 64.65 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEG-------VQSEIPEFNVSYKP---- 417
Cdd:PRK13635 13 FRYPDAATYaLKDVSFSVYEGEW-----VAIVGHNGSGKSTLAKLLNGLLLPEAGtitvggmVLSEETVWDVRRQVgmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 418 QGNDSkrectvrQLLHDKIRDACA---------HPQF---MSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPAD 485
Cdd:PRK13635 88 QNPDN-------QFVGATVQDDVAfglenigvpREEMverVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 486 IYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYlADRVIVY-------EGQPA 544
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMnkgeileEGTPE 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
77-291 |
2.79e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 77 KDLAKDTTHRYGANGFK------LHRLPIPRP-GQVLGLVGTNGIGKSTALKIlagklkpnLGRFNTPPDWEEILTHFRG 149
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRvpgrtlLHPLSLTFPaGKVTGLIGHNGSGKSTLLKM--------LGRHQPPSEGEILLDAQPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 150 SELQS-YFIRvveenlKTAIKPQHVD-----YIKEVV-------RGNLGKMleKLDERGLMEEICADMELNQVLEREARQ 216
Cdd:PRK10575 76 ESWSSkAFAR------KVAYLPQQLPaaegmTVRELVaigrypwHGALGRF--GAADREKVEEAISLVGLKPLAHRLVDS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 217 VSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDLSVLDYLSDFVCCLYG 291
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRG 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
97-289 |
2.85e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 63.89 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 97 LPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF----NTPpdWEEILTHFR------GSELQSYFIRVVEENLKt 166
Cdd:cd03267 42 FTIEK-GEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVP--WKRRKKFLRrigvvfGQKTQLWWDLPVIDSFY- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 167 aikpqhvdYIKEVVRgnlgkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:cd03267 118 --------LLAAIYD------LPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 247 LDVRQRLKAAQVIRSLLR-HDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:cd03267 184 LDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
352-538 |
2.95e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 352 YPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAfpreEGVQS---EIPEFNVsykpqgND---SKRE 425
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEF-----IVLVGPSGCGKSTLLRMVAGL----ERITSgeiWIGGRVV------NElepADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 C-------------TVRQ-----LlhdKIRDacahpqfMS---------DVIRPLQIEQLMDQVVKTLSGGEKQRVAitl 478
Cdd:PRK11650 78 IamvfqnyalyphmSVREnmaygL---KIRG-------MPkaeieervaEAARILELEPLLDRKPRELSGGQRQRVA--- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 479 cLG-----KPAdIYLIDEPSAHLDSEQRITASKVIKRfiLHA--KKTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK11650 145 -MGraivrEPA-VFLFDEPLSNLDAKLRVQMRLEIQR--LHRrlKTTSLYVTHDQVEAMTLADRVVV 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
357-557 |
3.09e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 357 KQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVS-------------YKPQGNDSK 423
Cdd:PRK10895 17 RVVEDVSLTVNSGE-----IVGLLGPNGAGKTTTFYMVVGIVPRDAG-NIIIDDEDISllplhararrgigYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 424 RECTVRQLLHD--KIRDACAHPQF---MSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDS 498
Cdd:PRK10895 91 RRLSVYDNLMAvlQIRDDLSAEQRedrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 499 EQRITaskvIKRFILHAKKTA---FIVEHDFIMATYLADRV-IVYEGqpavKCIAH-SPQSLLS 557
Cdd:PRK10895 171 ISVID----IKRIIEHLRDSGlgvLITDHNVRETLAVCERAyIVSQG----HLIAHgTPTEILQ 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
103-276 |
3.10e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.24 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweeilthfrgsELQSYFIRVVEENL-----KTAIKPQHVD--Y 175
Cdd:PRK13632 35 GEYVAILGHNGSGKSTISKILTGLLKPQSG------------------EIKIDGITISKENLkeirkKIGIIFQNPDnqF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IKEVVRGNLGKMLE-KLDERGLMEEICAD------MElnQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:PRK13632 97 IGATVEDDIAFGLEnKKVPPKKMKDIIDDlakkvgME--DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180
....*....|....*....|....*....
gi 15231301 249 VRQRLKAAQVIRSLLRH-DSYVIVVEHDL 276
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTrKKTLISITHDM 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
80-281 |
3.50e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.94 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 80 AKDTTHRYGANGFK--------LHRLPIP-RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG--RFNTPPdweeiLTHFR 148
Cdd:PRK10419 6 VSGLSHHYAHGGLSgkhqhqtvLNNVSLSlKSGETVALLGRSGCGKSTLARLLVGLESPSQGnvSWRGEP-----LAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 149 GSELQSY--FIRVVEENLKTAIKPQHVdyIKEVVRGNLgKMLEKLDERGL---MEEICADMELN-QVLEREARQVSGGEL 222
Cdd:PRK10419 81 RAQRKAFrrDIQMVFQDSISAVNPRKT--VREIIREPL-RHLLSLDKAERlarASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 223 QRFAIAAVFVKKADIYMFDEPSSYLDvrqRLKAAQVIRSL--LRH--DSYVIVVEHDLSVLDY 281
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLD---LVLQAGVIRLLkkLQQqfGTACLFITHDLRLVER 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
101-303 |
3.53e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 63.25 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG-------RFNTP-PDweeilthfRGSELQSYFI---RVVEENLKTAIK 169
Cdd:TIGR01184 9 QQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilegkQITEPgPD--------RMVVFQNYSLlpwLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 170 pqhvdyikEVVRGnlgkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD- 248
Cdd:TIGR01184 81 --------RVLPD-----LSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDa 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 249 -VRQRLKaAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAY--GVVTLPF 303
Cdd:TIGR01184 148 lTRGNLQ-EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANigQILEVPF 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
377-525 |
4.34e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 377 IVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFNVSY---KPQGNDSKrecTVR-----------QLL--HDKIRDAC 440
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYlpqEPQLDPTK---TVRenveegvaeikDALdrFNEISAKY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 441 AHPQF-----------MSDVIRPL-------QIEQLM--------DQVVKTLSGGEKQRVAIT-LCLGKPaDIYLIDEPS 493
Cdd:TIGR03719 111 AEPDAdfdklaaeqaeLQEIIDAAdawdldsQLEIAMdalrcppwDADVTKLSGGERRRVALCrLLLSKP-DMLLLDEPT 189
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 494 AHLDSEQritaskV--IKRFILHAKKTAFIVEHD 525
Cdd:TIGR03719 190 NHLDAES------VawLERHLQEYPGTVVAVTHD 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
210-297 |
4.93e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 61.96 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 210 LEREARQVSGGELQRFAIAAVFVK--KADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYlSDFVC 287
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWII 159
|
90
....*....|
gi 15231301 288 CLYGKPGAYG 297
Cdd:cd03238 160 DFGPGSGKSG 169
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
102-274 |
5.78e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeILTHFRGSELQSYFIRVVEENLKTAIKP-----QHVDYI 176
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT---------IKLDGGDIDDPDVAEACHYLGHRNAMKPaltvaENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEVvRGNlgkmleklDERGLMEEICAdMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR-QRLKA 255
Cdd:PRK13539 98 AAF-LGG--------EELDIAAALEA-VGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAaVALFA 167
|
170
....*....|....*....
gi 15231301 256 AqVIRSLLRHDSYVIVVEH 274
Cdd:PRK13539 168 E-LIRAHLAQGGIVIAATH 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
101-297 |
5.95e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 62.30 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG--RFNTPPDWEEILTHF------RGselqSYFIRVVEENLKtaikpqh 172
Cdd:cd03269 24 EKGEIFGLLGPNGAGKTTTIRMILGIILPDSGevLFDGKPLDIAARNRIgylpeeRG----LYPKMKVIDQLV------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 vdYIKEVvrgnlgKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQR 252
Cdd:cd03269 93 --YLAQL------KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15231301 253 LKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLY-GKPGAYG 297
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNkGRAVLYG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
364-537 |
6.44e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 62.37 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAG-------------------------AFPREE-GV--QSE--IPEFnv 413
Cdd:COG1136 29 LSIEAGEF-----VAIVGPSGSGKSTLLNILGGldrptsgevlidgqdisslserelaRLRRRHiGFvfQFFnlLPEL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 414 sykpqgndskrecTVRQ-----LLHDKIRDACAHPQFMsDVIRPLQIEQLMDQVVKTLSGGEKQRVAI--TLcLGKPAdI 486
Cdd:COG1136 102 -------------TALEnvalpLLLAGVSRKERRERAR-ELLERVGLGDRLDHRPSQLSGGQQQRVAIarAL-VNRPK-L 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 487 YLIDEPSAHLDSEqriTASKVIKRFILHAK---KTAFIVEHDFIMATYlADRVI 537
Cdd:COG1136 166 ILADEPTGNLDSK---TGEEVLELLRELNRelgTTIVMVTHDPELAAR-ADRVI 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
359-546 |
6.67e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 62.48 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAG-AFPREEGVQSEIPEF------------NVSYKPQgndskre 425
Cdd:TIGR01184 1 LKGVNLTIQQGEF-----ISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQItepgpdrmvvfqNYSLLPW------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 CTVRQ---LLHDKIRDACAHP---QFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:TIGR01184 69 LTVREniaLAVDRVLPDLSKSerrAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 500 QRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQPAVK 546
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAN 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
101-251 |
7.41e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWEEILTHFRGSELQSYFirVVEENLKTAIKPqh 172
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtTTPPSRRPVSMLFQENNLFSHL--TVAQNIGLGLNP-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 vdyikevvrgNLgkmleKLD--ERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD-- 248
Cdd:PRK10771 99 ----------GL-----KLNaaQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
...
gi 15231301 249 VRQ 251
Cdd:PRK10771 164 LRQ 166
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
102-501 |
8.20e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDW-----------------EEILT---HFRgsELQSYFIRVVE 161
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawvnqetpalpqpalEYVIDgdrEYR--QLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 162 ENLKTAIKPQH--VDYIKE-VVRGNLGKMLEKLderGLMEEicadmelnqVLEREARQVSGGELQRFAIAAVFVKKADIY 238
Cdd:PRK10636 104 RNDGHAIATIHgkLDAIDAwTIRSRAASLLHGL---GFSNE---------QLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 239 MFDEPSSYLDvrqrLKAaqVI---RSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYgkpgaygvvtlpfsvREGINVFLAG 315
Cdd:PRK10636 172 LLDEPTNHLD----LDA--VIwleKWLKSYQGTLILISHDRDFLDPIVDKIIHIE---------------QQSLFEYTGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 316 FIPTENLRFRDESLTFRVSETTQENDGEVKSY---------------ARYKY--------------------------PN 354
Cdd:PRK10636 231 YSSFEVQRATRLAQQQAMYESQQERVAHLQSYidrfrakatkakqaqSRIKMlermeliapahvdnpfhfsfrapeslPN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 355 ----MTKQ---------LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFNVSYKPQ--- 418
Cdd:PRK10636 311 pllkMEKVsagygdriiLDSIKLNLVPGSR-----IGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQhql 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 ----GNDSKRECTVR---QLLHDKIRDACAHPQFMSDVIrplqieqlmDQVVKTLSGGEKQRVAITLCLGKPADIYLIDE 491
Cdd:PRK10636 386 eflrADESPLQHLARlapQELEQKLRDYLGGFGFQGDKV---------TEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
490
....*....|
gi 15231301 492 PSAHLDSEQR 501
Cdd:PRK10636 457 PTNHLDLDMR 466
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
101-542 |
8.86e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDWEEILTHFRGSELQSYFIR---------VVEENLKTAIKPQ 171
Cdd:PRK09700 29 YPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYqelsvidelTVLENLYIGRHLT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 H-------VDYIKEVVRGNLgkMLEKLDERGLMEEICADMELNqvlerearqvsggELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:PRK09700 109 KkvcgvniIDWREMRVRAAM--MLLRVGLKVDLDEKVANLSIS-------------HKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 245 SYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLygKPGAYGVVTLpfsVREGINVFLAGFIPTENLRF 324
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM--KDGSSVCSGM---VSDVSNDDIVRLMVGRELQN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 325 RDESLTFRVSETTQENDGEVKSYARYKYpnmtKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGv 404
Cdd:PRK09700 249 RFNAMKENVSNLAHETVFEVRNVTSRDR----KKVRDISFSVCRGE-----ILGFAGLVGSGRTELMNCLFGVDKRAGG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 405 qsEIPEFNVSYKPQG------------NDSKREC------TVRQ------------------LLHDKIRDACAHPQFMSD 448
Cdd:PRK09700 319 --EIRLNGKDISPRSpldavkkgmayiTESRRDNgffpnfSIAQnmaisrslkdggykgamgLFHEVDEQRTAENQRELL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 449 VIRPLQIEQLMDQvvktLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIkRFILHAKKTAFIVEHDF-- 526
Cdd:PRK09700 397 ALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM-RQLADDGKVILMVSSELpe 471
|
490
....*....|....*..
gi 15231301 527 IMAtyLADRVIVY-EGQ 542
Cdd:PRK09700 472 IIT--VCDRIAVFcEGR 486
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
377-499 |
8.93e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 377 IVMLGENGTGKTTFIRMLAGafpreegVQSEI-------PEFNVSY---KPQGNDSKrecTVRQ-----------LLH-- 433
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAG-------VDKEFegearpaPGIKVGYlpqEPQLDPEK---TVREnveegvaevkaALDrf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 434 DKIRDACAHPQFMSD-----------VIRPL-------QIEQLM--------DQVVKTLSGGEKQRVAitLC---LGKPa 484
Cdd:PRK11819 106 NEIYAAYAEPDADFDalaaeqgelqeIIDAAdawdldsQLEIAMdalrcppwDAKVTKLSGGERRRVA--LCrllLEKP- 182
|
170
....*....|....*
gi 15231301 485 DIYLIDEPSAHLDSE 499
Cdd:PRK11819 183 DMLLLDEPTNHLDAE 197
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
81-275 |
9.43e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.55 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGA----NGFKLHrlpIpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEIltHFRGselqsyf 156
Cdd:COG3839 7 ENVSKSYGGvealKDIDLD---I-EDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG---------EI--LIGG------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 157 iRVVeenlkTAIKPQHVDyIKEV-----------VRGNLG---KML----EKLDERglMEEICADMELNQVLEREARQVS 218
Cdd:COG3839 65 -RDV-----TDLPPKDRN-IAMVfqsyalyphmtVYENIAfplKLRkvpkAEIDRR--VREAAELLGLEDLLDRKPKQLS 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 219 GGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHD 275
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrLGTTTIYVTHD 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
371-541 |
1.03e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.50 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 371 FTDSQIIVMLGENGTGKTTFIRMLAGAFPREEG-----------VQSEIPEFNVSYKPQGNDSKRECTVRQLL------- 432
Cdd:PRK10575 34 FPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGeilldaqplesWSSKAFARKVAYLPQQLPAAEGMTVRELVaigrypw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 433 HDKI-RDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRF 511
Cdd:PRK10575 114 HGALgRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190
....*....|....*....|....*....|
gi 15231301 512 ILHAKKTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
101-279 |
1.15e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.70 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR----------FNTPPDWEEIL-THFRGSELQsyFI-RVVEENLktAI 168
Cdd:PRK13644 26 KKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvlvsgidtgdFSKLQGIRKLVgIVFQNPETQ--FVgRTVEEDL--AF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 169 KPQHVdyikevvrgnlgkMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:PRK13644 102 GPENL-------------CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 249 VRQRLKAAQVIRSLLRHDSYVIVVEHDLSVL 279
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEEL 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
354-541 |
1.71e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.55 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFKLevMEG---EFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEGvqsEI---PEFNVSYKPQGNDSKRECT 427
Cdd:COG0488 3 NLSKSFGGRPL--LDDvslSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG---EVsipKGLRIGYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQL----------LHDKIRDACAHPQFMSDVIRPL-----------------QIEQLM----------DQVVKTLSGGE 470
Cdd:COG0488 78 VLDTvldgdaelraLEAELEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILsglgfpeedlDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 471 KQRVAitLC---LGKPaDIYLIDEPSAHLDSEqritaskVIK---RFILHAKKTAFIVEHD--FI--MATYLAD----RV 536
Cdd:COG0488 158 RRRVA--LAralLSEP-DLLLLDEPTNHLDLE-------SIEwleEFLKNYPGTVLVVSHDryFLdrVATRILEldrgKL 227
|
....*
gi 15231301 537 IVYEG 541
Cdd:COG0488 228 TLYPG 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
101-289 |
1.86e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNlgrfntpPDWE-EILthFRGSELQSYFIRVVEENlKTAIKPQHVDYIK-- 177
Cdd:PRK13549 29 RAGEIVSLCGENGAGKSTLMKVLSG-VYPH-------GTYEgEII--FEGEELQASNIRDTERA-GIAIIHQELALVKel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 178 ----------EVVRG---NLGKMLEKLDErgLMEEICADMELNQvlerEARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:PRK13549 98 svleniflgnEITPGgimDYDAMYLRAQK--LLAQLKLDINPAT----PVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231301 245 SYL---DVRQRLKaaqVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:PRK13549 172 ASLtesETAVLLD---IIRDLKAHGIACIYISHKLNEVKAISDTICVI 216
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
9-72 |
2.06e-10 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 57.05 E-value: 2.06e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 9 AIVSEDRCKpkKCRQeCKKSCPVvktgkLCIEVGStsKSAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG2768 6 PYVDEEKCI--GCGA-CVKVCPV-----GAISIED--GKAVIDPEKCIGCGACIEVCPVGAIKI 59
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
102-542 |
2.12e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNtppdWEEILTHFRG-SELQSYFIRVVEENLKtaIKPQHVdyIKEvv 180
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL----YLGKEVTFNGpKSSQEAGIGIIHQELN--LIPQLT--IAE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 rgN--LGK----MLEKLDERGLMEEicADMELNQV-LEREARQVSG----GELQRFAIAAVFVKKADIYMFDEPSSYLDV 249
Cdd:PRK10762 99 --NifLGRefvnRFGRIDWKKMYAE--ADKLLARLnLRFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 250 RQRLKAAQVIRSLLRHDSYVIVVEHDLSVLdylsdfvcclygkpgaygvvtlpFSVREGINVFLAGfiptenlRFRDESl 329
Cdd:PRK10762 175 TETESLFRVIRELKSQGRGIVYISHRLKEI-----------------------FEICDDVTVFRDG-------QFIAER- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 330 tfRVSETTQENDGE--VKSYARYKYPNMTKQLGDFKLEVME--GE------FT--DSQIIVMLGENGTGKTTFIRMLAGA 397
Cdd:PRK10762 224 --EVADLTEDSLIEmmVGRKLEDQYPRLDKAPGEVRLKVDNlsGPgvndvsFTlrKGEILGVSGLMGAGRTELMKVLYGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 398 FPREEGVQSEIPEFNVSYKPQ----------GNDSKRE--------------CTVRQLLHDKIR-DACAHPQFMSDVIRP 452
Cdd:PRK10762 302 LPRTSGYVTLDGHEVVTRSPQdglangivyiSEDRKRDglvlgmsvkenmslTALRYFSRAGGSlKHADEQQAVSDFIRL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 453 LQIEQ-LMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFILHAKK---TAFIVEHDFIM 528
Cdd:PRK10762 382 FNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD----VGAKKEIYQLINQFKAeglSIILVSSEMPE 457
|
490
....*....|....*
gi 15231301 529 ATYLADRVIV-YEGQ 542
Cdd:PRK10762 458 VLGMSDRILVmHEGR 472
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
359-538 |
2.13e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEG--VQSEIPEFNVSYK---------PQGNDSKRECT 427
Cdd:PRK09536 19 LDGVDLSVREGSL-----VGLVGPNGAGKTTLLRAINGTLTPTAGtvLVAGDDVEALSARaasrrvasvPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQLL-------------HDKIRDAcAHPQFMSDVirplQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSA 494
Cdd:PRK09536 94 VRQVVemgrtphrsrfdtWTETDRA-AVERAMERT----GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 495 HLDSEQRITASKVIKRFIlHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK09536 169 SLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVL 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
317-538 |
2.19e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 61.19 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 317 IPTENLRFrdeslTFRVSETTQENDGEVKSYARYKYPNMTKqLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAG 396
Cdd:cd03267 1 IEVSNLSK-----SYRVYSKEPGLIGSLKSLFKRKYREVEA-LKGISFTIEKGE-----IVGFIGPNGAGKTTTLKILSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 397 AFPREEG---VQSEIPefnvsYKPQGNDSKRECTV----RQLLHD-KIRDACAhpqFMSDV--IRP-------------L 453
Cdd:cd03267 70 LLQPTSGevrVAGLVP-----WKRRKKFLRRIGVVfgqkTQLWWDlPVIDSFY---LLAAIydLPParfkkrldelselL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 454 QIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFILHAKK----TAFIVEHDFIMA 529
Cdd:cd03267 142 DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD----VVAQENIRNFLKEYNRergtTVLLTSHYMKDI 217
|
....*....
gi 15231301 530 TYLADRVIV 538
Cdd:cd03267 218 EALARRVLV 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
101-279 |
2.27e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.25 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR----------------FNtpPDweeiLThfrgselqsyfirvVEEN- 163
Cdd:COG1134 50 ERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRvevngrvsallelgagFH--PE----LT--------------GRENi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 164 -LKTAIkpqhvdyikevvrgnLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQR--FAIAAVFvkKADIYMF 240
Cdd:COG1134 110 yLNGRL---------------LGLSRKEIDEK--FDEIVEFAELGDFIDQPVKTYSSGMRARlaFAVATAV--DPDILLV 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 241 DEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVL 279
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAV 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
354-541 |
2.34e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 60.62 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVsykpqgNDSKRECt 427
Cdd:cd03262 5 NLHKSFGDFHvlkgidLTVKKGE-----VVVIIGPSGSGKSTLLRCINLLEEPDSG-TIIIDGLKL------TDDKKNI- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 vrqllhDKIRDAC----------AHPQFMSDVIRPLQI-------------EQLMDQV---------VKTLSGGEKQRVA 475
Cdd:cd03262 72 ------NELRQKVgmvfqqfnlfPHLTVLENITLAPIKvkgmskaeaeeraLELLEKVgladkadayPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 476 I--TLCLgKPaDIYLIDEPSAHLDSEQRITASKVIKRfILHAKKTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:cd03262 146 IarALAM-NP-KVMLFDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
79-277 |
2.40e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 79 LAKDTTHRYGA----NGFKLHrlpIPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF---NTPPD--WEEILTHFRG 149
Cdd:PRK11247 14 LLNAVSKRYGErtvlNQLDLH---IP-AGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagTAPLAeaREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 150 SELQSYfirvveenlKTAIkpqhvDYIKEVVRGNL-GKMLEKLDERGLMEeicadmelnQVLEREArQVSGGELQRFAIA 228
Cdd:PRK11247 90 ARLLPW---------KKVI-----DNVGLGLKGQWrDAALQALAAVGLAD---------RANEWPA-ALSGGQKQRVALA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15231301 229 AVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSL-LRHDSYVIVVEHDLS 277
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVS 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
359-565 |
2.62e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAgafpreegvQSEIP----------EFNVSYKPqgnDSKRECTV 428
Cdd:PRK11124 18 LFDITLDCPQGE-----TLVLLGPSGAGKSSLLRVLN---------LLEMPrsgtlniagnHFDFSKTP---SDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQ----------------LLHDKIRDAC---------AHPQFMSDVIRpLQIEQLMDQVVKTLSGGEKQRVAITLCLGKP 483
Cdd:PRK11124 81 RRnvgmvfqqynlwphltVQQNLIEAPCrvlglskdqALARAEKLLER-LRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 484 ADIYLIDEPSAHLDSEqrITASKV-IKRFILHAKKTAFIVEHDFIMATYLADRVIVYEG-----QPAVKCIAHsPQSllS 557
Cdd:PRK11124 160 PQVLLFDEPTAALDPE--ITAQIVsIIRELAETGITQVIVTHEVEVARKTASRVVYMENghiveQGDASCFTQ-PQT--E 234
|
....*...
gi 15231301 558 GMNHFLSH 565
Cdd:PRK11124 235 AFKNYLSH 242
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-497 |
2.71e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFKLEVMEgEFTDSQIIVMLGENGTGKTTFIRMLAGA---------------FPREEGVQSEIPEFNVSYKPQ 418
Cdd:PRK11144 5 NFKQQLGDLCLTVNL-TLPAQGITAIFGRSGAGKTSLINAISGLtrpqkgrivlngrvlFDAEKGICLPPEKRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 gnDSkrectvRQLLHDKIRD----ACAH---PQFmSDVIRPLQIEQLMDQVVKTLSGGEKQRVAI--TLcLGKPaDIYLI 489
Cdd:PRK11144 84 --DA------RLFPHYKVRGnlryGMAKsmvAQF-DKIVALLGIEPLLDRYPGSLSGGEKQRVAIgrAL-LTAP-ELLLM 152
|
....*...
gi 15231301 490 DEPSAHLD 497
Cdd:PRK11144 153 DEPLASLD 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
101-276 |
2.83e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNLG--RFNTPPdweeiLTHFRGSELQSYFIRVVEENLKTAIKP--QHVDYi 176
Cdd:PRK03695 20 RAGEILHLVGPNGAGKSTLLARMAG-LLPGSGsiQFAGQP-----LEAWSAAELARHRAYLSQQQTPPFAMPvfQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 kevvrgNLGKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVK-------KADIYMFDEPSSYLDV 249
Cdd:PRK03695 93 ------HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*..
gi 15231301 250 RQRLKAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
359-542 |
3.03e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGVqseipEFNVSYKpqGNDSKRECTVRQllhdkiRD 438
Cdd:cd03233 23 LKDFSGVVKPGE-----MVLVLGRPGSGCSTLLKALANRTEGNVSV-----EGDIHYN--GIPYKEFAEKYP------GE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 439 ACAHPQfmSDV-IRPLQIEQLMD--------QVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqrITASKVIK 509
Cdd:cd03233 85 IIYVSE--EDVhFPTLTVRETLDfalrckgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS---STALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 510 --RFILHAKKTAFIVehdfimATYLA--------DRVIV-YEGQ 542
Cdd:cd03233 160 ciRTMADVLKTTTFV------SLYQAsdeiydlfDKVLVlYEGR 197
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
85-286 |
3.06e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 62.05 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 85 HRYGanGFKLH-RLPIPRPGqVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQSyfirvVEEN 163
Cdd:TIGR02142 7 KRLG--DFSLDaDFTLPGQG-VTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-----------VLNGRTLFD-----SRKG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 164 LKTAIKPQHVDYIKE--------VVRGNL--GKMLEKLDERGLM-EEICADMELNQVLEREARQVSGGELQRFAIAAVFV 232
Cdd:TIGR02142 68 IFLPPEKRRIGYVFQearlfphlSVRGNLryGMKRARPSERRISfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 233 KKADIYMFDEPSSYLDVRQRlkaAQVIRSLLR-HDSY---VIVVEHDLSVLDYLSDFV 286
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDDPRK---YEILPYLERlHAEFgipILYVSHSLQEVLRLADRV 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
102-541 |
3.08e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.03 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGklkpnlgrfntppdweeILTHFRGSELQSyfirvveENLKTAIKPQ--HVDYIKEv 179
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLRIMAG-----------------VDKDFNGEARPQ-------PGIKVGYLPQepQLDPTKT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 VRGN----LGKMLEKLDErglMEEICA-----DMELNQVLEREAR----------------------------------Q 216
Cdd:TIGR03719 85 VRENveegVAEIKDALDR---FNEISAkyaepDADFDKLAAEQAElqeiidaadawdldsqleiamdalrcppwdadvtK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 217 VSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQrlkAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL---YGKP 293
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELdrgRGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 294 --GAYgvvtlpfsvreginvflAGFIPTENLRFRDESLTFRVSETTQENDGE----------VKSYARY-KYPNMTKQ-- 358
Cdd:TIGR03719 239 weGNY-----------------SSWLEQKQKRLEQEEKEESARQKTLKRELEwvrqspkgrqAKSKARLaRYEELLSQef 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 ----------------LGDFKLEV--MEGEFTD-------------SQIIVMLGENGTGKTTFIRMLAGAFPREEGVQSE 407
Cdd:TIGR03719 302 qkrnetaeiyippgprLGDKVIEAenLTKAFGDklliddlsfklppGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 408 IPEFNVSYKPQGND----SKrecTVRQLL---HDKI---------RDACAHPQFMSDvirplqieqlmDQ--VVKTLSGG 469
Cdd:TIGR03719 382 GETVKLAYVDQSRDaldpNK---TVWEEIsggLDIIklgkreipsRAYVGRFNFKGS-----------DQqkKVGQLSGG 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 470 EKQRVAITLCLGKPADIYLIDEPSAHLDSEqritASKVIKRFILHAKKTAFIVEHDfimaTYLADRV----IVYEG 541
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVE----TLRALEEALLNFAGCAVVISHD----RWFLDRIathiLAFEG 515
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
103-275 |
3.08e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.16 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWEEILTHFrgselQSYFI---RVVEENLKTAIKPQ 171
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRPINMMF-----QSYALfphMTVEQNIAFGLKQD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HvdyikevvrgnlgkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD--V 249
Cdd:PRK11607 120 K---------------LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkL 184
|
170 180
....*....|....*....|....*.
gi 15231301 250 RQRLKaAQVIRSLLRHDSYVIVVEHD 275
Cdd:PRK11607 185 RDRMQ-LEVVDILERVGVTCVMVTHD 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
375-498 |
3.23e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 375 QIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipefNVSYKPQGNDSKRECTVRQLL-HdkiRDACaHP--------QF 445
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPPAAG--------TIKLDGGDIDDPDVAEACHYLgH---RNAM-KPaltvaenlEF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 446 MSDVI--RPLQIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDS 498
Cdd:PRK13539 97 WAAFLggEELDIAAALEAVglaplahlpFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
101-276 |
3.35e-10 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 58.98 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGselqsyfirvveenlktaikpqhvdyiKEVV 180
Cdd:cd03216 24 RRGEVHALLGENGAGKSTLMKILSGLYKPDSG---------EIL--VDG---------------------------KEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNLgkmleklderglmeeicadmelnqvleREAR--------QVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQR 252
Cdd:cd03216 66 FASP---------------------------RDARragiamvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180
....*....|....*....|....
gi 15231301 253 LKAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:cd03216 119 ERLFKVIRRLRAQGVAVIFISHRL 142
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
101-275 |
3.39e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilTHFRGSELQSyfirvVEENLKTAIKPQHVDYIKE-- 178
Cdd:PRK10584 34 KRGETIALIGESGSGKSTLLAILAGLDDGSSGE-----------VSLVGQPLHQ-----MDEEARAKLRAKHVGFVFQsf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 ----------------VVRGNLGKmleklDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDE 242
Cdd:PRK10584 98 mliptlnalenvelpaLLRGESSR-----QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 243 PSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHD 275
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNReHGTTLILVTHD 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
361-537 |
3.49e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 361 DFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFNVSYKPQGNDSKRECTV---------RQL 431
Cdd:PRK15064 337 NLNLLLEAGE-----RLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLtlfdwmsqwRQE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 432 LHDK--IRDACAHPQFMSDVIRplqieqlmdQVVKTLSGGEKQRVAI-TLCLGKPaDIYLIDEPSAHLDSEQRITASKVI 508
Cdd:PRK15064 412 GDDEqaVRGTLGRLLFSQDDIK---------KSVKVLSGGEKGRMLFgKLMMQKP-NVLVMDEPTNHMDMESIESLNMAL 481
|
170 180
....*....|....*....|....*....
gi 15231301 509 KRFilhaKKTAFIVEHDFIMATYLADRVI 537
Cdd:PRK15064 482 EKY----EGTLIFVSHDREFVSSLATRII 506
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
375-503 |
3.54e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 375 QIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipefNVSYKPQGNDSKRECTVRQLLHdkirdaCAHPQFMSDVIRPL- 453
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAG--------RVLLNGGPLDFQRDSIARGLLY------LGHAPGIKTTLSVLe 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 454 ------------QIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD--SEQRIT 503
Cdd:cd03231 93 nlrfwhadhsdeQVEEALARVglngfedrpVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkaGVARFA 165
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
101-277 |
3.55e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.18 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF---NTP-PDWEEILTHFR----GSELQsYFIRVVEENLKTAIKPQH 172
Cdd:cd03248 38 HPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldGKPiSQYEHKYLHSKvslvGQEPV-LFARSLQDNIAYGLQSCS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 VDYIKEV-VRGNLGKMLEKLdERGLMEEicadmelnqVLEREArQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQ 251
Cdd:cd03248 117 FECVKEAaQKAHAHSFISEL-ASGYDTE---------VGEKGS-QLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180
....*....|....*....|....*.
gi 15231301 252 RLKAAQVIRSLLRHDSyVIVVEHDLS 277
Cdd:cd03248 186 EQQVQQALYDWPERRT-VLVIAHRLS 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
81-286 |
4.03e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGANGF--KLHrLPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTppDWEEIlTHfrgSELQSYFIR 158
Cdd:PRK11432 10 KNITKRFGSNTVidNLN-LTIKQ-GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI--DGEDV-TH---RSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 159 VV------------EENLKTAIKPQHVDyiKEVVRGNLGKMLEKLDERGlmeeicadMElnqvlEREARQVSGGELQRFA 226
Cdd:PRK11432 82 MVfqsyalfphmslGENVGYGLKMLGVP--KEERKQRVKEALELVDLAG--------FE-----DRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 227 IAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSL-LRHDSYVIVVEHDLSVLDYLSDFV 286
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTV 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
369-509 |
4.48e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 59.98 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 369 GEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREE---------GVQSEIPEF--NVSYKPQGNDSKRECTVRQLLH---- 433
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsgqilfnGQPRKPDQFqkCVAYVRQDDILLPGLTVRETLTytai 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 434 --------DKIRDACAHPQFMSDvirpLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqrITAS 505
Cdd:cd03234 108 lrlprkssDAIRKKRVEDVLLRD----LALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS---FTAL 180
|
....
gi 15231301 506 KVIK 509
Cdd:cd03234 181 NLVS 184
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
345-542 |
4.53e-10 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 60.21 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 345 KSYARYKYPNmtKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------------VQSEIPE 410
Cdd:cd03257 9 VSFPTGGGSV--KALDDVSFSIKKGE-----TLGLVGESGSGKSTLARAILGLLKPTSGsiifdgkdllklsrRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 411 FNVSYKPQG-----NDSKrecTVRQLLHDKIRdacAHPQFMSDVIRPLQIEQLMDQVVKT----------LSGGEKQRVA 475
Cdd:cd03257 82 KEIQMVFQDpmsslNPRM---TIGEQIAEPLR---IHGKLSKKEARKEAVLLLLVGVGLPeevlnrypheLSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 476 I--TLCLgKPaDIYLIDEPSAHLDSeqritaskVIKRFILH-------AKKTAFI-VEHDFIMATYLADRVIV-YEGQ 542
Cdd:cd03257 156 IarALAL-NP-KLLIADEPTSALDV--------SVQAQILDllkklqeELGLTLLfITHDLGVVAKIADRVAVmYAGK 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
350-557 |
4.95e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.77 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKPQGNDSKREcTVR 429
Cdd:PRK13644 9 YSYPDGTPALENINLVIKKGEY-----IGIIGKNGSGKSTLALHLNGLLRPQKG------KVLVSGIDTGDFSKLQ-GIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 430 QLLHDKIRDAcaHPQFMSDVIR-------------PLQIEQLMDQVV-------------KTLSGGEKQRVAITLCLGKP 483
Cdd:PRK13644 77 KLVGIVFQNP--ETQFVGRTVEedlafgpenlclpPIEIRKRVDRALaeiglekyrhrspKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 484 ADIYLIDEPSAHLDSEQRITASKVIKRfiLHAK-KTAFIVEHDfIMATYLADRVIVYEGQPAVkcIAHSPQSLLS 557
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKK--LHEKgKTIVYITHN-LEELHDADRIIVMDRGKIV--LEGEPENVLS 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
101-289 |
5.66e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNT--------------PPDWEEILTHFRGSELQSYFIRVVEEnlkT 166
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeiKPVRKKVGVVFQFPESQLFEETVLKD---V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 167 AIKPQHVDYIKEVVRGNLGkmlEKLDERGLMEEIcadmelnqvLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:PRK13643 107 AFGPQNFGIPKEKAEKIAA---EKLEMVGLADEF---------WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 247 LDVRQRLKAAQVIRSLLRHDSYVIVVEHDL-SVLDYlSDFVCCL 289
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMdDVADY-ADYVYLL 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
102-284 |
5.75e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDWEeiLTHFRGSELQsyFIRVVEENLK--TAIKPQHVDyikEV 179
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIK--LGYFAQHQLE--FLRADESPLQhlARLAPQELE---QK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 VRGNLGKMLEKLDerglmeeicadmelnQVLErEARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDV--RQRLKAAq 257
Cdd:PRK10636 410 LRDYLGGFGFQGD---------------KVTE-ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLdmRQALTEA- 472
|
170 180
....*....|....*....|....*..
gi 15231301 258 virsLLRHDSYVIVVEHDLSVLDYLSD 284
Cdd:PRK10636 473 ----LIDFEGALVVVSHDRHLLRSTTD 495
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
101-277 |
6.86e-10 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 59.55 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTppDWEEI----LTHFRGSelqsyfIRVV---------------- 160
Cdd:cd03253 25 PAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI--DGQDIrevtLDSLRRA------IGVVpqdtvlfndtigynir 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 161 --------EENLKTAIKPQHVDYIKevvrgnlgKMLEKLD----ERGLMeeicadmelnqvlerearqVSGGELQRFAIA 228
Cdd:cd03253 97 ygrpdatdEEVIEAAKAAQIHDKIM--------RFPDGYDtivgERGLK-------------------LSGGEKQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 229 AVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSyVIVVEHDLS 277
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT-TIVIAHRLS 197
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
352-540 |
7.88e-10 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 58.96 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 352 YPNMTKQLGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGafpREEGVQSEIpefNVSYKPQGNDSKREC----- 426
Cdd:cd03292 10 YPNGTAALDGINISISAGEFV-----FLVGPSGAGKSTLLKLIYK---EELPTSGTI---RVNGQDVSDLRGRAIpylrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 ---TVRQ----LLHDKIRDACAHPQFMSDVIR---PLQIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPADIY 487
Cdd:cd03292 79 kigVVFQdfrlLPDRNVYENVAFALEVTGVPPreiRKRVPAALELVglshkhralPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 488 LIDEPSAHLDSEqriTASKVIKRF--ILHAKKTAFIVEHDFIMATYLADRVIVYE 540
Cdd:cd03292 159 IADEPTGNLDPD---TTWEIMNLLkkINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
362-558 |
8.91e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.21 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 362 FKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG------------VQSEIPefnVSYKPQGNDSKRECTVR 429
Cdd:PRK10771 18 FDLTVERGE-----RVAILGPSGAGKSTLLNLIAGFLTPASGsltlngqdhtttPPSRRP---VSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 430 Q---L-LHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITAS 505
Cdd:PRK10771 90 QnigLgLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 506 KVIKRFILHAKKTAFIVEHDFIMATYLADR-VIVYEGQpavkcIAH--SPQSLLSG 558
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRsLVVADGR-----IAWdgPTDELLSG 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
101-284 |
9.38e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.98 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNTPPDWEEILT-------HFRGSELQ--SYFIRVVEEnlKTAIk 169
Cdd:COG4778 35 AAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDLAQaspreilALRRRTIGyvSQFLRVIPR--VSAL- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 170 pqhvdyikEVVrgnlgkmLEKLDERGLMEEICadmelnqvlEREARQV------------------SGGELQRFAIAAVF 231
Cdd:COG4778 112 --------DVV-------AEPLLERGVDREEA---------RARARELlarlnlperlwdlppatfSGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 232 VKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSD 284
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAD 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
101-277 |
9.56e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.33 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAgklkpnlgRFNTPP--------------DWEEILTHFrGSELQSYFI--RVVEENL 164
Cdd:COG1132 364 PPGETVALVGPSGSGKSTLVNLLL--------RFYDPTsgrilidgvdirdlTLESLRRQI-GVVPQDTFLfsGTIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 165 KTAIKPQHVDYIKEVVR-GNLGKMLEKLDErGLmeeicadmelNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEP 243
Cdd:COG1132 435 RYGRPDATDEEVEEAAKaAQAHEFIEALPD-GY----------DTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 244 SSYLDVRQrlkAAQVIRSL--LRHDSYVIVVEHDLS 277
Cdd:COG1132 504 TSALDTET---EALIQEALerLMKGRTTIVIAHRLS 536
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
84-277 |
1.04e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 59.04 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 84 THRYGANG-FKLHRLPIP-RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWeeiLTHFRGSELQ 153
Cdd:cd03252 7 RFRYKPDGpVILDNISLRiKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaLADPAW---LRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 154 S--YFIRVVEENLKTAIKPQHVDYIKEVVRgnlgkmlekldERGLMEEICADME-LNQVLEREARQVSGGELQRFAIAAV 230
Cdd:cd03252 84 EnvLFNRSIRDNIALADPGMSMERVIEAAK-----------LAGAHDFISELPEgYDTIVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 231 FVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSyVIVVEHDLS 277
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRT-VIIIAHRLS 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
99-277 |
1.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.38 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 99 IPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FN----TPPDWEEILTH----FRGSELQsyFI-RVVEENLKTA 167
Cdd:PRK13648 32 IPK-GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifYNnqaiTDDNFEKLRKHigivFQNPDNQ--FVgSIVKYDVAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 168 IKPQHVDYikevvrgnlGKMLEKLDErgLMEEIcaDMeLNQVlEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYL 247
Cdd:PRK13648 109 LENHAVPY---------DEMHRRVSE--ALKQV--DM-LERA-DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 248 DVRQRLKAAQVIRSL-LRHDSYVIVVEHDLS 277
Cdd:PRK13648 174 DPDARQNLLDLVRKVkSEHNITIISITHDLS 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
101-287 |
1.19e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.99 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYfirvVEENLKTAIK--PQHVDYIKE 178
Cdd:PRK11160 364 KAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG---------EIL--LNGQPIADY----SEAALRQAISvvSQRVHLFSA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 VVRGNL---------GKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDV 249
Cdd:PRK11160 429 TLRDNLllaapnasdEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15231301 250 RQRlkaaQVIRSLLRH---DSYVIVVEHDLSVLDYLsDFVC 287
Cdd:PRK11160 509 ETE----RQILELLAEhaqNKTVLMITHRLTGLEQF-DRIC 544
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
348-538 |
1.32e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 59.05 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 348 ARYKYPNMTKQ-LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipefNVSY--KPQGNDSKR 424
Cdd:COG1124 9 VSYGQGGRRVPvLKDVSLEVAPGE-----SFGLVGESGSGKSTLLRALAGLERPWSG--------EVTFdgRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 E--CTVRQLLHDKirDACAHPQF-MSDVIR-PLQ----------IEQLMDQV----------VKTLSGGEKQRVAI--TL 478
Cdd:COG1124 76 AfrRRVQMVFQDP--YASLHPRHtVDRILAePLRihglpdreerIAELLEQVglppsfldryPHQLSGGQRQRVAIarAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 479 CLgKPaDIYLIDEPSAHLDSeqrITASKVIkRFILHAKK----TAFIVEHDFIMATYLADRVIV 538
Cdd:COG1124 154 IL-EP-ELLLLDEPTSALDV---SVQAEIL-NLLKDLREerglTYLFVSHDLAVVAHLCDRVAV 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
370-537 |
1.67e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 56.98 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 370 EFTDSQIIVMLGENGTGKTTFIR----MLAGAFPREEgvqseipefnvsykpQGNDSKRECTVrqllhdkirdACAHPQF 445
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDaiglALGGAQSATR---------------RRSGVKAGCIV----------AAVSAEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 446 MSdvirplqieqlmdqVVKTLSGGEKQRVAITLCLG----KPADIYLIDEPSAHLDSEQRITASKVIKRFILHaKKTAFI 521
Cdd:cd03227 72 IF--------------TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIV 136
|
170
....*....|....*.
gi 15231301 522 VEHDFIMATyLADRVI 537
Cdd:cd03227 137 ITHLPELAE-LADKLI 151
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
101-317 |
1.69e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 58.40 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWEEILTHFrgselQSYfirvveenlktAIKPqH 172
Cdd:cd03300 24 KEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkditNLPPHKRPVNTVF-----QNY-----------ALFP-H 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 VDYIKEVVrgnLGKMLEKLDERGLMEEICADMELNQVLEREAR---QVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDV 249
Cdd:cd03300 87 LTVFENIA---FGLRLKKLPKAEIKERVAEALDLVQLEGYANRkpsQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 250 RQRlKAAQV-IRSLlrHDSY---VIVVEHDLSVLDYLSDFVCCLygKPGAYGVVTLPFSV-REGINVFLAGFI 317
Cdd:cd03300 164 KLR-KDMQLeLKRL--QKELgitFVFVTHDQEEALTMSDRIAVM--NKGKIQQIGTPEEIyEEPANRFVADFI 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
101-306 |
1.85e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.85 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSY-------------F--IRV-----V 160
Cdd:PRK11300 29 REQEIVSLIGPNGAGKTTVFNCLTGFYKPTGG---------TIL--LRGQHIEGLpghqiarmgvvrtFqhVRLfremtV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 161 EENLKTAikpQHVDYIKEVVRGNLGKMLEKLDERGLMEEICA---DMELNQVLEREARQVSGGELQRFAIAAVFVKKADI 237
Cdd:PRK11300 98 IENLLVA---QHQQLKTGLFSGLLKTPAFRRAESEALDRAATwleRVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 238 YMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDLSVLDYLSDFVCCL-YGKPGAYGvvtLPFSVR 306
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVnQGTPLANG---TPEEIR 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
101-542 |
2.03e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQsyFIRVVE-ENLKTAIKPQHVDYIKEV 179
Cdd:COG1129 28 RPGEVHALLGENGAGKSTLMKILSGVYQPDSG---------EIL--LDGEPVR--FRSPRDaQAAGIAIIHQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 -VRGN--LGKMLEK---LDERGLME---EICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:COG1129 95 sVAENifLGREPRRgglIDWRAMRRrarELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 251 --QRLKAaqVIRSLLRHDSYVIVVEHDLS-VLDyLSDFVCCLygkpgaygvvtlpfsvREGINVflaGFIPTENLRfRDE 327
Cdd:COG1129 175 evERLFR--IIRRLKAQGVAIIYISHRLDeVFE-IADRVTVL----------------RDGRLV---GTGPVAELT-EDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 328 --------SLTFRVSETTQENDG---EVKSYARykypnmTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAG 396
Cdd:COG1129 232 lvrlmvgrELEDLFPKRAAAPGEvvlEVEGLSV------GGVVRDVSFSVRAGE-----ILGIAGLVGAGRTELARALFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 397 AFPREEGvqsEI-----------------------PE--------------FNVSYKPQGNDSKRectvRQLLHDKIRDA 439
Cdd:COG1129 301 ADPADSG---EIrldgkpvrirsprdairagiayvPEdrkgeglvldlsirENITLASLDRLSRG----GLLDRRRERAL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 440 CAHpqfmsdvirplQIEQL------MDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFI- 512
Cdd:COG1129 374 AEE-----------YIKRLriktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID----VGAKAEIYRLIr 438
|
490 500 510
....*....|....*....|....*....|....*
gi 15231301 513 -LHAKKTAFIV---EHDFIMAtyLADRVIV-YEGQ 542
Cdd:COG1129 439 eLAAEGKAVIVissELPELLG--LSDRILVmREGR 471
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
375-541 |
2.07e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.49 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 375 QIIVMLGENGTGKTT----FIRMLAgafPREEGVQSE---IPEFN-------VSYKPQGNDSKRECTVRQLL-------- 432
Cdd:PRK11231 29 KITALIGPNGCGKSTllkcFARLLT---PQSGTVFLGdkpISMLSsrqlarrLALLPQHHLTPEGITVRELVaygrspwl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 433 --------HDKIRDACAhpqfMSDvirpLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITA 504
Cdd:PRK11231 106 slwgrlsaEDNARVNQA----MEQ----TRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 15231301 505 SKVIKRfiLHAK-KTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:PRK11231 178 MRLMRE--LNTQgKTVVTVLHDLNQASRYCDHLVVLAN 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
103-286 |
2.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPD-------WE---EILTHFRGSELQsyFI-RVVEENLKTAIKPQ 171
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvWDirhKIGMVFQNPDNQ--FVgATVEDDVAFGLENK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HVDYIKEVVRGNlgkmlEKLDERGLMEeicadmelnqVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQ 251
Cdd:PRK13650 111 GIPHEEMKERVN-----EALELVGMQD----------FKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 252 RLKAAQVIRSLL-RHDSYVIVVEHDLSVLDyLSDFV 286
Cdd:PRK13650 176 RLELIKTIKGIRdDYQMTVISITHDLDEVA-LSDRV 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
103-277 |
2.34e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.46 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAgklkpnlgRFNTPPDWEEILThfrGSELQSYFIRVVEENL----KTAIKPQHVDYIKE 178
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLS--------RLMTPAHGHVWLD---GEHIQHYASKEVARRIgllaQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 VVRGN-----LGKMLEKLDErglmEEICADMELNQVLEREARQV---SGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:PRK10253 102 VARGRyphqpLFTRWRKEDE----EAVTKAMQATGITHLADQSVdtlSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180
....*....|....*....|....*...
gi 15231301 251 QRLKAAQVIRSLLRHDSYVI-VVEHDLS 277
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLaAVLHDLN 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
81-276 |
3.13e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 57.46 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGanGFKLH-RLPIPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeILthFRGSELQSYFI-- 157
Cdd:COG3840 5 DDLTYRYG--DFPLRfDLTIA-AGERVAILGPSGAGKSTLLNLIAGFLPPDSGR---------IL--WNGQDLTALPPae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 158 RVV-----EENLKTaikpqHVDyikevVRGNLGKMLE---KL--DERGLMEEICADMELNQVLEREARQVSGGELQRFAI 227
Cdd:COG3840 71 RPVsmlfqENNLFP-----HLT-----VAQNIGLGLRpglKLtaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15231301 228 AAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDL 276
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDP 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
102-276 |
3.44e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.98 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppDWEEILTHFRGSELQsyfirvveENLKTAikpQHVDYIKEV-- 179
Cdd:TIGR01189 25 AGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV----RWNGTPLAEQRDEPH--------ENILYL---GHLPGLKPEls 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 VRGNLGKMLEKL-DERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR-QRLKAAQ 257
Cdd:TIGR01189 90 ALENLHFWAAIHgGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAgVALLAGL 169
|
170
....*....|....*....
gi 15231301 258 VIRSLLRHDSYVIVVEHDL 276
Cdd:TIGR01189 170 LRAHLARGGIVLLTTHQDL 188
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
102-276 |
3.56e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.10 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNtppdweeiLTHFRGSELQSYFIR----VVEENlktaikP--QHVDY 175
Cdd:PRK13635 32 EGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT--------VGGMVLSEETVWDVRrqvgMVFQN------PdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IKE--VVRG--NLG----KMLEKLDErglmeeicadmELNQV-----LEREARQVSGGELQRFAIAAVFVKKADIYMFDE 242
Cdd:PRK13635 98 TVQddVAFGleNIGvpreEMVERVDQ-----------ALRQVgmedfLNREPHRLSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190
....*....|....*....|....*....|....*
gi 15231301 243 PSSYLDVRQRLKAAQVIRSLLRH-DSYVIVVEHDL 276
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKEQkGITVLSITHDL 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
354-538 |
3.57e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 57.63 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGaFprEEGVQSEI-----PEFNV-SYKPQGNd 421
Cdd:cd03300 5 NVSKFYGGFValdgvsLDIKEGEF-----FTLLGPSGCGKTTLLRLIAG-F--ETPTSGEIlldgkDITNLpPHKRPVN- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 422 skrecTVRQ----LLHDKIRDACAHP---QFMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPAD 485
Cdd:cd03300 76 -----TVFQnyalFPHLTVFENIAFGlrlKKLPKAEIKERVAEALDLVqlegyanrkPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 486 IYLIDEPSAHLDSEQRITASKVIKRfiLHAK-KTAFI-VEHDFIMATYLADRVIV 538
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKR--LQKElGITFVfVTHDQEEALTMSDRIAV 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
103-290 |
3.70e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFN---------TPPDWEEILthfrgSELQSYFI-------------RVV 160
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmKDDEWRAVR-----SDIQMIFQdplaslnprmtigEII 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 161 EENLKTAIKPQHVDYIKEVVRgnlgKMLEKLderGLmeeicadmeLNQVLEREARQVSGGELQRFAIAAVFVKKADIYMF 240
Cdd:PRK15079 122 AEPLRTYHPKLSRQEVKDRVK----AMMLKV---GL---------LPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 241 DEPSSYLDVRQRlkaAQVI---RSLLRH-DSYVIVVEHDLSVLDYLSDFVCCLY 290
Cdd:PRK15079 186 DEPVSALDVSIQ---AQVVnllQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
349-543 |
3.94e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.78 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKPQGNDSKRECTV 428
Cdd:PRK13639 8 KYSYPDGTEALKGINFKAEKGE-----MVALLGPNGAGKSTLFLHFNGILKPTSG------EVLIKGEPIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQ---LLHDKIRDACAHPQFMSDV-IRPLQIEQLMDQVVKT--------------------LSGGEKQRVAITLCLGKPA 484
Cdd:PRK13639 77 RKtvgIVFQNPDDQLFAPTVEEDVaFGPLNLGLSKEEVEKRvkealkavgmegfenkpphhLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 485 DIYLIDEPSAHLDSeqrITASKVIKRFILHAKK--TAFIVEHDFIMATYLADRV-------IVYEGQP 543
Cdd:PRK13639 157 EIIVLDEPTSGLDP---MGASQIMKLLYDLNKEgiTIIISTHDVDLVPVYADKVyvmsdgkIIKEGTP 221
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
6-73 |
4.03e-09 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 53.52 E-value: 4.03e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 6 TRIAIVSEDRCKpkKCRQeCKKSCPVvktgkLCIEVGSTsKSAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:COG1144 22 VERPVVDEDKCI--GCGL-CWIVCPD-----GAIRVDDG-KYYGIDYDYCKGCGICAEVCPVKAIEMV 80
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
344-543 |
4.80e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.69 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 344 VKSYARYKYPNMTKQLGDFKL-EVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEGV----QSEIPEF------- 411
Cdd:PRK10253 2 TESVARLRGEQLTLGYGKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHvwldGEHIQHYaskevar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 412 NVSYKPQGNDSKRECTVRQLLhdkIRDACAH-PQF----------MSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCL 480
Cdd:PRK10253 82 RIGLLAQNATTPGDITVQELV---ARGRYPHqPLFtrwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 481 GKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLA-------DRVIVYEGQP 543
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYAshlialrEGKIVAQGAP 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
359-565 |
4.94e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAgafpreegvQSEIP----------EFNVSYKPQGNDSKR---- 424
Cdd:COG4161 18 LFDINLECPSGE-----TLVLLGPSGAGKSSLLRVLN---------LLETPdsgqlniaghQFDFSQKPSEKAIRLlrqk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 ------------ECTVRQLLHD------KIRDACAHPQFMSDVIRpLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADI 486
Cdd:COG4161 84 vgmvfqqynlwpHLTVMENLIEapckvlGLSKEQAREKAMKLLAR-LRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 487 YLIDEPSAHLDSEqrITASKV-IKRFILHAKKTAFIVEHDFIMATYLADRV-------IVYEGQPAvkCIAHsPQSllSG 558
Cdd:COG4161 163 LLFDEPTAALDPE--ITAQVVeIIRELSQTGITQVIVTHEVEFARKVASQVvymekgrIIEQGDAS--HFTQ-PQT--EA 235
|
....*..
gi 15231301 559 MNHFLSH 565
Cdd:COG4161 236 FAHYLSH 242
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
375-542 |
5.60e-09 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 56.81 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 375 QIIVMLGENGTGKTTFIRMLAGAFPREEGVQSE----IPEFNVsYKPQGNDSKRECT---VRQ---LLHDKIRDACAHPQ 444
Cdd:cd03260 27 EITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgevlLDGKDI-YDLDVDVLELRRRvgmVFQkpnPFPGSIYDNVAYGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 445 FMSDVIRPLQIEQLMDQVVKT---------------LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqriTASKVIK 509
Cdd:cd03260 106 RLHGIKLKEELDERVEEALRKaalwdevkdrlhalgLSGGQQQRLCLARALANEPEVLLLDEPTSALDP----ISTAKIE 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 510 RFILHAKK--TAFIVEHDFIMATYLADRVIV-YEGQ 542
Cdd:cd03260 182 ELIAELKKeyTIVIVTHNMQQAARVADRTAFlLNGR 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
458-593 |
6.63e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 458 LMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVI 537
Cdd:PRK13646 138 VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVI 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 538 VY-EGQPAVKCiahSPQSLLSGMNHFLS-HLNItfrrdptnfrPRINKLEsiKDKEQK 593
Cdd:PRK13646 218 VMkEGSIVSQT---SPKELFKDKKKLADwHIGL----------PEIVQLQ--YDFEQK 260
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
101-278 |
6.83e-09 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 56.81 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNtppdwEEILTHFRGSELQSYFIRVV----EENLktaIKPQHVd 174
Cdd:cd03256 25 NPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlID-----GTDINKLKGKALRQLRRQIGmifqQFNL---IERLSV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 yIKEVVRGNLGKM------------------LEKLDERGLMEeicadmelnqVLEREARQVSGGELQRFAIAAVFVKKAD 236
Cdd:cd03256 96 -LENVLSGRLGRRstwrslfglfpkeekqraLAALERVGLLD----------KAYQRADQLSGGQQQRVAIARALMQQPK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 237 IYMFDEPSSYLDVrqrlKAAQVIRSLLR-----HDSYVIVVEHDLSV 278
Cdd:cd03256 165 LILADEPVASLDP----ASSRQVMDLLKrinreEGITVIVSLHQVDL 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
190-291 |
6.86e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 190 KLDERGLMEEICADMEL----NQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSL-LR 264
Cdd:PRK14258 120 KLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLR 199
|
90 100
....*....|....*....|....*..
gi 15231301 265 HDSYVIVVEHDLSVLDYLSDFVCCLYG 291
Cdd:PRK14258 200 SELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
359-542 |
7.17e-09 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 56.74 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGV------------QSEIPEF--NVSYKPQGN---D 421
Cdd:cd03261 16 LKGVDLDVRRGE-----ILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgedisglsEAELYRLrrRMGMLFQSGalfD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 422 SKrecTVRQ----LLHDkirdacaHPQFMSDVIRPLQIEQL--------MDQVVKTLSGGEKQRVAI--TLCLgKPaDIY 487
Cdd:cd03261 91 SL---TVFEnvafPLRE-------HTRLSEEEIREIVLEKLeavglrgaEDLYPAELSGGMKKRVALarALAL-DP-ELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 488 LIDEPSAHLDSeqriTASKVIKRFILHAKK----TAFIVEHDFIMATYLADRVIV-YEGQ 542
Cdd:cd03261 159 LYDEPTAGLDP----IASGVIDDLIRSLKKelglTSIMVTHDLDTAFAIADRIAVlYDGK 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
376-499 |
7.39e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 55.83 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 376 IIVMLGENGTGKTTFIRMLAGAFPREEGV----------QSEIPEFNVSYKPQGNDSKRECTVRQLLHDKIRDACAHPQF 445
Cdd:TIGR01189 28 ALQVTGPNGIGKTTLLRILAGLLRPDSGEvrwngtplaeQRDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQRT 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 446 MSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:TIGR01189 108 IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
102-278 |
7.57e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---------FNTPPDWEEILTHFR--GSELQSYFI---RVVEENLKTA 167
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdFSQKPSEKAIRLLRQkvGMVFQQYNLwphLTVMENLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 168 ikPQHVdyikevvrgnLGkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYL 247
Cdd:COG4161 107 --PCKV----------LG--LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 248 DVRQRLKAAQVIRSLLRHDSYVIVVEHDLSV 278
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVIVTHEVEF 203
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-72 |
7.67e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 56.65 E-value: 7.67e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 8 IAIVSEDRCKpkKCRQeCKKSCPVvktgkLCIEVGSTSKSAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1145 176 KAVIDAEKCI--GCGL-CVKVCPT-----GAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISL 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
103-257 |
7.75e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.03 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPDWEEILTHFrgselQSYFI---RVVEENLKTAIKPQ 171
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqditHVPAENRHVNTVF-----QSYALfphMTVFENVAFGLRMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HV--DYIKEVVRGNLgKMLeKLDERGlmeeicadmelnqvlEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDV 249
Cdd:PRK09452 115 KTpaAEITPRVMEAL-RMV-QLEEFA---------------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170
....*....|....
gi 15231301 250 RQR------LKAAQ 257
Cdd:PRK09452 178 KLRkqmqneLKALQ 191
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
7-73 |
8.23e-09 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 52.42 E-value: 8.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 7 RIAIVSEDRCKpkKCRQeCKKSCPvvkTGklCIEVGsTSKSAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:COG1149 4 KIPVIDEEKCI--GCGL-CVEVCP---EG--AIKLD-DGGAPVVDPDLCTGCGACVGVCPTGAITLE 61
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-277 |
8.32e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTppDWEEIlthfRGSELQSY-------------FIRVVEENLKTA 167
Cdd:PRK13657 359 KPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI--DGTDI----RTVTRASLrrniavvfqdaglFNRSIEDNIRVG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 168 iKPQHVDyiKEVVRGnlGKMLEKLD--ERglmeeicADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:PRK13657 433 -RPDATD--EEMRAA--AERAQAHDfiER-------KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 246 YLDV--RQRLKAAQvirSLLRHDSYVIVVEHDLS 277
Cdd:PRK13657 501 ALDVetEAKVKAAL---DELMKGRTTFIIAHRLS 531
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
10-70 |
8.72e-09 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 53.94 E-value: 8.72e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 10 IVSEDRCKpkKCRQeCKKSCPV--VKTGKLCIEVGSTSKSAFISEELCIGCGICVKKCPFEAI 70
Cdd:cd10549 36 EIDEDKCV--FCGA-CVEVCPTgaIELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAI 95
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
322-538 |
9.57e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.24 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 322 LRFRDESLTFRVSETTQENDGEVKSYARYKYPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPRE 401
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGE-----SVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 402 EG---VQSEIP---EFNVSYKPQ--GND-----------SKREctVRQLLhDKIRDacahpqFmSDvirplqIEQLMDQV 462
Cdd:COG1134 80 SGrveVNGRVSallELGAGFHPEltGREniylngrllglSRKE--IDEKF-DEIVE------F-AE------LGDFIDQP 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 463 VKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAkKTAFIVEHDFIMATYLADRVIV 538
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIW 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
444-537 |
1.03e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.02 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 444 QFMSDV-IRPLQIEQLMdqvvKTLSGGEKQRVAITLCLGKPAD--IYLIDEPSAHLDSEQRITASKVIKRfILHAKKTAF 520
Cdd:cd03238 69 QFLIDVgLGYLTLGQKL----STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG-LIDLGNTVI 143
|
90
....*....|....*..
gi 15231301 521 IVEHDFIMATYlADRVI 537
Cdd:cd03238 144 LIEHNLDVLSS-ADWII 159
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
466-540 |
1.05e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.61 E-value: 1.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYE 540
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIE 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
103-274 |
1.06e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 56.13 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLkPNLGRFN----------TPPDWEEILTHFRGSE-LQSYFirVVEENLK-TAIKP 170
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSgqilfngqprKPDQFQKCVAYVRQDDiLLPGL--TVRETLTyTAILR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 171 QHvdyikevvRGNLGKMLEKLDERGLMEEiCADMELNQVLereARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:cd03234 110 LP--------RKSSDAIRKKRVEDVLLRD-LALTRIGGNL---VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....
gi 15231301 251 QRLKAAQVIRSLLRHDSYVIVVEH 274
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-541 |
1.07e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 365 EVMEG---EFTDSQIIVMLGENGTGKTTFIRML--AGAFPREEGVQSEIPEFNVS-YKPQGNDSKRECTVrQLLHDK--- 435
Cdd:PRK14258 21 KILEGvsmEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEFFNQNiYERRVNLNRLRRQV-SMVHPKpnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 436 ----IRDACA--------HPQFMSDVI--RPLQIEQLMDQVVKT-------LSGGEKQRVAITLCLGKPADIYLIDEPSA 494
Cdd:PRK14258 100 fpmsVYDNVAygvkivgwRPKLEIDDIveSALKDADLWDEIKHKihksaldLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 495 HLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
377-521 |
1.09e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.85 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 377 IVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFN-------VSYKPQGndskrecTVRQLLhdkirdacahpqfmsdv 449
Cdd:cd03223 30 LLITGPSGTGKSSLFRALAGLWPWGSG-RIGMPEGEdllflpqRPYLPLG-------TLREQL----------------- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 450 IRPLQieqlmdqvvKTLSGGEKQRVAIT-LCLGKPaDIYLIDEPSAHLD--SEQRITAskvikrfILHAKKTAFI 521
Cdd:cd03223 85 IYPWD---------DVLSGGEQQRLAFArLLLHKP-KFVFLDEATSALDeeSEDRLYQ-------LLKELGITVI 142
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
210-285 |
1.11e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 55.73 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 210 LEREARQVSGGELQRFAIAAVFVKKAD--IYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVL---DYLSD 284
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIraaDHVID 210
|
.
gi 15231301 285 F 285
Cdd:cd03270 211 I 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
354-556 |
1.27e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.15 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDfKLEVMEGEFTDS--QIIVMLGENGTGKTTFIRMLAGAFPREEGV----------QSEIPEFNVSYKPQGND 421
Cdd:PRK13536 46 GVSKSYGD-KAVVNGLSFTVAsgECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgvpvpaRARLARARIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 422 SKRECTVRQLLHDKIRDACAHPQFMSDVIRPL----QIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD 497
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTREIEAVIPSLlefaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 498 SEQRITASKVIkRFILHAKKTAFIVEHDFIMATYLADRVIVYEGqpAVKCIAHSPQSLL 556
Cdd:PRK13536 205 PHARHLIWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVLEA--GRKIAEGRPHALI 260
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
6-77 |
1.30e-08 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 51.59 E-value: 1.30e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 6 TRIAIVSEDRCKpkKCRqECKKSCPVvktgkLCIEVgsTSKSAFISEELCIGCGICVKKCPFEAIQIINLPK 77
Cdd:COG2221 7 TWPPKIDEEKCI--GCG-LCVAVCPT-----GAISL--DDGKLVIDEEKCIGCGACIRVCPTGAIKGEKPKK 68
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
7-73 |
1.32e-08 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 53.89 E-value: 1.32e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 7 RIAIV-SEDRCKPKKCRQ----ECKKSCPVvktGKLCIEVGSTSksafISEELCIGCGICVKKCPFEAIQII 73
Cdd:COG1142 37 RIRVVrKAGVSAPVQCRHcedaPCAEVCPV---GAITRDDGAVV----VDEEKCIGCGLCVLACPFGAITMV 101
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
99-276 |
1.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.35 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 99 IPRpGQVLGLVGTNGIGKSTALKILAGKLKPNlgrfntppDWEEILTHFRGSELQSYFIRVVEEnlKTAIKPQHVD--YI 176
Cdd:PRK13640 30 IPR-GSWTALIGHNGSGKSTISKLINGLLLPD--------DNPNSKITVDGITLTAKTVWDIRE--KVGIVFQNPDnqFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEVVRGNLGKMLE-KLDERGLMEEICADMeLNQV-----LEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:PRK13640 99 GATVGDDVAFGLEnRAVPRPEMIKIVRDV-LADVgmldyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180
....*....|....*....|....*..
gi 15231301 251 QRLKAAQVIRSLLRHDSYVIV-VEHDL 276
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVIsITHDI 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
84-304 |
1.38e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 84 THRYGANGFKLHRLPIPRpGQVLGLVGTNGIGKSTALKILAGKLKpnlgrfntppdweeiLTHFRGSELQSYFIRVVEEN 163
Cdd:PRK15056 15 TWRNGHTALRDASFTVPG-GSIAALVGVNGSGKSTLFKALMGFVR---------------LASGKISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 164 LkTAIKPQ--HVDY-----IKEVVR-GNLGKM----LEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVF 231
Cdd:PRK15056 79 L-VAYVPQseEVDWsfpvlVEDVVMmGRYGHMgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 232 VKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYGKPGAYGVVTLPFS 304
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFT 230
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
7-90 |
1.38e-08 |
|
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 54.19 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 7 RIAIVSEDR-CKPKKCRQ-E---CKKSCPVvktGKLCIEVGSTsksaFISEELCIGCGICVKKCPFEAIQII-NLPKDLA 80
Cdd:cd10554 41 RLRVVKTGEvTAPVQCRQcEdapCANVCPV---GAISQEDGVV----QVDEERCIGCKLCVLACPFGAIEMApTTVPGVD 113
|
90
....*....|
gi 15231301 81 KDTTHRYGAN 90
Cdd:cd10554 114 WERGPRAVAV 123
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
101-278 |
1.39e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.41 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKST-ALKILagKLKPNLGR--FNTPPdweeiLTHFRGSELQSYF--IRVVEENLKTAIKPQ-HVD 174
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTtGLALL--RLINSQGEiwFDGQP-----LHNLNRRQLLPVRhrIQVVFQDPNSSLNPRlNVL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 YIKE----VVRGNLGKMLEKLDERGLMEEICADMELNQvleREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDvr 250
Cdd:PRK15134 383 QIIEeglrVHQPTLSAAQREQQVIAVMEEVGLDPETRH---RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-- 457
|
170 180 190
....*....|....*....|....*....|...
gi 15231301 251 qRLKAAQvIRSLL-----RHDSYVIVVEHDLSV 278
Cdd:PRK15134 458 -KTVQAQ-ILALLkslqqKHQLAYLFISHDLHV 488
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
102-283 |
1.40e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGklkpnlgrFNTPPDWEEIlthFRGSELQSyfirvVEENLKTAIKPQHVDYIK---- 177
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGG--------LDTPTSGDVI---FNGQPMSK-----LSSAAKAELRNQKLGFIYqfhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 178 --------EVVRGNL---GKMLEKLDERGLmeEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:PRK11629 98 llpdftalENVAMPLligKKKPAEINSRAL--EMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15231301 247 LDVRQrlkaAQVIRSLL-----RHDSYVIVVEHDLSVLDYLS 283
Cdd:PRK11629 176 LDARN----ADSIFQLLgelnrLQGTAFLVVTHDLQLAKRMS 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
359-538 |
1.56e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAfprEEGVQSEI--PEFNVSYKPQgndSKREC-TVRQ----L 431
Cdd:PRK09452 30 ISNLDLTINNGEF-----LTLLGPSGCGKTTVLRLIAGF---ETPDSGRImlDGQDITHVPA---ENRHVnTVFQsyalF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 432 LHDKIRDACAHPQFMSDV----IRP--------LQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:PRK09452 99 PHMTVFENVAFGLRMQKTpaaeITPrvmealrmVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15231301 500 QRITASKVIKRfiLHAK-KTAFI-VEHDFIMATYLADRVIV 538
Cdd:PRK09452 179 LRKQMQNELKA--LQRKlGITFVfVTHDQEEALTMSDRIVV 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
101-264 |
1.56e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 56.64 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------NTPPdweeiltHFRGSEL--QSYfirvveenlktAIKP 170
Cdd:COG3842 29 EPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgrdvtGLPP-------EKRNVGMvfQDY-----------ALFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 171 qHVDyikevVRGNLG---KM--LEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:COG3842 91 -HLT-----VAENVAfglRMrgVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170
....*....|....*....
gi 15231301 246 YLDVRQRLKAAQVIRSLLR 264
Cdd:COG3842 165 ALDAKLREEMREELRRLQR 183
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
101-277 |
1.95e-08 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 54.84 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--------FNTPPDWEEILTHFrGSELQSYFI---RVVEENLKTA-I 168
Cdd:cd03262 24 KKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglklTDDKKNINELRQKV-GMVFQQFNLfphLTVLENITLApI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 169 KPQHVDYiKEVVRgnlgKMLEKLDERGLMEEICAdmelnqvlerEARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:cd03262 103 KVKGMSK-AEAEE----RALELLEKVGLADKADA----------YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190
....*....|....*....|....*....|..
gi 15231301 249 ---VRQRLkaaQVIRSLLRHDSYVIVVEHDLS 277
Cdd:cd03262 168 pelVGEVL---DVMKDLAEEGMTMVVVTHEMG 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
359-538 |
2.12e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.55 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqseipefnvsykpqgndskrECTV--RQLLHDKI 436
Cdd:PRK13548 18 LDDVSLTLRPGEVV-----AILGPNGAGKSTLLRALSGELSPDSG---------------------EVRLngRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 437 RDACAH----PQFMS--------DVIR----PLQ---------IEQLMDQV---------VKTLSGGEKQRV--AITLC- 479
Cdd:PRK13548 72 AELARRravlPQHSSlsfpftveEVVAmgraPHGlsraeddalVAAALAQVdlahlagrdYPQLSGGEQQRVqlARVLAq 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 480 LGKPAD---IYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK13548 152 LWEPDGpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
350-538 |
2.17e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.51 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEG----VQSEIPEFN-------VSYKPQ 418
Cdd:PRK13647 12 FRYKDGTKALKGLSLSIPEGSKT-----ALLGPNGAGKSTLLLHLNGIYLPQRGrvkvMGREVNAENekwvrskVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 GNDSkrectvrQLLHDKIRDACAH-PQFM-----------SDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADI 486
Cdd:PRK13647 87 DPDD-------QVFSSTVWDDVAFgPVNMgldkdeverrvEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 487 YLIDEPSAHLDSEQRITASKVIKRfiLHAK-KTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDR--LHNQgKTVIVATHDVDLAAEWADQVIV 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
350-542 |
2.19e-08 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 54.14 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTK-QLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIPEFNVSYKPQGNDSKREC-- 426
Cdd:cd03246 8 FRYPGAEPpVLRNVSFSIEPGES-----LAIIGPSGSGKSTLARLILGLLRPTSG---RVRLDGADISQWDPNELGDHvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 TVRQ---LLHDKIRDAcahpqfmsdvirplqieqlmdqvvkTLSGGEKQRVAITLCL-GKPAdIYLIDEPSAHLDS--EQ 500
Cdd:cd03246 80 YLPQddeLFSGSIAEN-------------------------ILSGGQRQRLGLARALyGNPR-ILVLDEPNSHLDVegER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15231301 501 RITAskVIKRFILhAKKTAFIVEHDfiMATY-LADRVIVYEGQ 542
Cdd:cd03246 134 ALNQ--AIAALKA-AGATRIVIAHR--PETLaSADRILVLEDG 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
101-279 |
2.25e-08 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 54.14 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilthfrgselqsyfIRVveenlktaikpQHVDyIKEVV 180
Cdd:cd03246 26 EPGESLAIIGPSGSGKSTLARLILGLLRPTSGR-----------------------VRL-----------DGAD-ISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNLGKML------EKLDERGLMEEIcadmelnqvlerearqVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLK 254
Cdd:cd03246 71 PNELGDHVgylpqdDELFSGSIAENI----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180
....*....|....*....|....*
gi 15231301 255 AAQVIRSLLRHDSYVIVVEHDLSVL 279
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHRPETL 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
375-530 |
2.50e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 375 QIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIpefnvsykpqgNDSKRECTVRQLLHDKIRdacahpqfmsdvirplq 454
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYI-----------DGEDILEEVLDQLLLIIV----------------- 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 455 ieqlmDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVehDFIMAT 530
Cdd:smart00382 55 -----GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL--TVILTT 123
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
102-499 |
2.60e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNtppdweeILTHFRGSELQ---------SYFIRVVE--ENLKTAIKP 170
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII-------YEQDLIVARLQqdpprnvegTVYDFVAEgiEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 171 QH-------VDYIKEVVRgNLGKMLEKLDERGL------MEEICADMELNQvlEREARQVSGGELQRFAIAAVFVKKADI 237
Cdd:PRK11147 101 YHdishlveTDPSEKNLN-ELAKLQEQLDHHNLwqlenrINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 238 YMFDEPSSYLDV------RQRLKAAQVIRSLLRHDSYVI------VVEHDLSVL-DYLSDFVCCLYGKPGAYGVVTLP-- 302
Cdd:PRK11147 178 LLLDEPTNHLDIetiewlEGFLKTFQGSIIFISHDRSFIrnmatrIVDLDRGKLvSYPGNYDQYLLEKEEALRVEELQna 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 303 -FS---------VREGINVflagfiptenLRFRDE---------------------SLTFRVSETTQ--------ENdge 343
Cdd:PRK11147 258 eFDrklaqeevwIRQGIKA----------RRTRNEgrvralkalrrerserrevmgTAKMQVEEASRsgkivfemEN--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 344 vksyARYKYPNmtKQL-GDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG-----VQSEIPEF------ 411
Cdd:PRK11147 325 ----VNYQIDG--KQLvKDFSAQVQRGD-----KIALIGPNGCGKTTLLKLMLGQLQADSGrihcgTKLEVAYFdqhrae 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 412 ---------NVSykpqgnDSKRECTV----RQLLhDKIRDACAHPQfmsdviRPLQieqlmdqVVKTLSGGEKQRVAITL 478
Cdd:PRK11147 394 ldpektvmdNLA------EGKQEVMVngrpRHVL-GYLQDFLFHPK------RAMT-------PVKALSGGERNRLLLAR 453
|
490 500
....*....|....*....|.
gi 15231301 479 CLGKPADIYLIDEPSAHLDSE 499
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVE 474
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
9-70 |
2.65e-08 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 52.78 E-value: 2.65e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 9 AIVSEDRCKpkKCRqECKKSCPVvktGKLCIEVGstsKSAFISEELCIGCGICVKKCPFEAI 70
Cdd:cd10549 73 AEIDEEKCI--GCG-LCVKVCPV---DAITLEDE---LEIVIDKEKCIGCGICAEVCPVNAI 125
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
101-292 |
2.74e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFN------TPPDWEEILTHFR---GSELQSYFIRVVEENLKTAIK-- 169
Cdd:PRK13641 31 EEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhiTPETGNKNLKKLRkkvSLVFQFPEAQLFENTVLKDVEfg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 170 PQHVDYIKEVVRGNLGKMLEKLderGLMEeicadmelnQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDV 249
Cdd:PRK13641 111 PKNFGFSEDEAKEKALKWLKKV---GLSE---------DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 250 RQRLKAAQVIRSLLRHDSYVIVVEHDL-SVLDYLSDFVCCLYGK 292
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGK 222
|
|
| RLI |
pfam04068 |
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in ... |
6-37 |
2.82e-08 |
|
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in endoribonuclease RNase L inhibitor. Found at the N-terminal end of RNase L inhibitor proteins, adjacent to the 4Fe-4S binding domain, fer4, pfam00037. Also often found adjacent to the DUF367 domain pfam04034 in uncharacterized proteins. The RNase L system plays a major role in the anti-viral and anti-proliferative activities of interferons, and could possibly play a more general role in the regulation of RNA stability in mammalian cells. Inhibitory activity requires concentration-dependent association of RLI with RNase L.
Pssm-ID: 427689 [Multi-domain] Cd Length: 35 Bit Score: 49.82 E-value: 2.82e-08
10 20 30
....*....|....*....|....*....|....*
gi 15231301 6 TRIAIVSEDRCKPKKCRQ-ECKKSCPV--VKTGKL 37
Cdd:pfam04068 1 MRLAIVDFDQCDPKKCTGrKCIRFCPVreVRTGKK 35
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
8-72 |
2.93e-08 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 50.48 E-value: 2.93e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 8 IAIVSEDRCKpkKCRqECKKSCPVVktgklCIEVGSTSKSAF-ISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1146 2 MPVIDTDKCI--GCG-ACVEVCPVD-----VLELDEEGKKALvINPEECIGCGACELVCPVGAITV 59
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
371-542 |
3.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 371 FTDSQIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEF----NVSYKPQGNDSKRECTV------RQLLHDKI-RDA 439
Cdd:PRK13645 34 FKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG-QTIVGDYaipaNLKKIKEVKRLRKEIGLvfqfpeYQLFQETIeKDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 440 CAHP--------QFMSDVIRPLQIEQLMDQVVK----TLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKV 507
Cdd:PRK13645 113 AFGPvnlgenkqEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 508 IKRFILHAKKTAFIVEHDFIMATYLADRVIV-YEGQ 542
Cdd:PRK13645 193 FERLNKEYKKRIIMVTHNMDQVLRIADEVIVmHEGK 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
101-284 |
3.48e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQsyFIRVVEE-NLKTAIKPQHVDYIKEV 179
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-----------LIDGQEMR--FASTTAAlAAGVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 -VRGN--LGKMLEK---LDERGLMEEICADME-LNQVLEREA--RQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:PRK11288 95 tVAENlyLGQLPHKggiVNRRLLNYEAREQLEhLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180 190
....*....|....*....|....*....|....
gi 15231301 251 QRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSD 284
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRVILYVSHRMEEIFALCD 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
347-566 |
3.50e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 54.41 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 347 YARYKyPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG-----------VQSEIPEFNVSY 415
Cdd:cd03252 7 RFRYK-PDGPVILDNISLRIKPGE-----VVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlalADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 416 KPQGN-----------DSKRECTVRQLLHDKIRDACAHpQFMSDVirPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPA 484
Cdd:cd03252 81 VLQENvlfnrsirdniALADPGMSMERVIEAAKLAGAH-DFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 485 DIYLIDEPSAHLDSEqritASKVIKRFI--LHAKKTAFIVEHDfIMATYLADRVIVYEGQPAVKCIAHspQSLLS--GMN 560
Cdd:cd03252 158 RILIFDEATSALDYE----SEHAIMRNMhdICAGRTVIIIAHR-LSTVKNADRIIVMEKGRIVEQGSH--DELLAenGLY 230
|
....*.
gi 15231301 561 HFLSHL 566
Cdd:cd03252 231 AYLYQL 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
81-289 |
3.65e-08 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 54.34 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGANGFKLHRLPIPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLG--RFNTPPdweeiLTHFRGSEL----- 152
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISaGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtiRVNGQD-----VSDLRGRAIpylrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 153 ------QSYFI---RVVEENLktAIKPQHVDYIKEVVRGNLGKMLEKLDERGLMEEIcadmelnqvlereARQVSGGELQ 223
Cdd:cd03292 79 kigvvfQDFRLlpdRNVYENV--AFALEVTGVPPREIRKRVPAALELVGLSHKHRAL-------------PAELSGGEQQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 224 RFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
359-529 |
3.88e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGeftdsQIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFNVSYKPQGN--DSKRECTVRQ--LLHD 434
Cdd:PRK09544 20 LSDVSLELKPG-----KILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLylDTTLPLTVNRflRLRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 435 KIRDACAHPqfmsdVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILH 514
Cdd:PRK09544 95 GTKKEDILP-----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170
....*....|....*..
gi 15231301 515 AKKTAFIVEHD--FIMA 529
Cdd:PRK09544 170 LDCAVLMVSHDlhLVMA 186
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
354-540 |
3.92e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 55.54 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAG---------------AF----PREEGV---- 404
Cdd:COG1118 7 NISKRFGSFTllddvsLEIASGE-----LVALLGPSGSGKTTLLRIIAGletpdsgrivlngrdLFtnlpPRERRVgfvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 405 QS----------EipefNVSY----KPQGNDSKREcTVRQLLhdkirdacahpqfmsdviRPLQIEQLMDQVVKTLSGGE 470
Cdd:COG1118 82 QHyalfphmtvaE----NIAFglrvRPPSKAEIRA-RVEELL------------------ELVQLEGLADRYPSQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 471 KQRVAItlclgkpA-------DIYLIDEPSAHLDS----EQRITASKVIKRFilhaKKTAFIVEHDFIMATYLADRVIVY 539
Cdd:COG1118 139 RQRVAL-------AralavepEVLLLDEPFGALDAkvrkELRRWLRRLHDEL----GGTTVFVTHDQEEALELADRVVVM 207
|
.
gi 15231301 540 E 540
Cdd:COG1118 208 N 208
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
14-74 |
3.95e-08 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 55.80 E-value: 3.95e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 14 DRCKPKKCRQeCKKSCPVVKtgklcieVGSTSKSAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG4624 89 DKEKCKNCYP-CVRACPVKA-------IKVDDGKAEIDEEKCISCGQCVAVCPFGAITEKS 141
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
103-339 |
4.05e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAG-------KLKPNLGRFN-TPPDWEEIlthfrGSELQSYFIR---VVEENLKTAIKPQ 171
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGleditsgDLFIGEKRMNdVPPAERGV-----GMVFQSYALYphlSVAENMSFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HVDYikevvrgnlgkmlEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD--- 248
Cdd:PRK11000 104 GAKK-------------EEINQR--VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaal 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 249 -VRQRLKAAQVIRSLLRhdsYVIVVEHDLSVLDYLSDFVCCLYGkpGAYGVVTLPFSVRE-GINVFLAGFIPTENLRFrd 326
Cdd:PRK11000 169 rVQMRIEISRLHKRLGR---TMIYVTHDQVEAMTLADKIVVLDA--GRVAQVGKPLELYHyPANRFVAGFIGSPKMNF-- 241
|
250
....*....|...
gi 15231301 327 esLTFRVSETTQE 339
Cdd:PRK11000 242 --LPVKVTATAIE 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
354-542 |
4.20e-08 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 54.22 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGV---------------QSEIP-EF 411
Cdd:COG1127 10 NLTKSFGDRVvldgvsLDVPRGE-----ILAIIGGSGSGKSVLLKLIIGLLRPDSGEilvdgqditglsekeLYELRrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 412 NVSYkpQGN---DSKrecTVRQ-----------LLHDKIRDAcahpqfmsdVIRPLQ------IEQLM-DQvvktLSGGE 470
Cdd:COG1127 85 GMLF--QGGalfDSL---TVFEnvafplrehtdLSEAEIREL---------VLEKLElvglpgAADKMpSE----LSGGM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 471 KQRVAI--TLCLgKPaDIYLIDEPSAHLDseqRITaSKVIKRFILHAKK----TAFIVEHDFIMATYLADRVIV-YEGQ 542
Cdd:COG1127 147 RKRVALarALAL-DP-EILLYDEPTAGLD---PIT-SAVIDELIRELRDelglTSVVVTHDLDSAFAIADRVAVlADGK 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
101-292 |
4.21e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 55.12 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FntppDWEEIlTHFRGSELQSYF--IRVVEENLKTAIKPQHV--D 174
Cdd:COG4608 42 RRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEilF----DGQDI-TGLSGRELRPLRrrMQMVFQDPYASLNPRMTvgD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 YIKEVVRGNlgkmlEKLDERGLMEEICADME---LN-QVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:COG4608 117 IIAEPLRIH-----GLASKAERRERVAELLElvgLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231301 251 QRlkaAQVIRSL--LRHD---SYVIvVEHDLSVLDYLSDFVCCLY-GK 292
Cdd:COG4608 192 IQ---AQVLNLLedLQDElglTYLF-ISHDLSVVRHISDRVAVMYlGK 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
359-538 |
4.25e-08 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 53.76 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIPEFNVSYKPQGNDSKR------------EC 426
Cdd:cd03268 16 LDDISLHVKKGE-----IYGFLGPNGAGKTTTMKIILGLIKPDSG---EITFDGKSYQKNIEALRRigalieapgfypNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 TVRQ--LLHDKIRDacahpqfmsdvIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLC-LGKPaDIYLIDEPSA 494
Cdd:cd03268 88 TAREnlRLLARLLG-----------IRKKRIDEVLDVVglkdsakkkVKGFSLGMKQRLGIALAlLGNP-DLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 495 HLDSEqritASKVIKRFIL-HAK--KTAFIVEHdfIMA--TYLADRVIV 538
Cdd:cd03268 156 GLDPD----GIKELRELILsLRDqgITVLISSH--LLSeiQKVADRIGI 198
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
101-291 |
4.42e-08 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 55.06 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG-----RFN-------TPPDWEEIlthfRGSELQSYF----------IR 158
Cdd:COG0444 29 RRGETLGLVGESGSGKSTLARAILGLLPPPGItsgeiLFDgedllklSEKELRKI----RGREIQMIFqdpmtslnpvMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 159 V---VEENLKTaikpqHVDYIKEVVRGNLGKMLEKlderglmeeicadMELNQVLEREAR---QVSGGELQRFAIAAVFV 232
Cdd:COG0444 105 VgdqIAEPLRI-----HGGLSKAEARERAIELLER-------------VGLPDPERRLDRyphELSGGMRQRVMIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 233 KKADIYMFDEPSSYLDVR-QrlkaAQVIRsLLR-----HDSYVIVVEHDLSVLDYLSDFVCCLYG 291
Cdd:COG0444 167 LEPKLLIADEPTTALDVTiQ----AQILN-LLKdlqreLGLAILFITHDLGVVAEIADRVAVMYA 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
73-278 |
4.85e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 55.90 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 73 INLPKDL-AKDTTHRYGANGFKLH--RLPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdwEEILTHFRG 149
Cdd:TIGR01193 468 NNLNGDIvINDVSYSYGYGSNILSdiSLTIKM-NSKTTIVGMSGSGKSTLAKLLVGFFQARSG--------EILLNGFSL 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 150 SELQSYFIRvveenlktaikpQHVDYIKE-------------VVRGNLGKMLEKLDERGLMEEICADME-----LNQVLE 211
Cdd:TIGR01193 539 KDIDRHTLR------------QFINYLPQepyifsgsilenlLLGAKENVSQDEIWAACEIAEIKDDIEnmplgYQTELS 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 212 REARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVrqrLKAAQVIRSLLR-HDSYVIVVEHDLSV 278
Cdd:TIGR01193 607 EEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT---ITEKKIVNNLLNlQDKTIIFVAHRLSV 671
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
101-294 |
4.99e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 54.33 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYFIRV--------------VEENLKT 166
Cdd:COG1116 35 AAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG---------EVL--VDGKPVTGPGPDRgvvfqepallpwltVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 167 AIKPQHV--DYIKEVVRgnlgKMLEKlderglmeeicadMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:COG1116 104 GLELRGVpkAERRERAR----ELLEL-------------VGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 245 SYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDLS--VldYLSDFVCCLYGKPG 294
Cdd:COG1116 167 GALDALTRERLQDELLRLWQeTGKTVLFVTHDVDeaV--FLADRVVVLSARPG 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
103-278 |
5.37e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKIL-------AGKLKPNLGRFN--TPPDWEEILTHFR--GSELQSYFI---RVVEENLKTAi 168
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDfsKTPSDKAIRELRRnvGMVFQQYNLwphLTVQQNLIEA- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 169 kPQHVdyikevvrgnLGkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:PRK11124 107 -PCRV----------LG--LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190
....*....|....*....|....*....|
gi 15231301 249 VRQRLKAAQVIRSLLRHDSYVIVVEHDLSV 278
Cdd:PRK11124 174 PEITAQIVSIIRELAETGITQVIVTHEVEV 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
344-542 |
5.38e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 54.09 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 344 VKSYARykypnmTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGV----QSEIPEFNV------ 413
Cdd:cd03218 7 SKRYGK------RKVVNGVSLSVKQGE-----IVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldGQDITKLPMhkrarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 414 --SYKPQGNDSKRECTVRQ---------LLHDKIRDacahpQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGK 482
Cdd:cd03218 76 giGYLPQEASIFRKLTVEEnilavleirGLSKKERE-----EKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 483 PADIYLIDEPSAHLDSeqriTASKVIKRFILHAKKTA---FIVEHDFIMATYLADRV-IVYEGQ 542
Cdd:cd03218 151 NPKFLLLDEPFAGVDP----IAVQDIQKIIKILKDRGigvLITDHNVRETLSITDRAyIIYEGK 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
350-538 |
5.80e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.52 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGV------------QSEIPEF--NVSY 415
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEF-----VFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkRREIPYLrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 416 KPQgnDSKrectvrqLLHDK-------------------IRDAcahpqfMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAI 476
Cdd:COG2884 84 VFQ--DFR-------LLPDRtvyenvalplrvtgksrkeIRRR------VREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 477 T--LcLGKPaDIYLIDEPSAHLDSEqriTASKVIKRFI-LHAKKTAfivehdFIMATYlaDRVIV 538
Cdd:COG2884 149 AraL-VNRP-ELLLADEPTGNLDPE---TSWEIMELLEeINRRGTT------VLIATH--DLELV 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
81-277 |
5.82e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 53.94 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGANGFkLHR--LPIpRPGQVLGLVGTNGIGKSTALK-------ILAGKLKPNLGRFNTPPDWEEILTHFRGSE 151
Cdd:PRK09493 5 KNVSKHFGPTQV-LHNidLNI-DQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKVNDPKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 152 LQSYFI---RVVEENLktAIKPQHVdyikevvRGnlgkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIA 228
Cdd:PRK09493 83 FQQFYLfphLTALENV--MFGPLRV-------RG-----ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 229 AVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLS 277
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
13-72 |
6.34e-08 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 49.74 E-value: 6.34e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 13 EDRCKpkKCRQeCKKSCPVvktgkLCIEVGST--SKSAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1143 1 EDKCI--GCGL-CVRVCPV-----DAITIEDGepGKVYVIDPDKCIGCGLCVEVCPTGAISM 54
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
332-538 |
6.79e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 55.52 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 332 RVSETTQENDGEVKSYARYKYPNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEF 411
Cdd:TIGR01193 463 KRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNS-----KTTIVGMSGSGKSTLAKLLVGFFQARSG-EILLNGF 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 412 NVS------------YKPQ---------------GNDSKREctvrqllHDKIRDACAHPQFMSDVIR-PLQIEQLMDQVV 463
Cdd:TIGR01193 537 SLKdidrhtlrqfinYLPQepyifsgsilenlllGAKENVS-------QDEIWAACEIAEIKDDIENmPLGYQTELSEEG 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 464 KTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqrITASKVIKRFILHAKKTAFIVEHDFIMATyLADRVIV 538
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAK-QSDKIIV 680
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
354-499 |
7.49e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.86 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFnvsykpqGNDSKRECTV-RQLL 432
Cdd:PRK09984 15 NQHQALHAVDLNIHHGE-----MVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELL-------GRTVQREGRLaRDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 433 HDKIRDACAHPQF--------MSDVI-----------------------RPLQ------IEQLMDQVVKTLSGGEKQRVA 475
Cdd:PRK09984 83 KSRANTGYIFQQFnlvnrlsvLENVLigalgstpfwrtcfswftreqkqRALQaltrvgMVHFAHQRVSTLSGGQQQRVA 162
|
170 180
....*....|....*....|....
gi 15231301 476 ITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPE 186
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
18-86 |
7.68e-08 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 51.24 E-value: 7.68e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 18 PKKCRQ--ECKKSCPvvkTGklCIEV---GSTSKSAFISEELCIGCGICVKKCPFEAIQIINLPKDLAKDTTHR 86
Cdd:cd10549 5 PEKCIGcgICVKACP---TD--AIELgpnGAIARGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEA 73
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
362-524 |
7.87e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 362 FKLEvmegeftDSQIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEipEFNVSYKPQGN----DSKRECTVRQLLHDKIR 437
Cdd:TIGR01271 447 FKLE-------KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH--SGRISFSPQTSwimpGTIKDNIIFGLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 438 dacahpqfMSDVIRPLQIEQ------------LMDQVVkTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD--SEQRIT 503
Cdd:TIGR01271 518 --------YTSVIKACQLEEdialfpekdktvLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKEIF 588
|
170 180
....*....|....*....|....*
gi 15231301 504 ASKVIKrfiLHAKKTAFIV----EH 524
Cdd:TIGR01271 589 ESCLCK---LMSNKTRILVtsklEH 610
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
375-502 |
8.62e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.24 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 375 QIIVMLGENGTGKTTFIRMLAGAFPRE-----EGVqsEIPEFNVSYKPQ-----GNDSkrectvrQLLHDKIRD--ACAH 442
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFLPYQgslkiNGI--ELRELDPESWRKhlswvGQNP-------QLPHGTLRDnvLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 443 PQfMSDVirplQIEQLMDQ----------------VVK----TLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD--SEQ 500
Cdd:PRK11174 448 PD-ASDE----QLQQALENawvseflpllpqgldtPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDahSEQ 522
|
..
gi 15231301 501 RI 502
Cdd:PRK11174 523 LV 524
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
343-570 |
8.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.97 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 343 EVKSyARYKY-PNMTK-QLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEG----VQSEIPEFNVSYK 416
Cdd:PRK13650 6 EVKN-LTFKYkEDQEKyTLNDVSFHVKQGEW-----LSIIGHNGSGKSTTVRLIDGLLEAESGqiiiDGDLLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 417 PQGNDSKRECTVRQLLHDKIRDACA---------HPQFMSDVIRPLQIEQLMDqvVKT-----LSGGEKQRVAITLCLGK 482
Cdd:PRK13650 80 RHKIGMVFQNPDNQFVGATVEDDVAfglenkgipHEEMKERVNEALELVGMQD--FKEreparLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 483 PADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATyLADRVIVY-EGQpaVKCIAhSPQSLLSGMNH 561
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMkNGQ--VESTS-TPRELFSRGND 233
|
250
....*....|
gi 15231301 562 FLS-HLNITF 570
Cdd:PRK13650 234 LLQlGLDIPF 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
350-541 |
9.82e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-----LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIR-MLAGAFPREEGVQSEipefnvsykpqGNDSK 423
Cdd:PRK13633 12 YKYESNEESteklaLDDVNLEVKKGEF-----LVILGRNGSGKSTIAKhMNALLIPSEGKVYVD-----------GLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 424 RECTVRqllhdKIRDACA----HP--QFMS-----DV--------IRPLQIEQLMDQVVKT-------------LSGGEK 471
Cdd:PRK13633 76 DEENLW-----DIRNKAGmvfqNPdnQIVAtiveeDVafgpenlgIPPEEIRERVDESLKKvgmyeyrrhaphlLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 472 QRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHdFIMATYLADRVIVYEG 541
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH-YMEEAVEADRIIVMDS 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-537 |
1.09e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.22 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQ------LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLaGAFPREEGVQSEIPEFNVsykpqgnDSKRECT 427
Cdd:PRK11264 8 NLVKKfhgqtvLHGIDLEVKPGE-----VVAIIGPSGSGKTTLLRCI-NLLEQPEAGTIRVGDITI-------DTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQLLHDKIRDACA----------HPQFMSDVIR-PLQIE------------QLMDQV---------VKTLSGGEKQRVA 475
Cdd:PRK11264 75 QQKGLIRQLRQHVGfvfqnfnlfpHRTVLENIIEgPVIVKgepkeeatararELLAKVglagketsyPRRLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 476 ITLCLGKPADIYLIDEPSAHLDSEQRITASKVIkRFILHAKKTAFIVEHDFIMATYLADRVI 537
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTI-RQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
4-73 |
1.31e-07 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 50.65 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 4 RLTRIAIVS---EDRCKPKKCRQ----ECKKSCPV------VKTGKLCIevgstsksafiSEELCIGCGICVKKCPFEAI 70
Cdd:cd10550 29 SLSRIRVVRfepEGLDVPVVCRQcedaPCVEACPVgaisrdEETGAVVV-----------DEDKCIGCGMCVEACPFGAI 97
|
...
gi 15231301 71 QII 73
Cdd:cd10550 98 RVD 100
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
101-262 |
1.33e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 52.26 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG-----RFNTPPdWEEILTHFRGSelqsyFIRVVEENLktaikpqHVDY 175
Cdd:cd03233 31 KPGEMVLVLGRPGSGCSTLLKALANRTEGNVSvegdiHYNGIP-YKEFAEKYPGE-----IIYVSEEDV-------HFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IkeVVRGNLgkmleklderglmeEICADMELNQVLereaRQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKA 255
Cdd:cd03233 98 L--TVRETL--------------DFALRCKGNEFV----RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
....*..
gi 15231301 256 AQVIRSL 262
Cdd:cd03233 158 LKCIRTM 164
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
353-565 |
1.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.58 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 353 PNMTKQLGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGVQ--SEIPEFNVSYKPQGNDSKRECTV-- 428
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYT-----ALIGHTGSGKSTLLQHLNGLLQPTEGKVtvGDIVVSSTSKQKEIKPVRKKVGVvf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 ----RQLLHDKI-RDACAHPQFM------SDVIRPLQIE------QLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDE 491
Cdd:PRK13643 91 qfpeSQLFEETVlKDVAFGPQNFgipkekAEKIAAEKLEmvgladEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 492 PSAHLDSEQRITASKVIKRfILHAKKTAFIVEHDFIMATYLADRVIVYEGQPAVKCiaHSPQSLLSGMNHFLSH 565
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISC--GTPSDVFQEVDFLKAH 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
353-538 |
1.72e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.13 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 353 PNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKP-QGNDSKRECTV--- 428
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEF-----VGLIGHTGSGKSTLIQHLNGLLKPTSG-KIIIDGVDITDKKvKLSDIRKKVGLvfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 ---RQLLHDKI-RDACAHPQFM--SD------VIRPLQI-----EQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDE 491
Cdd:PRK13637 91 ypeYQLFEETIeKDIAFGPINLglSEeeienrVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 492 PSAHLDSEQRITASKVIKRfiLHAKK--TAFIVEHDFIMATYLADRVIV 538
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKE--LHKEYnmTIILVSHSMEDVAKLADRIIV 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
101-538 |
1.80e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweEI----LTHFRGSELQSYFIRVVeenlktaikPQ--HVd 174
Cdd:PRK15439 35 HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-------EIggnpCARLTPAKAHQLGIYLV---------PQepLL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 YIKEVVRGN-LGKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRL 253
Cdd:PRK15439 98 FPNLSVKENiLFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 254 KAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVcclygkpgaygvvtlpfSV-REGInVFLAGfiPTENlrFRDESLTFR 332
Cdd:PRK15439 178 RLFSRIRELLAQGVGIVFISHKLPEIRQLADRI-----------------SVmRDGT-IALSG--KTAD--LSTDDIIQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 333 VSETTQENDGEVKSYARYKYPN--MTKQLG---------------DFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLA 395
Cdd:PRK15439 236 ITPAAREKSLSASQKLWLELPGnrRQQAAGapvltvedltgegfrNISLEVRAGE-----ILGLAGVVGAGRTELAETLY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 396 GAFPREEGV----QSEI----------------PE--------------FNVSYKPQGN-----DSKRECTVRQLLHDKI 436
Cdd:PRK15439 311 GLRPARGGRimlnGKEInalstaqrlarglvylPEdrqssglyldaplaWNVCALTHNRrgfwiKPARENAVLERYRRAL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 437 RDACAHPqfmsdvirplqieqlmDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfiLHAK 516
Cdd:PRK15439 391 NIKFNHA----------------EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS--IAAQ 452
|
490 500
....*....|....*....|...
gi 15231301 517 KTAFI-VEHDFIMATYLADRVIV 538
Cdd:PRK15439 453 NVAVLfISSDLEEIEQMADRVLV 475
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-542 |
1.81e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDfkLEVMEG---EFTDSQIIVMLGENGTGKTTFIRMLAGAF-----PREEG---------------------- 403
Cdd:PRK14247 8 DLKVSFGQ--VEVLDGvnlEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGevyldgqdifkmdvielrrrvq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 404 ----VQSEIPEF----NVSYKPQGN---DSKREctvrqlLHDKIRDACAHPQFMSDVirplqiEQLMDQVVKTLSGGEKQ 472
Cdd:PRK14247 86 mvfqIPNPIPNLsifeNVALGLKLNrlvKSKKE------LQERVRWALEKAQLWDEV------KDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 473 RVAITLCLGKPADIYLIDEPSAHLDSEQriTASkvIKRFILHAKK--TAFIVEHDFIMATYLADRV-IVYEGQ 542
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPEN--TAK--IESLFLELKKdmTIVLVTHFPQQAARISDYVaFLYKGQ 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
81-286 |
1.91e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRY--GANGFKLHRLPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF---NTPPDWE-EILTHFR---GSE 151
Cdd:PRK13636 9 EELNYNYsdGTHALKGININIKK-GEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdGKPIDYSrKGLMKLResvGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 152 LQSyfirvVEENLKTAIKPQHVDYikevvrGNLGKMLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVF 231
Cdd:PRK13636 88 FQD-----PDNQLFSASVYQDVSF------GAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 232 VKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRH-DSYVIVVEHDLSVLDYLSDFV 286
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNV 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
379-541 |
2.08e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 379 MLGENGTGKTTFIRMLAGAFPREEGVQS----EIPE------FNVSYKPQGNDSKRECTVRQLLHDKIRDACAHPQFMSD 448
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISlcgePVPSrarharQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 449 VIRPL----QIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIkRFILHAKKTAFIVEH 524
Cdd:PRK13537 118 LVPPLlefaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERL-RSLLARGKTILLTTH 196
|
170
....*....|....*..
gi 15231301 525 DFIMATYLADRVIVYEG 541
Cdd:PRK13537 197 FMEEAERLCDRLCVIEE 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
359-522 |
2.10e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.94 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGVQSEipEFNVSYKPQGN----DSKRECTVRQLLHD 434
Cdd:cd03291 53 LKNINLKIEKGE-----MLAITGSTGSGKTSLLMLILGELEPSEGKIKH--SGRISFSSQFSwimpGTIKENIIFGVSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 435 KIR-----DACahpQFMSDVIR-PLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD--SEQRITASK 506
Cdd:cd03291 126 EYRyksvvKAC---QLEEDITKfPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfTEKEIFESC 202
|
170
....*....|....*.
gi 15231301 507 VIKrfiLHAKKTAFIV 522
Cdd:cd03291 203 VCK---LMANKTRILV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-543 |
2.10e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 53.65 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK-LEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAG--AFPREEG------------VQSEIPEF------- 411
Cdd:TIGR03269 5 NLTKKFDGKEvLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyhvalcekcGYVERPSKvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 412 -------------NVSYKPQGNDSKRECTVRQ-----------------LLHDKIRDACAHPQFMSDVIRPLQIEQLMDQ 461
Cdd:TIGR03269 85 cggtlepeevdfwNLSDKLRRRIRKRIAIMLQrtfalygddtvldnvleALEEIGYEGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 462 VVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEH------DFI-MATYLAD 534
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLSdKAIWLEN 244
|
....*....
gi 15231301 535 RVIVYEGQP 543
Cdd:TIGR03269 245 GEIKEEGTP 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
81-277 |
2.12e-07 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 52.23 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGANGFKLHR---LPIPRpGQVLGLVGTNGIGKSTALKILAgklkpnlgRFnTPPDWEEILthFRGSELQSYFI 157
Cdd:cd03251 4 KNVTFRYPGDGPPVLRdisLDIPA-GETVALVGPSGSGKSTLVNLIP--------RF-YDVDSGRIL--IDGHDVRDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 158 RVVEENLktAIKPQHV----DYIKEVVR-GNLGKMLEKLDER----GLMEEICaDME--LNQVLEREARQVSGGELQRFA 226
Cdd:cd03251 72 ASLRRQI--GLVSQDVflfnDTVAENIAyGRPGATREEVEEAaraaNAHEFIM-ELPegYDTVIGERGVKLSGGQRQRIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15231301 227 IAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRhDSYVIVVEHDLS 277
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLS 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
81-304 |
2.14e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.88 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGANGFKLHRLPIPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNTPPDWEEILTHFRGselqsyFI 157
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPrNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlIRGEPITKENIREVRK------FV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 158 RVVEENLKTAIKPQHVDyiKEVVRG--NLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKA 235
Cdd:PRK13652 81 GLVFQNPDDQIFSPTVE--QDIAFGpiNLGLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 236 DIYMFDEPSSYLDVRQRLKAAQVIRSL-LRHDSYVIVVEHDLSVLDYLSDFVCCL-YGKPGAYGVVTLPFS 304
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMdKGRIVAYGTVEEIFL 227
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
216-276 |
2.24e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 2.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 216 QVSGGELQRFAIAAVF----VKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
46-74 |
2.30e-07 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 48.19 E-value: 2.30e-07
10 20
....*....|....*....|....*....
gi 15231301 46 KSAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG1149 4 KIPVIDEEKCIGCGLCVEVCPEGAIKLDD 32
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
99-279 |
2.41e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 51.70 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 99 IPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPD--------WeeilthfrgseLQSYFIRvveENlktaI-- 168
Cdd:cd03250 28 VPK-GELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepW-----------IQNGTIR---EN----Ilf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 169 -KPQHVDYIKEVVRG-NLGKMLEKLDErGLMEEIcADMELNqvlerearqVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:cd03250 89 gKPFDEERYEKVIKAcALEPDLEILPD-GDLTEI-GEKGIN---------LSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190
....*....|....*....|....*....|....*
gi 15231301 247 LD--VRQRLkAAQVIRSLLRHDSYVIVVEHDLSVL 279
Cdd:cd03250 158 VDahVGRHI-FENCILGLLLNNKTRILVTHQLQLL 191
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
361-542 |
2.57e-07 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 52.26 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 361 DFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSykpQGNDS-------KRECTVRQ--- 430
Cdd:cd03294 42 DVSLDVREGE-----IFVIMGLSGSGKSTLLRCINRLIEPTSG-KVLIDGQDIA---AMSRKelrelrrKKISMVFQsfa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 431 -LLHDKIRDACAHP---QFMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD 497
Cdd:cd03294 113 lLPHRTVLENVAFGlevQGVPRAEREERAAEALELVglegwehkyPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231301 498 SEQRITASKVIKRfiLHAK--KTAFIVEHDFIMATYLADRV-IVYEGQ 542
Cdd:cd03294 193 PLIRREMQDELLR--LQAElqKTIVFITHDLDEALRLGDRIaIMKDGR 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
101-286 |
2.70e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.53 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKST-ALKILagKLKPNLG--RFNTPPdweeiLTHFRGSELQSY-------F------------I- 157
Cdd:COG4172 310 RRGETLGLVGESGSGKSTlGLALL--RLIPSEGeiRFDGQD-----LDGLSRRALRPLrrrmqvvFqdpfgslsprmtVg 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 158 RVVEENLktaikpqHVDYIKEVVRGNLGKMLEKLDERGLMEEicadmelnqVLEREARQVSGGELQRFAIAAVFVKKADI 237
Cdd:COG4172 383 QIIAEGL-------RVHGPGLSAAERRARVAEALEEVGLDPA---------ARHRYPHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 238 YMFDEPSSYLDVRQRlkaAQVIrSLLR-----HD-SYvIVVEHDLSVLDYLSDFV 286
Cdd:COG4172 447 LVLDEPTSALDVSVQ---AQIL-DLLRdlqreHGlAY-LFISHDLAVVRALAHRV 496
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
77-286 |
2.77e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 77 KDLAKdtTHRYGANGFKLHRL----PIP---RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILT---- 145
Cdd:PRK15112 8 RNLSK--TFRYRTGWFRRQTVeavkPLSftlREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG---------ELLIddhp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 146 -HFRGSELQSYFIRVVEENLKTAIKPqhvdyikevvRGNLGKMLEklderglmeeicADMELNQVLEREARQ-------- 216
Cdd:PRK15112 77 lHFGDYSYRSQRIRMIFQDPSTSLNP----------RQRISQILD------------FPLRLNTDLEPEQREkqiietlr 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 217 ---------------VSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRlkaAQVIRSLL----RHD-SYVIVVEHdL 276
Cdd:PRK15112 135 qvgllpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR---SQLINLMLelqeKQGiSYIYVTQH-L 210
|
250
....*....|
gi 15231301 277 SVLDYLSDFV 286
Cdd:PRK15112 211 GMMKHISDQV 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
86-287 |
3.03e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.50 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 86 RYGA----NGFKLHrlpiPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPdwEEILTHFRGSELQsyfIRVVE 161
Cdd:PRK13537 16 RYGDklvvDGLSFH----VQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG--EPVPSRARHARQR---VGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 162 E--NLKTaikpqhvDYikeVVRGNL---GKM--LEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKK 234
Cdd:PRK13537 87 QfdNLDP-------DF---TVRENLlvfGRYfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 235 ADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVC 287
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLC 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
104-284 |
3.09e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 104 QVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILTHFRGSELQsyfIRVVEENLktAIKPQHVDYIKEVVRGN 183
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSG---------TVLVGGKDIETN---LDAVRQSL--GMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 184 LGKMLEKL-----DERGL-MEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRlkaaQ 257
Cdd:TIGR01257 1023 HILFYAQLkgrswEEAQLeMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR----R 1098
|
170 180 190
....*....|....*....|....*....|
gi 15231301 258 VIRSLL---RHDSYVIVVEHDLSVLDYLSD 284
Cdd:TIGR01257 1099 SIWDLLlkyRSGRTIIMSTHHMDEADLLGD 1128
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
101-290 |
3.31e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.99 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKlkpnlgrfntpPDWEEIlthfRGSelqsyfIRVVEENLkTAIKPqhvdyikevv 180
Cdd:cd03217 24 KKGEVHALMGPNGSGKSTLAKTIMGH-----------PKYEVT----EGE------ILFKGEDI-TDLPP---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 rgnlgkmleklDERGLM---------EEIcADMELNQVLereaRQV----SGGELQRFAIAAVFVKKADIYMFDEPSSYL 247
Cdd:cd03217 72 -----------EERARLgiflafqypPEI-PGVKNADFL----RYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 248 DVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYL-SDFVCCLY 290
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLY 179
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
359-543 |
3.59e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 51.79 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKP-QGNDSKREcTVRQllHD--- 434
Cdd:COG4525 23 LQDVSLTIESGEFV-----VALGASGCGKTTLLNLIAGFLAPSSG------EITLDGVPvTGPGADRG-VVFQ--KDall 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 435 ---KIRDACAHP---QFMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:COG4525 89 pwlNVLDNVAFGlrlRGVPKAERRARAEELLALVgladfarrrIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 500 QRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQP 543
Cdd:COG4525 169 TREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP 212
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
106-275 |
3.67e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 106 LGLVGTNGIGKSTALKILAGKLKPNLGR-FNTPPDWEEILT--HFRGSELQS----YFIR----VVEENLKTAIkpqhvd 174
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTvFRSAKVRMAVFSqhHVDGLDLSSnpllYMMRcfpgVPEQKLRAHL------ 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 yikevvrGNLGkmleklderglmeeICADMELNQVLerearQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDvrqrLK 254
Cdd:PLN03073 612 -------GSFG--------------VTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LD 661
|
170 180
....*....|....*....|..
gi 15231301 255 AAQ-VIRSLLRHDSYVIVVEHD 275
Cdd:PLN03073 662 AVEaLIQGLVLFQGGVLMVSHD 683
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
354-537 |
3.98e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 51.13 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLG------DFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGV-------QSEIPEFNVSYKPQGN 420
Cdd:cd03269 5 NVTKRFGrvtaldDISFSVEKGE-----IFGLLGPNGAGKTTTIRMILGIILPDSGEvlfdgkpLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 421 DSKRECTVR-QLLH------DKIRDACAHpqfMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPS 493
Cdd:cd03269 80 GLYPKMKVIdQLVYlaqlkgLKKEEARRR---IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 494 AHLDSeqriTASKVIKRFILHAK---KTAFIVEHDFIMATYLADRVI 537
Cdd:cd03269 157 SGLDP----VNVELLKDVIRELAragKTVILSTHQMELVEELCDRVL 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
346-543 |
4.45e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 346 SYARykypNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKPQGNdSKRE 425
Cdd:PRK13543 18 AFSR----NEEPVFGPLDFHVDAGE-----ALLVQGDNGAGKTTLLRVLAGLLHVESG------QIQIDGKTATR-GDRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 CTVRQLLH-----------DKIRDACA----HPQFM-SDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLI 489
Cdd:PRK13543 82 RFMAYLGHlpglkadlstlENLHFLCGlhgrRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 490 DEPSAHLDSEQrITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQP 543
Cdd:PRK13543 162 DEPYANLDLEG-ITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
17-81 |
4.90e-07 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 49.31 E-value: 4.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 17 KPKKCRQ----ECKKSCPV-----VKTGKlcievgstsksAFISEELCIGCGICVKKCPFEAIQIINLPKDLAK 81
Cdd:cd04410 46 LPVSCMHcedpPCVKACPTgaiykDEDGI-----------VLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVK 108
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
369-509 |
5.25e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 50.24 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 369 GEFTDSQIIVMLGENGTGKTTFIRMLAGAFPREeGVQSEIpefNVSYKPQGNDSKRECT--VRQllHDKIrdacaHPQFm 446
Cdd:cd03213 30 GKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL-GVSGEV---LINGRPLDKRSFRKIIgyVPQ--DDIL-----HPTL- 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 447 sdVIRplqiEQLMDQV-VKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqrITASKVIK 509
Cdd:cd03213 98 --TVR----ETLMFAAkLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS---SSALQVMS 152
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
466-538 |
5.49e-07 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 5.49e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDS--EQRITASkvIKRfiLHAKKTAFIVEHDF--IMAtylADRVIV 538
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDThtEREIQAA--LRD--VSKGRTTIVIAHRLstIVN---ADKIIV 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
92-277 |
5.62e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.80 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 92 FKLHrlpiprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTppDWEEIlthfrgSELQSYFIRVveenlKTAIKPQ 171
Cdd:TIGR00958 502 FTLH------PGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL--DGVPL------VQYDHHYLHR-----QVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HVDYIKEVVRGNLGKMLEKLDERGLM---EEICAD---MELNQVLERE----ARQVSGGELQRFAIAAVFVKKADIYMFD 241
Cdd:TIGR00958 563 EPVLFSGSVRENIAYGLTDTPDEEIMaaaKAANAHdfiMEFPNGYDTEvgekGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 242 EPSSYLDVRQRlKAAQVIRSllRHDSYVIVVEHDLS 277
Cdd:TIGR00958 643 EATSALDAECE-QLLQESRS--RASRTVLLIAHRLS 675
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
101-289 |
5.91e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.27 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPdweeilthfrgselqsyfirvveeNLKTAIKPQ--HVD---- 174
Cdd:PRK09544 28 KPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------------------KLRIGYVPQklYLDttlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 -YIKEVVRgnLGKMLEKLDERGLMEEICADMELNQVLERearqVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRL 253
Cdd:PRK09544 84 lTVNRFLR--LRPGTKKEDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 15231301 254 KAAQVIRSLLRH-DSYVIVVEHDLSVLDYLSDFVCCL 289
Cdd:PRK09544 158 ALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
446-540 |
6.76e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.34 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 446 MSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHD 525
Cdd:PRK13652 118 VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQ 197
|
90
....*....|....*
gi 15231301 526 FIMATYLADRVIVYE 540
Cdd:PRK13652 198 LDLVPEMADYIYVMD 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
101-265 |
6.85e-07 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 50.62 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNtppdwEEILTH---FRGSEL--------QSYFIRV-VEENLKT 166
Cdd:cd03218 24 KQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilLD-----GQDITKlpmHKRARLgigylpqeASIFRKLtVEENILA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 167 AIKPQHVDYikevvrgnlGKMLEKLDErgLMEEicadMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:cd03218 99 VLEIRGLSK---------KEREEKLEE--LLEE----FHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170
....*....|....*....
gi 15231301 247 LDVrqrlKAAQVIRSLLRH 265
Cdd:cd03218 164 VDP----IAVQDIQKIIKI 178
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
350-540 |
7.84e-07 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 50.31 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPN-MTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQGNDSKRECTV 428
Cdd:cd03251 8 FRYPGdGPPVLRDISLDIPAGET-----VALVGPSGSGKSTLVNLIPRFYDVDSG-RILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQ---LLHDKIRDACAHPQF---MSDVIRPLQIEQLMDQVVK--------------TLSGGEKQRVAITLCLGKPADIYL 488
Cdd:cd03251 82 SQdvfLFNDTVAENIAYGRPgatREEVEEAARAANAHEFIMElpegydtvigergvKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 489 IDEPSAHLDSEQRITASKVIKRfiLHAKKTAFIVEHDF--IMAtylADRVIVYE 540
Cdd:cd03251 162 LDEATSALDTESERLVQAALER--LMKNRTTFVIAHRLstIEN---ADRIVVLE 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
359-537 |
8.07e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 50.51 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGafpreegvqseipefnvSYKPQG-----NDSKR-----ECTV 428
Cdd:COG4778 27 LDGVSFSVAAGEC-----VALTGPSGAGKSTLLKCIYG-----------------NYLPDSgsilvRHDGGwvdlaQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQLLHdkIRdacAH-----PQFMS--------D-VIRPLqIEQLMDQVV-----------------------KTLSGGEK 471
Cdd:COG4778 85 REILA--LR---RRtigyvSQFLRviprvsalDvVAEPL-LERGVDREEarararellarlnlperlwdlppATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 472 QRVAITLCLGKPADIYLIDEPSAHLDSEQRItaskVIKRFILHAKK--TAFI-VEHDF-IMATyLADRVI 537
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEAKArgTAIIgIFHDEeVREA-VADRVV 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
466-594 |
8.36e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEqritASKVIKRFILHAK---KTAFIVEHDFIMATYLADRVIVYEGQ 542
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK----GEHEMMQLILDAKannKTVFVITHTMEHVLEVADEVIVMDKG 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 543 PAVKciAHSPQSLLsgMN-HFLSHLNIT------FRRDPTNFRPRINKLesiKDKEQKT 594
Cdd:PRK13631 253 KILK--TGTPYEIF--TDqHIINSTSIQvprviqVINDLIKKDPKYKKL---YQKQPRT 304
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
376-541 |
8.64e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 376 IIVMLGENGTGKTTFIRMLAGAFPREEGVQSEipEFNVSYKPQG----NDSKRE-----CTVRQLLHDKIRDACAhpqFM 446
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--KGSVAYVPQQawiqNDSLREnilfgKALNEKYYQQVLEACA---LL 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 447 SDV-IRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE-QRITASKVIKRFILHAKKTAFIVEH 524
Cdd:TIGR00957 741 PDLeILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTH 820
|
170
....*....|....*....
gi 15231301 525 DFimaTYL--ADRVIVYEG 541
Cdd:TIGR00957 821 GI---SYLpqVDVIIVMSG 836
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
365-538 |
1.17e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 365 EVMEG---EFTDSQIIVMLGENGTGKTTFIRMLAGAFPREEGV---QSEipefNVSYKPQGNDSKRE--CTV-----RQL 431
Cdd:PRK13638 15 PVLKGlnlDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAvlwQGK----PLDYSKRGLLALRQqvATVfqdpeQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 432 LHDKIRDACAHP------------QFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:PRK13638 91 FYTDIDSDIAFSlrnlgvpeaeitRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 500 QRITASKVIKRFILHAKKTAfIVEHDFIMATYLADRVIV 538
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVI-ISSHDIDLIYEISDAVYV 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
101-350 |
1.33e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 50.49 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQsyfirvveenlktaikpqhvdyikEVV 180
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPDSG---------EVL--WDGEPLD------------------------PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNLGKMLEkldERGL------MEEIC------------ADMELNQVLER---------EARQVSGGELQRFAIAAVFVK 233
Cdd:COG4152 70 RRRIGYLPE---ERGLypkmkvGEQLVylarlkglskaeAKRRADEWLERlglgdrankKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 234 KADIYMFDEPSSYLDV--RQRLKaaQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLY-GKPGAYGVV--------TLP 302
Cdd:COG4152 147 DPELLILDEPFSGLDPvnVELLK--DVIRELAAKGTTVIFSSHQMELVEELCDRIVIINkGRKVLSGSVdeirrqfgRNT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 303 FSVR-EGINVFLAGFIPTENLRFRDESLTFRVSETTQEND--------GEVKSYARY 350
Cdd:COG4152 225 LRLEaDGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQEllrallarGPVREFEEV 281
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
101-286 |
1.35e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 50.07 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKlkpnlgrfntpPDWE----EILthFRGselqsyfirvveENLkTAIKP------ 170
Cdd:COG0396 24 KPGEVHAIMGPNGSGKSTLAKVLMGH-----------PKYEvtsgSIL--LDG------------EDI-LELSPderara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 171 ------QH---------VDYIKEVVRGNLGKMLEKLDERGLMEEICADMELNQ-VLEREarqV----SGGELQRFAIAAV 230
Cdd:COG0396 78 giflafQYpveipgvsvSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRY---VnegfSGGEKKRNEILQM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 231 FVKKADIYMFDEPSSYLDVrQRLKA-AQVIRSLLRHDSYVIVVEHDLSVLDYLS-DFV 286
Cdd:COG0396 155 LLLEPKLAILDETDSGLDI-DALRIvAEGVNKLRSPDRGILIITHYQRILDYIKpDFV 211
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
45-74 |
1.48e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 45.88 E-value: 1.48e-06
10 20 30
....*....|....*....|....*....|
gi 15231301 45 SKSAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG2768 3 LGKPYVDEEKCIGCGACVKVCPVGAISIED 32
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
364-538 |
1.54e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------------VQSE------IP-EFNVSykPQ---- 418
Cdd:COG1129 25 LELRPGE-----VHALLGENGAGKSTLMKILSGVYQPDSGeilldgepvrfrspRDAQaagiaiIHqELNLV--PNlsva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 -----GNDSKRECTVRqllHDKIRDACAhpQFMSDV---IRPlqieqlmDQVVKTLSGGEKQRVAITLCLGKPADIyLI- 489
Cdd:COG1129 98 eniflGREPRRGGLID---WRAMRRRAR--ELLARLgldIDP-------DTPVGDLSVAQQQLVEIARALSRDARV-LIl 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 490 DEPSAHLDSEQRITASKVIKRfiLHAKKTAFI-VEHDF--IMAtyLADRVIV 538
Cdd:COG1129 165 DEPTASLTEREVERLFRIIRR--LKAQGVAIIyISHRLdeVFE--IADRVTV 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
349-551 |
1.59e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.09 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGVqSEIPEFNVSYKPQGNDSKRECTV 428
Cdd:PRK13642 13 KYEKESDVNQLNGVSFSITKGEW-----VSIIGQNGSGKSTTARLIDGLFEEFEGK-VKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 -----RQLLHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKT------------LSGGEKQRVAITLCLGKPADIYLIDE 491
Cdd:PRK13642 87 fqnpdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVnmldfktreparLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 492 PSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYlADRVIVYEGQPAVKCIAHS 551
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPS 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
352-538 |
1.73e-06 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 49.53 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 352 YPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKPQGNDSKRECTVRQ- 430
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGET-----VAIVGPTGAGKTTLINLLMRFYDPQKG-QILIDGIDIRDISRKSLRSMIGVVLQd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 431 --LLHDKIRD--ACAHPQF-MSDVIRPLQIEQLMDQVVK--------------TLSGGEKQRVAITLCLGKPADIYLIDE 491
Cdd:cd03254 86 tfLFSGTIMEniRLGRPNAtDEEVIEAAKEAGAHDFIMKlpngydtvlgenggNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15231301 492 PSAHLDS--EQRITASkvIKRfiLHAKKTAFIVEHDfiMATYL-ADRVIV 538
Cdd:cd03254 166 ATSNIDTetEKLIQEA--LEK--LMKGRTSIIIAHR--LSTIKnADKILV 209
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
2-73 |
1.73e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 48.02 E-value: 1.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 2 SDRLTRI--AIVSEDRC----KPKKCRQeCKKSCPVVktGKLCIEVGSTSKsAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:cd16373 77 EEQKVKMgvAVIDKDRClawqGGTDCGV-CVEACPTE--AIAIVLEDDVLR-PVVDEDKCVGCGLCEYVCPVEPPKAI 150
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
101-277 |
1.78e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 49.46 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAgklkpnlgRFNTPPDWEEILTHFRGSELQSYFIR----VVE-----------ENLK 165
Cdd:cd03249 27 PPGKTVALVGSSGCGKSTVVSLLE--------RFYDPTSGEILLDGVDIRDLNLRWLRsqigLVSqepvlfdgtiaENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 166 TAIKPQHVDYIKEVVR-GNLGKMLEKLDERglmeeicadmeLNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:cd03249 99 YGKPDATDEEVEEAAKkANIHDFIMSLPDG-----------YDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 15231301 245 SYLD------VRQRLKAAQVIRSllrhdsyVIVVEHDLS 277
Cdd:cd03249 168 SALDaeseklVQEALDRAMKGRT-------TIVIAHRLS 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
354-538 |
1.79e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.60 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQ------LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvQSEIPEFNVSYKP---------- 417
Cdd:PRK11607 24 NLTKSfdgqhaVDDVSLTIYKGE-----IFALLGASGCGKSTLLRMLAGFEQPTAG-QIMLDGVDLSHVPpyqrpinmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 418 QGNDSKRECTVRQ-----LLHDKIRDACAHPQfMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEP 492
Cdd:PRK11607 98 QSYALFPHMTVEQniafgLKQDKLPKAEIASR-VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15231301 493 SAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAI 222
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
50-71 |
1.87e-06 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 44.55 E-value: 1.87e-06
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
352-535 |
1.87e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.39 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 352 YPNMTKQLGDFKLEvmegeFTDSQIIVMLGENGTGKTTFIRMLagafpreEGVQSEIPEFN----VSYKPQGNDSKRECT 427
Cdd:PRK14239 14 YYNKKKALNSVSLD-----FYPNEITALIGPSGSGKSTLLRSI-------NRMNDLNPEVTitgsIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRqlLHDKIRDACAHPQ-F-MS---DVIRPLQI-----EQLMDQVVKT---------------------LSGGEKQRVAI 476
Cdd:PRK14239 82 VD--LRKEIGMVFQQPNpFpMSiyeNVVYGLRLkgikdKQVLDEAVEKslkgasiwdevkdrlhdsalgLSGGQQQRVCI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 477 TLCLGKPADIYLIDEPSAHLDSeqrITASKVIKR-FILHAKKTAFIVEHDFIMATYLADR 535
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDP---ISAGKIEETlLGLKDDYTMLLVTRSMQQASRISDR 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
466-565 |
2.07e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 49.32 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFilhAKK--TAFIVEHDFIMATYLADRVIVYEGQP 543
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL---AEEgmTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
90 100
....*....|....*....|....*....
gi 15231301 544 avkcIAH--SPQSLLSG-----MNHFLSH 565
Cdd:PRK09493 214 ----IAEdgDPQVLIKNppsqrLQEFLQH 238
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
103-293 |
2.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.66 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGR-----FNtPPDWEEILTHFR---GSELQSYFIRVVEENLKtaikpqhvd 174
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgVD-ITDKKVKLSDIRkkvGLVFQYPEYQLFEETIE--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 yiKEVVRG--NLGKMLEKLDER--GLMEEICADMElnQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:PRK13637 103 --KDIAFGpiNLGLSEEEIENRvkRAMNIVGLDYE--DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 251 QRLKAAQVIRSLlrHDSY---VIVVEHDLSVLDYLSDFV-------CCLYGKP 293
Cdd:PRK13637 179 GRDEILNKIKEL--HKEYnmtIILVSHSMEDVAKLADRIivmnkgkCELQGTP 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
103-276 |
2.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.78 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTppdwEEILTHfrgSELQSYFIRVVEENLKTAIK-PQHV---DYI-K 177
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV----DDITIT---HKTKDKYIRPVRKRIGMVFQfPESQlfeDTVeR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 178 EVVRG--NLGKMLEKLDERG--LMeeicadMELN---QVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:PRK13646 106 EIIFGpkNFKMNLDEVKNYAhrLL------MDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180
....*....|....*....|....*..
gi 15231301 251 QRLKAAQVIRSL-LRHDSYVIVVEHDL 276
Cdd:PRK13646 180 SKRQVMRLLKSLqTDENKTIILVSHDM 206
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-544 |
2.23e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqSEIPEFNVSYKPQG----NdskreCTVRQ--LL 432
Cdd:PTZ00243 676 LRDVSVSVPRGKLT-----VVLGATGSGKSTLLQSLLSQFEISEG--RVWAERSIAYVPQQawimN-----ATVRGniLF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 433 HDKIRDACAHpqfmsDVIRPLQIEQLMDQV---VKT--------LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE-- 499
Cdd:PTZ00243 744 FDEEDAARLA-----DAVRVSQLEADLAQLgggLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvg 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 500 QRITASKVIKRFilhAKKTAFIVEH--------DFIMAtyLADRVIVYEGQPA 544
Cdd:PTZ00243 819 ERVVEECFLGAL---AGKTRVLATHqvhvvpraDYVVA--LGDGRVEFSGSSA 866
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
356-537 |
2.24e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.94 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 356 TKQLGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF---NVSYKPQgndskr 424
Cdd:PRK10247 20 AKILNNISFSLRAGEFK-----LITGPSGCGKSTLLKIVASLISPTSGtllfegedISTLKPEIyrqQVSYCAQ------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 ectVRQLLHDKIRDACAHP-----------QFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPS 493
Cdd:PRK10247 89 ---TPTLFGDTVYDNLIFPwqirnqqpdpaIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 494 AHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYlADRVI 537
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
103-252 |
2.47e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGklkpnlgrfntppdWEEIlthfRGSELqsyFI--RVVeenlkTAIKPQHVDyIKEV- 179
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAG--------------LERI----TSGEI---WIggRVV-----NELEPADRD-IAMVf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 ----------VRGNLGKML-------EKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDE 242
Cdd:PRK11650 83 qnyalyphmsVRENMAYGLkirgmpkAEIEER--VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170
....*....|
gi 15231301 243 PSSYLDVRQR 252
Cdd:PRK11650 161 PLSNLDAKLR 170
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
456-564 |
2.91e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.44 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 456 EQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFiLHAKKTAFIVEHDFIMATYLADR 535
Cdd:PRK13641 136 EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADD 214
|
90 100 110
....*....|....*....|....*....|....
gi 15231301 536 VIVYEGQpavKCIAH-SPQSLLSGMN----HFLS 564
Cdd:PRK13641 215 VLVLEHG---KLIKHaSPKEIFSDKEwlkkHYLD 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
102-286 |
2.95e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKS-TALKILagKLKPnlgrfnTPP------------------DwEEILTHFRGSELQSYFirvvEE 162
Cdd:PRK15134 34 AGETLALVGESGSGKSvTALSIL--RLLP------SPPvvypsgdirfhgesllhaS-EQTLRGVRGNKIAMIF----QE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 163 NLkTAIKPQHvdyikevvrgNLGKML-EKLD-ERGLMEEiCADMELNQVLER----EAR--------QVSGGELQRFAIA 228
Cdd:PRK15134 101 PM-VSLNPLH----------TLEKQLyEVLSlHRGMRRE-AARGEILNCLDRvgirQAAkrltdyphQLSGGERQRVMIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 229 AVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRH-DSYVIVVEHDLSVLDYLSDFV 286
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRV 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
357-542 |
3.01e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 47.81 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 357 KQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipEFNVSYKPQGNDSKRECTVRQLLH--- 433
Cdd:cd03215 14 GAVRDVSFEVRAGE-----IVGIAGLVGNGQTELAEALFGLRPPASG------EITLDGKPVTRRSPRDAIRAGIAYvpe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 434 DKIRDACAHPQfmsDVIRPLQIEQLmdqvvktLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFIL 513
Cdd:cd03215 83 DRKREGLVLDL---SVAENIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGAKAEIYRLIR 148
|
170 180 190
....*....|....*....|....*....|....*
gi 15231301 514 HAKK--TAFIV---EHDFIMAtyLADRVIV-YEGQ 542
Cdd:cd03215 149 ELADagKAVLLissELDELLG--LCDRILVmYEGR 181
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
350-538 |
3.02e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.41 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGVQSEIP--EFNVSYKPQGNDSKREC 426
Cdd:PRK13640 13 FTYPDSKKPaLNDISFSIPRGSWT-----ALIGHNGSGKSTISKLINGLLLPDDNPNSKITvdGITLTAKTVWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 TV-----RQLLHDKIRDACA---------HPQFMS---DVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLI 489
Cdd:PRK13640 88 IVfqnpdNQFVGATVGDDVAfglenravpRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15231301 490 DEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDfIMATYLADRVIV 538
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLV 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
218-290 |
3.30e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 3.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 218 SGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRlkaAQVIRSL--LRHD---SYVIvVEHDLSVLDYLSDFVCCLY 290
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ---AQVLNLMmdLQQElglSYVF-ISHDLSVVEHIADEVMVMY 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
105-290 |
4.01e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.50 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 105 VLGLVGTNGIGKSTALKILAGKLKPnlgrFNTPPDWEEILTHFRGSELQSYFIRVVEENLKTAIKPQHVDYIKevVRGNL 184
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEI----YDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLS--IYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 185 GKML------EKLDERGLMEEICADM----ELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLK 254
Cdd:PRK14246 112 AYPLkshgikEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQA 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 255 AAQVIRSlLRHDSYVIVVEHDLSVLDYLSDFVCCLY 290
Cdd:PRK14246 192 IEKLITE-LKNEIAIVIVSHNPQQVARVADYVAFLY 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
210-284 |
4.06e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.01 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 210 LEREARQVSGGELQRFAIAAVFVKKAD---IYMFDEPSSYL---DVRQRLkaaQVIRSLLRHDSYVIVVEHDLSVL---D 280
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLL---EVLQRLVDKGNTVVVIEHNLDVIktaD 899
|
....
gi 15231301 281 YLSD 284
Cdd:TIGR00630 900 YIID 903
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
50-74 |
4.11e-06 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 46.24 E-value: 4.11e-06
10 20
....*....|....*....|....*
gi 15231301 50 ISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:cd10549 3 YDPEKCIGCGICVKACPTDAIELGP 27
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
353-541 |
4.17e-06 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 48.35 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 353 PNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAfpreegvqsEIP-EFNVSYKPQGNDSKRECTVRQ- 430
Cdd:cd03258 15 GGKVTALKDVSLSVPKGE-----IFGIIGRSGAGKSTLIRCINGL---------ERPtSGSVLVDGTDLTLLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 431 ------------LLHDK-IRDACAHP---QFMSDVIRPLQIEQLMDQV---------VKTLSGGEKQRVAITLCLGKPAD 485
Cdd:cd03258 81 rrrigmifqhfnLLSSRtVFENVALPleiAGVPKAEIEERVLELLELVgledkadayPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 486 IYLIDEPSAHLDSE--QRITA--SKVIKRFILhakkTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:cd03258 161 VLLCDEATSALDPEttQSILAllRDINRELGL----TIVLITHEMEVVKRICDRVAVMEK 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
102-248 |
4.45e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilthfrgselqsyfIRVVEENLKTAIKPQHVDYIkevvr 181
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQ-----------------------IQIDGKTATRGDRSRFMAYL----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 182 GNLGKMLEKLDERGLMEEICA-------DMELNQVL--------EREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLCGlhgrrakQMPGSALAivglagyeDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
..
gi 15231301 247 LD 248
Cdd:PRK13543 168 LD 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
375-533 |
4.76e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.54 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 375 QIIVMLGENGTGKTTFIRMLAGAFP-----------------REEGV--QSE--IPEFNVsykpQGN-----------DS 422
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPyqhgsitldgkpvegpgAERGVvfQNEglLPWRNV----QDNvafglqlagveKM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 423 KRECTVRQLLHdKIRDACAHPQFmsdvirplqIEQLmdqvvktlSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRI 502
Cdd:PRK11248 104 QRLEIAHQMLK-KVGLEGAEKRY---------IWQL--------SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 503 TASKVIKRFILHAKKTAFIVEHDFIMATYLA 533
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
350-562 |
5.27e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.44 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQ-LGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEGV----QSEIPEFNvsykpqgndskr 424
Cdd:PRK11160 346 FTYPDQPQPvLKGLSLQIKAGEK-----VALLGRTGCGKSTLLQLLTRAWDPQQGEillnGQPIADYS------------ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 ECTVRQ----------LLHDKIRD----AC--AHPQFMSDVIRPLQIEQLMDQVV----------KTLSGGEKQRVAITL 478
Cdd:PRK11160 409 EAALRQaisvvsqrvhLFSATLRDnlllAApnASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 479 CLGKPADIYLIDEPSAHLDS--EQRITAskVIKRFILHakKTAFIVEHDfimATYLA--DRVIVYEGQPAVKCIAHspQS 554
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAetERQILE--LLAEHAQN--KTVLMITHR---LTGLEqfDRICVMDNGQIIEQGTH--QE 559
|
....*...
gi 15231301 555 LLSGMNHF 562
Cdd:PRK11160 560 LLAQQGRY 567
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
108-275 |
5.42e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 108 LVGTNGIGKSTALKILAGKLKPNLGRFNTppdweeilthfrGSELQ-SYFI---------RVVEENL---KTAI----KP 170
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHC------------GTKLEvAYFDqhraeldpeKTVMDNLaegKQEVmvngRP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 171 QHVdyikevvrgnLGKMLEKL--DERGlMEEIcadmelnqvlereaRQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:PRK11147 418 RHV----------LGYLQDFLfhPKRA-MTPV--------------KALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180 190
....*....|....*....|....*....|
gi 15231301 249 VrqrlKAAQVIRSLLrhDSY---VIVVEHD 275
Cdd:PRK11147 473 V----ETLELLEELL--DSYqgtVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
103-497 |
5.50e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDWEEILTHFRGSELQSYF------IRVVEENLKTAIKPQHVDYI 176
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQEVVGDDTTALQCVLntdierTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEVVRGN-----------LGKMLEKLDER-GLMEEICADMELNQVL----------EREARQVSGGELQRFAIAAVFVKK 234
Cdd:PLN03073 283 TETGKGKgankdgvdkdaVSQRLEEIYKRlELIDAYTAEARAASILaglsftpemqVKATKTFSGGWRMRIALARALFIE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 235 ADIYMFDEPSSYLDvrqrLKAAQVIRS-LLRHDSYVIVVEHDLSVLDYLSDFVCCLYGKP-----GAYGVvtlpfsvreg 308
Cdd:PLN03073 363 PDLLLLDEPTNHLD----LHAVLWLETyLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKlvtykGDYDT---------- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 309 invflagFIPTENLRFRDESLTFRVSETTQEN------------------DGEVKSYARYKYPNMTKQLGDFKLEVMEGE 370
Cdd:PLN03073 429 -------FERTREEQLKNQQKAFESNERSRSHmqafidkfrynakraslvQSRIKALDRLGHVDAVVNDPDYKFEFPTPD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 371 ---------FTDSQI---------------------IVMLGENGTGKTTFIRMLAGAFPREEGVQSEIPEFNVSYKPQGN 420
Cdd:PLN03073 502 drpgppiisFSDASFgypggpllfknlnfgidldsrIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHH 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 421 DSKRECTVRQLLH----------DKIRdacAHpqfmsdvIRPLQIE-QLMDQVVKTLSGGEKQRVAITLCLGKPADIYLI 489
Cdd:PLN03073 582 VDGLDLSSNPLLYmmrcfpgvpeQKLR---AH-------LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
....*...
gi 15231301 490 DEPSAHLD 497
Cdd:PLN03073 652 DEPSNHLD 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
210-537 |
5.68e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 210 LEREARQVSGGELQRFAIAA------VFVkkadIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHD---LSVLD 280
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATqigsglTGV----LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDedtIRAAD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 281 YLSDFvcclygKPGAyGVvtlpfsvrEGINVFLAGfiPTENLRFRDESLTFRVseTTQENDGEVKSYARYKYPNMTKQLG 360
Cdd:TIGR00630 558 YVIDI------GPGA-GE--------HGGEVVASG--TPEEILANPDSLTGQY--LSGRKKIEVPAERRPGNGKFLTLKG 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 361 -------DFKLEVMEGEFTdsqiiVMLGENGTGKTTFI---------------RMLAGAFPREEGVQSEIPEFNVSYKPQ 418
Cdd:TIGR00630 619 arennlkNITVSIPLGLFT-----CITGVSGSGKSTLIndtlypalanrlngaKTVPGRYTSIEGLEHLDKVIHIDQSPI 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 GNDSKRECTVRQLLHDKIRD-------------------------ACAHPQ----------FMSDVIRP----------- 452
Cdd:TIGR00630 694 GRTPRSNPATYTGVFDEIRElfaetpeakvrgytpgrfsfnvkggRCEACQgdgvikiemhFLPDVYVPcevckgkrynr 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 453 --LQI--------------------------------EQLMD---------QVVKTLSGGEKQRVAITLCLGKPAD---I 486
Cdd:TIGR00630 774 etLEVkykgkniadvldmtveeayeffeavpsisrklQTLCDvglgyirlgQPATTLSGGEAQRIKLAKELSKRSTgrtL 853
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 487 YLIDEPSAHLDSEQRITASKVIKRFIlHAKKTAFIVEHDF-IMATylADRVI 537
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVIEHNLdVIKT--ADYII 902
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
3-82 |
5.72e-06 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 49.25 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 3 DRLTRIAIVSEDRCKPKKCRQECKKSCPVVKTGKLCIEVGSTSKSAFISEELCIGCGICVKKCPFEAIQIINLPKDLAKD 82
Cdd:COG4624 41 HVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEIDEE 120
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
188-280 |
5.77e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 188 LEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDS 267
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100
....*....|....*....|...
gi 15231301 268 YVIV----------VEHDLSVLD 280
Cdd:NF000106 196 TVLLttqymeeaeqLAHELTVID 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
438-553 |
5.79e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 438 DACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLG-KPAdIYLIDEPSAHLDSEQRITASKVIKRFILHAK 516
Cdd:PRK10261 141 EAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALScRPA-VLIADEPTTALDVTIQAQILQLIKVLQKEMS 219
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15231301 517 KTAFIVEHDFIMATYLADRVIV-YEGQP----AVKCIAHSPQ 553
Cdd:PRK10261 220 MGVIFITHDMGVVAEIADRVLVmYQGEAvetgSVEQIFHAPQ 261
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
354-538 |
5.90e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.56 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLG------DFKLEVMEGeftdsQIIVMLGENGTGKTTFIRMLAG--------AFPREEGV------QSEI----- 408
Cdd:PRK11432 11 NITKRFGsntvidNLNLTIKQG-----TMVTLLGPSGCGKTTVLRLVAGlekptegqIFIDGEDVthrsiqQRDIcmvfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 409 -----PEF----NVSY--KPQGNdSKREctVRQllhdKIRDACAhpqfMSDvirplqIEQLMDQVVKTLSGGEKQRVAIT 477
Cdd:PRK11432 86 syalfPHMslgeNVGYglKMLGV-PKEE--RKQ----RVKEALE----LVD------LAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 478 LCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIV 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
354-538 |
6.46e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqsEIpefnvsykpqgndskrect 427
Cdd:COG3845 10 GITKRFGGVVanddvsLTVRPGE-----IHALLGENGAGKSTLMKILYGLYQPDSG---EI------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 vrqLLHDK---I---RDACA------HPQFMsdVIRPL-------------------------QIEQLMDQ--------- 461
Cdd:COG3845 63 ---LIDGKpvrIrspRDAIAlgigmvHQHFM--LVPNLtvaenivlgleptkggrldrkaaraRIRELSERygldvdpda 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 462 VVKTLSGGEKQRVAI--TLCLGkpADIyLI-DEPSAHLdSEQRITA-SKVIKRFIlHAKKTAFIVEHDF--IMAtyLADR 535
Cdd:COG3845 138 KVEDLSVGEQQRVEIlkALYRG--ARI-LIlDEPTAVL-TPQEADElFEILRRLA-AEGKSIIFITHKLreVMA--IADR 210
|
...
gi 15231301 536 VIV 538
Cdd:COG3845 211 VTV 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
351-539 |
6.72e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 351 KYPNMTKQLGDFKLEVMEGEFtdsqiIVMLGENGTGKTTFIRMLAGAFPREEG-----------------VQSEIPEFNV 413
Cdd:PRK13651 15 KLPTELKALDNVSVEINQGEF-----IAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkeKEKVLEKLVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 414 SyKPQGNDSKRECTVR------------QLLHDKI-RDACAHPqfMSDVIRPLQIEQLMDQVVK--------------TL 466
Cdd:PRK13651 90 Q-KTRFKKIKKIKEIRrrvgvvfqfaeyQLFEQTIeKDIIFGP--VSMGVSKEEAKKRAAKYIElvgldesylqrspfEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 467 SGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfiLHAK-KTAFIVEHDFIMATYLADRVIVY 539
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN--LNKQgKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
459-537 |
7.18e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 459 MDQVVKTLSGGEKQRVAITLCLGKPAD--IYLIDEPSAHL---DSEQRITASKVIKrfilHAKKTAFIVEHD--FIMAty 531
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhprDNDRLIETLKRLR----DLGNTVLVVEHDedTIRA-- 204
|
....*.
gi 15231301 532 lADRVI 537
Cdd:cd03270 205 -ADHVI 209
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
205-287 |
8.34e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 205 ELNQVLEREARQVSGGE------LQRFAIAAVFVKKADIYMFDEPSSYLD---VRQRLkaAQVIRSLLR-HDSYVIVVEH 274
Cdd:cd03240 104 ESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDeenIEESL--AEIIEERKSqKNFQLIVITH 181
|
90
....*....|...
gi 15231301 275 DLSVLDYLSDFVC 287
Cdd:cd03240 182 DEELVDAADHIYR 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
81-276 |
8.47e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.81 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRY--GANGFKLHRLPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPN------LGRFNTPPDWEEILTH----FR 148
Cdd:PRK13647 8 EDLHFRYkdGTKALKGLSLSIPE-GSKTALLGPNGAGKSTLLLHLNGIYLPQrgrvkvMGREVNAENEKWVRSKvglvFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 149 GSELQsYFIRVVEENLktAIKPQhvdyikevvrgNLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIA 228
Cdd:PRK13647 87 DPDDQ-VFSSTVWDDV--AFGPV-----------NMGLDKDEVERR--VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231301 229 AVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDV 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
464-539 |
9.80e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 9.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 464 KTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDfIMATYLADRVIVY 539
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR-IASIKRSDKIVVF 1431
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
101-247 |
1.07e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQsyfIRvveeNLKTAIK------PQH-- 172
Cdd:COG3845 29 RPGEIHALLGENGAGKSTLMKILYGLYQPDSG---------EIL--IDGKPVR---IR----SPRDAIAlgigmvHQHfm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 -VDY--IKE-VVRGNLGKMLEKLD---ERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:COG3845 91 lVPNltVAEnIVLGLEPTKGGRLDrkaARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
..
gi 15231301 246 YL 247
Cdd:COG3845 171 VL 172
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
215-277 |
1.07e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.44 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 215 RQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLS 277
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
103-286 |
1.09e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.43 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTppDWEEILTHFRGSELQSyfIR-------------VVEEN-LK-TA 167
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV--DDTLITSTSKNKDIKQ--IRkkvglvfqfpesqLFEETvLKdVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 168 IKPQHVDYIKEVVRGnlgKMLEKLDERGLMEEIcadmelnqvLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYL 247
Cdd:PRK13649 109 FGPQNFGVSQEEAEA---LAREKLALVGISESL---------FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15231301 248 DVRQRLKAAQVIRSLLRHDSYVIVVEHDL-SVLDYlSDFV 286
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANY-ADFV 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
103-291 |
1.10e-05 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 47.30 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNTPPDWEEILTHFR---GSELQSYFI---RVVEENlkTAIKPQHVD 174
Cdd:cd03295 27 GEFLVLIGPSGSGKTTTMKMINRLIEPTSGEifIDGEDIREQDPVELRrkiGYVIQQIGLfphMTVEEN--IALVPKLLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 175 YIKEVVRgnlgkmlEKLDErgLMEEIcaDMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLK 254
Cdd:cd03295 105 WPKEKIR-------ERADE--LLALV--GLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 15231301 255 AAQVIRSLLRHDSYVIV-VEHDLSVLDYLSDFVCCLYG 291
Cdd:cd03295 174 LQEEFKRLQQELGKTIVfVTHDIDEAFRLADRIAIMKN 211
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
24-72 |
1.13e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 45.25 E-value: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 24 ECKKSCPVvktgklcievGSTSKSA----FISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd16371 61 ACVKVCPT----------GAITKREdgivVVDQDKCIGCGYCVWACPYGAPQY 103
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
350-538 |
1.24e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.54 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqsEIPEFN--VSYKPQGNDSKRE-- 425
Cdd:PRK13636 13 YNYSDGTHALKGININIKKGEVT-----AILGGNGAGKSTLFQNLNGILKPSSG---RILFDGkpIDYSRKGLMKLREsv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 -------------CTVRQ----------LLHDKIRDACAHpqfmsdVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGK 482
Cdd:PRK13636 85 gmvfqdpdnqlfsASVYQdvsfgavnlkLPEDEVRKRVDN------ALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 483 PADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIV 538
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFV 214
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
218-284 |
1.25e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 1.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 218 SGGELQRFAIAAVFVKKAD---IYMFDEPSSYL---DVRQRLkaaQVIRSLLRHDSYVIVVEHDLSVL---DYLSD 284
Cdd:cd03271 171 SGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLL---EVLQRLVDKGNTVVVIEHNLDVIkcaDWIID 243
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-74 |
1.28e-05 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 47.02 E-value: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 8 IAIVSEDRCKPKKCRQECKKSCPVVKTGKLCIEVGSTSKSAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG1145 137 AALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKD 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
103-291 |
1.32e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELQSYFIRVVEENLKTAIKPQHVD------YI 176
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGILKPTSG---------EVL--IKGEPIKYDKKSLLEVRKTVGIVFQNPDdqlfapTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KE-VVRG--NLGKMLEKLDERglMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRL 253
Cdd:PRK13639 97 EEdVAFGplNLGLSKEEVEKR--VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 15231301 254 KAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLYG 291
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSD 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
103-290 |
1.38e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeiltHFRGSELQsyFIRVVEENLKTAIKPQhvdyiKEVVRG 182
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSI-----------VVNGQTIN--LVRDKDGQLKVADKNQ-----LRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 183 NLGKMLEKLDERGLMEEICADMELN-QVL---EREARQ----------------------VSGGELQRFAIAAVFVKKAD 236
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAPiQVLglsKQEAREravkylakvgideraqgkypvhLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15231301 237 IYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFVCCLY 290
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
359-511 |
1.48e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 46.76 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGV---QSEIPEFNV-------SYKPQGNDSKRECTV 428
Cdd:COG4138 12 LGPISAQVNAGE-----LIHLIGPNGAGKSTLLARMAGLLPGQGEIllnGRPLSDWSAaelarhrAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQLLHDKIRDACAHP---QFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCL----------GKpadIYLIDEPSAH 495
Cdd:COG4138 87 FQYLALHQPAGASSEaveQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinpeGQ---LLLLDEPMNS 163
|
170
....*....|....*.
gi 15231301 496 LDSEQRITASKVIKRF 511
Cdd:COG4138 164 LDVAQQAALDRLLREL 179
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
359-544 |
1.50e-05 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 47.03 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEGvqseipefNVSY--KPQGNDSKRE----------- 425
Cdd:COG4559 17 LDDVSLTLRPGELT-----AIIGPNGAGKSTLLKLLTGELTPSSG--------EVRLngRPLAAWSPWElarrravlpqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 426 ------CTVRQL----LHDKIRDACAHPQFMSDVIRPLQIEQLMDQVVKTLSGGEKQRV--AITLC-LGKPAD----IYL 488
Cdd:COG4559 84 sslafpFTVEEVvalgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVqlARVLAqLWEPVDggprWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 489 IDEPSAHLD-SEQRITASKViKRFiLHAKKTAFIVEHDFIMATYLADRV-------IVYEGQPA 544
Cdd:COG4559 164 LDEPTSALDlAHQHAVLRLA-RQL-ARRGGGVVAVLHDLNLAAQYADRIlllhqgrLVAQGTPE 225
|
|
| PorD_KorD |
TIGR02179 |
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number ... |
10-73 |
1.68e-05 |
|
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins.
Pssm-ID: 131234 [Multi-domain] Cd Length: 78 Bit Score: 43.09 E-value: 1.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 10 IVSEDRCKpkKCRqECKKSCPvvktgKLCIEVGSTSKSAfISEELCIGCGICVKKCPFEAIQII 73
Cdd:TIGR02179 21 VVDKEKCI--KCK-NCWLYCP-----EGAIQEDEGGFVG-IDYDYCKGCGICANVCPVKAIEMV 75
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
459-522 |
1.70e-05 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 46.48 E-value: 1.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 459 MDQVVKTLSGGEKQRVAITL--CLGK--PADIYLIDEPSAHLDSEQRITASKVIKRFilhAKKTAFIV 522
Cdd:cd03272 152 EQQEMQQLSGGQKSLVALALifAIQKcdPAPFYLFDEIDAALDAQYRTAVANMIKEL---SDGAQFIT 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
99-262 |
1.76e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 99 IPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLG------RFNTPPDwEEILTHFRG-----SELQSYF-IRVVEENLKT 166
Cdd:TIGR00956 83 LIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIgvegviTYDGITP-EEIKKHYRGdvvynAETDVHFpHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 167 AIKPQHVdyikevvrGNLGKMLEKLDERGLMEEICA-----DMELNQVLERE-ARQVSGGELQRFAIAAVFVKKADIYMF 240
Cdd:TIGR00956 162 AARCKTP--------QNRPDGVSREEYAKHIADVYMatyglSHTRNTKVGNDfVRGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180
....*....|....*....|..
gi 15231301 241 DEPSSYLDVRqrlKAAQVIRSL 262
Cdd:TIGR00956 234 DNATRGLDSA---TALEFIRAL 252
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
102-280 |
1.82e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilthfrgselqsyfirvveenlktaikpqhvdyikeVVR 181
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG---------------------------------------------VIY 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 182 GNLGKMLEKLDERglmeeicadmELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQR------LKA 255
Cdd:smart00382 36 IDGEDILEEVLDQ----------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEalllllEEL 105
|
170 180
....*....|....*....|....*
gi 15231301 256 AQVIRSLLRHDSYVIVVEHDLSVLD 280
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
97-290 |
1.85e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.37 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 97 LPIPRPGqVLGLVGTNGIGKSTALKILAGKLKPNlgrfntPPDWEEILTHFRGSELQSYFIRVVEENLKTAIKPQ----- 171
Cdd:PRK14267 25 LKIPQNG-VFALMGPSGCGKSTLLRTFNRLLELN------EEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQypnpf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 -HVDYIKEVVRG----NLGKMLEKLDER---GLMEEICADmELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEP 243
Cdd:PRK14267 98 pHLTIYDNVAIGvklnGLVKSKKELDERvewALKKAALWD-EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 244 SSYLDVRQRLKAAQVIRSlLRHDSYVIVVEHDLSVLDYLSDFVCCLY 290
Cdd:PRK14267 177 TANIDPVGTAKIEELLFE-LKKEYTIVLVTHSPAQAARVSDYVAFLY 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
350-540 |
1.94e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.65 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNMTKQLGDFKLEVMEGeftdsQIIVMLGENGTGKTTFIRMLAGAFPREEGVQSeIPEFNVSykpqgnDSKREC--- 426
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPG-----QTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL-IDGTDIR------TVTRASlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 427 ---TVRQ---LLHDKIRD--------------------ACAHpqfmsDVIrpLQIEQLMDQVV----KTLSGGEKQRVAI 476
Cdd:PRK13657 410 niaVVFQdagLFNRSIEDnirvgrpdatdeemraaaerAQAH-----DFI--ERKPDGYDTVVgergRQLSGGERQRLAI 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 477 TLCLGKPADIYLIDEPSAHLDSEqriTASKViKRFI--LHAKKTAFIVEHDfiMATYL-ADRVIVYE 540
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVE---TEAKV-KAALdeLMKGRTTFIIAHR--LSTVRnADRILVFD 543
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
466-505 |
1.97e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.51 E-value: 1.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDS--EQRITAS 505
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSrtERAIQAA 536
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
460-537 |
2.00e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 460 DQVVKTLSGGEKQRVAITLCLGkpADI----YLIDEPSAHL---DSEQRItasKVIKRfILHAKKTAFIVEHDFIMATyL 532
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLG--AELigitYILDEPSIGLhpqDTHKLI---NVIKK-LRDQGNTVLLVEHDEQMIS-L 543
|
....*
gi 15231301 533 ADRVI 537
Cdd:PRK00635 544 ADRII 548
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
92-290 |
2.02e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 92 FKLHRlpiprpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDW---------------EEILTHFRGSELQSYF 156
Cdd:PRK10261 37 FSLQR------GETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLlrrrsrqvielseqsAAQMRHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 157 irvvEENLkTAIKPQHV--DYIKEVVR--GNLGKMlEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFV 232
Cdd:PRK10261 111 ----QEPM-TSLNPVFTvgEQIAESIRlhQGASRE-EAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 233 KKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSY-VIVVEHDLSVLDYLSDFVCCLY 290
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMY 243
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
381-517 |
2.03e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 381 GENGTGKTTFIRMLAGAFPREEGvqsEIPEFNVSYKpqgndsKRECTVRQLL-----------HDKIRDACAHPQFMS-- 447
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKG---EILFERQSIK------KDLCTYQKQLcfvghrsginpYLTLRENCLYDIHFSpg 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 448 -----DVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITaskVIKRFILHAKK 517
Cdd:PRK13540 105 avgitELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT---IITKIQEHRAK 176
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
14-72 |
2.21e-05 |
|
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.
Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 45.84 E-value: 2.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 14 DRCKpkKCRQE-CKKSCPvvkTGKLC-IEVGSTsksaFISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd10560 76 DVCK--HCTDAgCLEACP---TGAIFrTEFGTV----YIQPDICNGCGYCVAACPFGVIDR 127
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
102-275 |
2.29e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF-------------NTPPDWEEILTHFrgsELQSYFirvveenlktaI 168
Cdd:PRK15064 344 AGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqDHAYDFENDLTLF---DWMSQW-----------R 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 169 KPQHVDyikEVVRGNLGKMLEKLDErglmeeicadmelnqvLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLD 248
Cdd:PRK15064 410 QEGDDE---QAVRGTLGRLLFSQDD----------------IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
170 180 190
....*....|....*....|....*....|.
gi 15231301 249 VrqrlkaaQVIRSL-LRHDSY---VIVVEHD 275
Cdd:PRK15064 471 M-------ESIESLnMALEKYegtLIFVSHD 494
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
101-275 |
2.48e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.86 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILthFRGSELqsyfirvveenlkTAIKP----QHVDY- 175
Cdd:PRK10247 31 RAGEFKLITGPSGCGKSTLLKIVASLISPTSG---------TLL--FEGEDI-------------STLKPeiyrQQVSYc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 ------IKEVVRGNL-------------GKMLEKLDERGLMEEIcadmelnqvLEREARQVSGGELQRFAIAAVFVKKAD 236
Cdd:PRK10247 87 aqtptlFGDTVYDNLifpwqirnqqpdpAIFLDDLERFALPDTI---------LTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15231301 237 IYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHD 275
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHD 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
81-274 |
2.61e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 81 KDTTHRYGANGfKLHRLPIP------RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPpdwEEILTH-------- 146
Cdd:PRK13634 6 QKVEHRYQYKT-PFERRALYdvnvsiPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG---ERVITAgkknkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 147 ---------FRGSELQsYFIRVVEENLktAIKPQHVDYIKEVVRGNLGKMLEKLderGLMEEicadmelnqVLEREARQV 217
Cdd:PRK13634 82 plrkkvgivFQFPEHQ-LFEETVEKDI--CFGPMNFGVSEEDAKQKAREMIELV---GLPEE---------LLARSPFEL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 218 SGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEH 274
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTH 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
102-280 |
2.68e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdwEEILThfrgselqsyfirvveENLKTAIKPQ--HVDYIKEv 179
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG--------EARPA----------------PGIKVGYLPQepQLDPEKT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 180 VRGN----LGKMLEKLDE-----------RGLMEEICADM-------------ELNQVLEREA------------RQVSG 219
Cdd:PRK11819 87 VRENveegVAEVKAALDRfneiyaayaepDADFDALAAEQgelqeiidaadawDLDSQLEIAMdalrcppwdakvTKLSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 220 GELQRFAIAAVFVKKADIYMFDEPSSYLDvrqrlkaAQVIRSLLRH-DSY---VIVVEHDLSVLD 280
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD-------AESVAWLEQFlHDYpgtVVAVTHDRYFLD 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
103-276 |
2.69e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLG-------RFNTPPDW---EEILTHFRGSELQsYFIRVVEENLKTAIKPQH 172
Cdd:PRK13642 33 GEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENVWnlrRKIGMVFQNPDNQ-FVGATVEDDVAFGMENQG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 VDyiKEvvrgnlgKMLEKLDERGLMeeicadMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQR 252
Cdd:PRK13642 112 IP--RE-------EMIKRVDEALLA------VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180
....*....|....*....|....*..
gi 15231301 253 LKAAQVIRSLlrHDSY---VIVVEHDL 276
Cdd:PRK13642 177 QEIMRVIHEI--KEKYqltVLSITHDL 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
102-284 |
2.69e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.92 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKIL--AGKLKPNLGRFNTppdweeilTHFRGSELQSYFIRVVEenLKTAI-------KPQH 172
Cdd:PRK14239 30 PNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGS--------IVYNGHNIYSPRTDTVD--LRKEIgmvfqqpNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 VDYIKEVVRG---NLGKMLEKLD---ERGLMEEICADmELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSY 246
Cdd:PRK14239 100 MSIYENVVYGlrlKGIKDKQVLDeavEKSLKGASIWD-EVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15231301 247 LDvrqRLKAAQVIRSL--LRHDSYVIVVEHDLSVLDYLSD 284
Cdd:PRK14239 179 LD---PISAGKIEETLlgLKDDYTMLLVTRSMQQASRISD 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
349-558 |
3.26e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.52 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 349 RYKYPNMTKQlgdFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGvqseipefNVSYkpQGND------S 422
Cdd:COG3840 8 TYRYGDFPLR---FDLTIAAGE-----RVAILGPSGAGKSTLLNLIAGFLPPDSG--------RILW--NGQDltalppA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 423 KR-------------ECTVRQ---L-LHDKIR-DACAHPQfMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCL--GK 482
Cdd:COG3840 70 ERpvsmlfqennlfpHLTVAQnigLgLRPGLKlTAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvrKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 483 PadIYLIDEPSAHLD---------------SEQRITaskvikrfILhakktafIVEHDFIMATYLADRVI-VYEGqpavK 546
Cdd:COG3840 149 P--ILLLDEPFSALDpalrqemldlvdelcRERGLT--------VL-------MVTHDPEDAARIADRVLlVADG----R 207
|
250
....*....|...
gi 15231301 547 CIAHSP-QSLLSG 558
Cdd:COG3840 208 IAADGPtAALLDG 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
465-538 |
3.34e-05 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 46.67 E-value: 3.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 465 TLSGGEKQRVAITLCL-GKPAdIYLIDEPSAHLDSEqritASKVIKRFILHAKK---TAFIVEHDF-IMAtyLADRVIV 538
Cdd:COG4618 467 RLSGGQRQRIGLARALyGDPR-LVVLDEPNSNLDDE----GEAALAAAIRALKArgaTVVVITHRPsLLA--AVDKLLV 538
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
101-281 |
3.36e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 44.85 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPnlgrfntppdweeilTHFRGSelqsyfIRVVEENLKTAIKPQHVDYIkevv 180
Cdd:cd03213 33 KPGELTAIMGPSGAGKSTLLNALAGRRTG---------------LGVSGE------VLINGRPLDKRSFRKIIGYV---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 rgnlgkmleklderglMEEicaDMELNQVLEREA-------RQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRL 253
Cdd:cd03213 88 ----------------PQD---DILHPTLTVRETlmfaaklRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180
....*....|....*....|....*...
gi 15231301 254 KAAQVIRSLLRHDSYVIVVEHDLSVLDY 281
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQPSSEIF 176
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
96-266 |
3.48e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 96 RLPIPrPGQVLGLVGTNGIGKSTALKILAGKLKPNlgrfntppdwEEILTHFRGS-----ELQSYFIRVVEENLKTAIKP 170
Cdd:PLN03232 637 NLEIP-VGSLVAIVGGTGEGKTSLISAMLGELSHA----------ETSSVVIRGSvayvpQVSWIFNATVRENILFGSDF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 171 QHVDYIKEVvrgNLGKMLEKLDerglmeeICADMELNQVLEREArQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR 250
Cdd:PLN03232 706 ESERYWRAI---DVTALQHDLD-------LLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170
....*....|....*.
gi 15231301 251 QrlkAAQVIRSLLRHD 266
Cdd:PLN03232 775 V---AHQVFDSCMKDE 787
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
464-535 |
3.80e-05 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 45.50 E-value: 3.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 464 KTLSGGEKQRVAITLCL-GKPAdIYLIDEPSAHLDSEqriTASKVIK-RFILHAKK--TAFIVEHDfimaTYLADR 535
Cdd:COG4181 145 AQLSGGEQQRVALARAFaTEPA-ILFADEPTGNLDAA---TGEQIIDlLFELNRERgtTLVLVTHD----PALAAR 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
97-285 |
4.27e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.54 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 97 LPIPRpGQVLGLVGTNGIGKSTALKILagklkpnlGRFN--TPPDWEEILTHFRGSELQSYFIRVVEENLKTAI---KPQ 171
Cdd:PRK14243 31 LDIPK-NQITAFIGPSGCGKSTILRCF--------NRLNdlIPGFRVEGKVTFHGKNLYAPDVDPVEVRRRIGMvfqKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HV-----DYIKEVVRGNLGKM-LEKLDERGLMEEICADmELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:PRK14243 102 PFpksiyDNIAYGARINGYKGdMDELVERSLRQAALWD-EVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15231301 246 YLDVRQRLKAAQVIRSLLRhDSYVIVVEHDLSVLDYLSDF 285
Cdd:PRK14243 181 ALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVSDM 219
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
52-73 |
4.61e-05 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 41.65 E-value: 4.61e-05
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
104-281 |
4.75e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.61 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 104 QVLGLVGTNGIGKSTALKILAGKLKPNLG----------------RFNTPPDWEEILTHFRGSELQSYFIRVVEENL-KT 166
Cdd:PRK13631 53 KIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhELITNPYSKKIKNFKELRRRVSMVFQFPEYQLfKD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 167 AIKpqhvdyiKEVVRGNLGKMLEKLDERGLMEEICADMELNQ-VLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSS 245
Cdd:PRK13631 133 TIE-------KDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15231301 246 YLDVRQRLKAAQVIRSLLRHDSYVIVV----EHDLSVLDY 281
Cdd:PRK13631 206 GLDPKGEHEMMQLILDAKANNKTVFVIthtmEHVLEVADE 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
102-279 |
4.91e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAgKLKPNLGRFNTPP-DWEEI-LTHFR---GSELQSYFIrvVEENLKTAIKPqHVDYI 176
Cdd:TIGR01271 1244 GGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVtLQTWRkafGVIPQKVFI--FSGTFRKNLDP-YEQWS 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 177 KEvvrgNLGKMLEKLDERGLMEEICAdmELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVrqrlKAA 256
Cdd:TIGR01271 1320 DE----EIWKVAEEVGLKSVIEQFPD--KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP----VTL 1389
|
170 180
....*....|....*....|....*.
gi 15231301 257 QVIRSLLRH---DSYVIVVEHDLSVL 279
Cdd:TIGR01271 1390 QIIRKTLKQsfsNCTVILSEHRVEAL 1415
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
21-72 |
5.27e-05 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 44.17 E-value: 5.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 21 CRQ----ECKKSCPVvktgklcievGSTSKSA----FISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG0437 60 CNHcddpPCVKVCPT----------GATYKREdgivLVDYDKCIGCRYCVAACPYGAPRF 109
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
7-73 |
5.83e-05 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 44.02 E-value: 5.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 7 RIAIVSEDRCKpkKCrQECKKSCPVVKTgklcieVGSTSKSAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:TIGR01944 106 MVALIDEDNCI--GC-TKCIQACPVDAI------VGAAKAMHTVIADECTGCDLCVEPCPTDCIEMI 163
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
49-74 |
5.87e-05 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 44.85 E-value: 5.87e-05
10 20
....*....|....*....|....*.
gi 15231301 49 FISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:NF038196 181 FHVTDKCIGCGICAKVCPVNNIEMED 206
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
44-72 |
5.93e-05 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 41.57 E-value: 5.93e-05
10 20
....*....|....*....|....*....
gi 15231301 44 TSKSAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG4231 13 TAMRYVIDEDKCTGCGACVKVCPADAIEE 41
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
102-290 |
6.91e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKIL-------AGKLKPNLGRFNTPPDweeilthfrgSELQSYF--IRVVEENLKTAIKPQH 172
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALlrlvesqGGEIIFNGQRIDTLSP----------GKLQALRrdIQFIFQDPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 -VDYikevvrgnlgKMLEKLDERGLMEEICADMELNQVLEREA----------RQVSGGELQRFAIAAVFVKKADIYMFD 241
Cdd:PRK10261 419 tVGD----------SIMEPLRVHGLLPGKAAAARVAWLLERVGllpehawrypHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15231301 242 EPSSYLDVRQRlkaAQVIRSL--LRHDSYV--IVVEHDLSVLDYLSDFVCCLY 290
Cdd:PRK10261 489 EAVSALDVSIR---GQIINLLldLQRDFGIayLFISHDMAVVERISHRVAVMY 538
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
55-74 |
7.00e-05 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 44.92 E-value: 7.00e-05
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
466-564 |
7.27e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.96 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfILHAKKTAFIVEHDFIMATYLADRVIVY------ 539
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVIFLhqgkie 231
|
90 100
....*....|....*....|....*.
gi 15231301 540 -EGQPAVkcIAHSPQSllSGMNHFLS 564
Cdd:PRK10619 232 eEGAPEQ--LFGNPQS--PRLQQFLK 253
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
92-249 |
9.42e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.46 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 92 FKLHRLPIPR-------PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeilthfRGSELQSYFIRV----- 159
Cdd:cd03291 45 LCLVGAPVLKninlkieKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFswimp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 160 --VEENLKTAIKPQHVDYIKEVVRGNLGKMLEKLDERGlmeeicadmelNQVLEREARQVSGGELQRFAIAAVFVKKADI 237
Cdd:cd03291 112 gtIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKD-----------NTVLGEGGITLSGGQRARISLARAVYKDADL 180
|
170
....*....|..
gi 15231301 238 YMFDEPSSYLDV 249
Cdd:cd03291 181 YLLDSPFGYLDV 192
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
55-80 |
9.66e-05 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 40.23 E-value: 9.66e-05
10 20
....*....|....*....|....*.
gi 15231301 55 CIGCGICVKKCPFEAIQIINLPKDLA 80
Cdd:pfam13187 2 CTGCGACVAACPAGAIVPDLVGQTIR 27
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
101-293 |
9.78e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 44.02 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALkilagklkpnlgrfntppdweeiLTHFRGSELQSYFIRVVEENLKT----------AIKP 170
Cdd:cd03244 28 KPGEKVGIVGRTGSGKSSLL-----------------------LALFRLVELSSGSILIDGVDISKiglhdlrsriSIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 171 QHVDYIKEVVRGNL--------GKMLEKLDERGLmEEICADME--LNQVLEREARQVSGGELQRFAIAAVFVKKADIYMF 240
Cdd:cd03244 85 QDPVLFSGTIRSNLdpfgeysdEELWQALERVGL-KEFVESLPggLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 241 DEPSSYLDVRQRLKAAQVIRSLLrHDSYVIVVEHDL-SVLDYlsDFVCCL-------YGKP 293
Cdd:cd03244 164 DEATASVDPETDALIQKTIREAF-KDCTVLTIAHRLdTIIDS--DRILVLdkgrvveFDSP 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
96-280 |
1.03e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.31 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 96 RLPiprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFntppdweeilthfrgselqsyfirVVEENLKTAikpqHVDY 175
Cdd:TIGR03719 344 KLP---PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------------------------EIGETVKLA----YVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IKEVVRGNlgkmlekldeRGLMEEICADMELNQVLERE--AR------------------QVSGGELQRFAIAAVFVKKA 235
Cdd:TIGR03719 393 SRDALDPN----------KTVWEEISGGLDIIKLGKREipSRayvgrfnfkgsdqqkkvgQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15231301 236 DIYMFDEPSSYLDVrQRLKAAQviRSLLRHDSYVIVVEHDLSVLD 280
Cdd:TIGR03719 463 NVLLLDEPTNDLDV-ETLRALE--EALLNFAGCAVVISHDRWFLD 504
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
218-284 |
1.08e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 218 SGGELQRFAIAAVFVKKAD---IYMFDEPSSYL---DVRQRLKaaqVIRSLLRHDSYVIVVEHDLSVL---DYLSD 284
Cdd:COG0178 828 SGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLLE---VLHRLVDKGNTVVVIEHNLDVIktaDWIID 900
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
361-546 |
1.10e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 361 DFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFpreEGVQSEIPEFNVSYKPQGNDSKRECTVRQLL-------- 432
Cdd:PRK10070 46 DASLAIEEGE-----IFVIMGLSGSGKSTMVRLLNRLI---EPTRGQVLIDGVDIAKISDAELREVRRKKIAmvfqsfal 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 433 --HDKIRDACAHPQFMS------------DVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDS 498
Cdd:PRK10070 118 mpHMTVLDNTAFGMELAginaeerrekalDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231301 499 EQRITASKVIKRFILHAKKTAFIVEHDFIMATYLADRVIVYEGQPAVK 546
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
25-72 |
1.13e-04 |
|
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.
Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 42.77 E-value: 1.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 25 CKKSCPVvktgklcievGSTSKSAF----ISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd16366 78 CLAACPT----------GAIIRTETgtvvVDPETCIGCGYCVNACPFDIPRF 119
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
18-74 |
1.19e-04 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 44.21 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 18 PKKCRQECKKSCPVVKTgKLCIEVGSTSKSAFIS-----EELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG2878 98 PEVAVVRCNGGCEKAKP-KYEYDGIKDCRAAVIGgpkgcEYGCIGCGDCIKACPFDAIVGAA 158
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
101-271 |
1.20e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.31 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-----FNTPPdwEEILTHFR---GSELQS----YFIRVVEENLktAI 168
Cdd:PRK13633 34 KKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKvyvdgLDTSD--EENLWDIRnkaGMVFQNpdnqIVATIVEEDV--AF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 169 KPQhvdyikevvrgNLGKMLEKLDERglmeeicADMELNQVLEREARQ-----VSGGELQRFAIAAVFVKKADIYMFDEP 243
Cdd:PRK13633 110 GPE-----------NLGIPPEEIRER-------VDESLKKVGMYEYRRhaphlLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180
....*....|....*....|....*...
gi 15231301 244 SSYLDVRQRLKAAQVIRSLLRHDSYVIV 271
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYGITII 199
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
218-277 |
1.34e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 44.81 E-value: 1.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 218 SGGELQRFAIAAVFVKKADIYMFDEPSSYLDVR--QRLKAAqvIRSLLRHDSyVIVVEHDLS 277
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRteRAIQAA--LREVARGRT-TLVIAHRLS 554
|
|
| FDH_b_like |
cd10562 |
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
25-72 |
1.44e-04 |
|
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.
Pssm-ID: 319884 [Multi-domain] Cd Length: 161 Bit Score: 42.68 E-value: 1.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15231301 25 CKKSCPvvkTGKLCI-EVGSTSksafISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd10562 78 CVKVCP---TGALYKtENGAVV----VDEDKCIGCGYCVAACPFDVPRY 119
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
48-70 |
1.60e-04 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 43.63 E-value: 1.60e-04
10 20
....*....|....*....|...
gi 15231301 48 AFISEELCIGCGICVKKCPFEAI 70
Cdd:PRK06991 80 AVIDEQLCIGCTLCMQACPVDAI 102
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
48-72 |
1.66e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.47 E-value: 1.66e-04
10 20
....*....|....*....|....*
gi 15231301 48 AFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1148 491 AEVDPEKCTGCGRCVEVCPYGAISI 515
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
103-281 |
1.71e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.92 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGrfntppdweEILTHFRGSELQSYFIRVVEENLKTAIKPQHVDYIKEV--V 180
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLLPDTG---------TIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIkeI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 181 RGNLG--------KMLEKLDERGLM-------------EEICADM-EL----NQVLEREARQVSGGELQRFAIAAVFVKK 234
Cdd:PRK13651 104 RRRVGvvfqfaeyQLFEQTIEKDIIfgpvsmgvskeeaKKRAAKYiELvgldESYLQRSPFELSGGQKRRVALAGILAME 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15231301 235 ADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDL-SVLDY 281
Cdd:PRK13651 184 PDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEW 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
210-286 |
1.74e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 210 LEREARQVSGGELQRFAIAAVF---VKKADIYMFDEPSSYL---DVRQRLkaaQVIRSLLRHDSYVIVVEHDLSVLDyLS 283
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhthDIKALI---YVLQSLTHQGHTVVIIEHNMHVVK-VA 878
|
...
gi 15231301 284 DFV 286
Cdd:PRK00635 879 DYV 881
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
101-277 |
1.78e-04 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 43.19 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilthfrgselqsyfIRVVEENLKT-------AIKPQHV 173
Cdd:COG4181 36 EAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-----------------------VRLAGQDLFAldedaraRLRARHV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 174 DYI------------KEVVrgnlgkM--LEKLDERGLMEEicADMELNQV-L-EREA---RQVSGGELQRFAIAAVFVKK 234
Cdd:COG4181 93 GFVfqsfqllptltaLENV------MlpLELAGRRDARAR--ARALLERVgLgHRLDhypAQLSGGEQQRVALARAFATE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15231301 235 ADIYMFDEPSSYLDVRQRLKAAQVIRSLLR-HDSYVIVVEHDLS 277
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
359-541 |
1.89e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 42.90 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 359 LGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGaFPREEGVQSEIpefnvsyKPQGND-SKRECTVRQLLhdKIR 437
Cdd:cd03217 16 LKGVNLTIKKGE-----VHALMGPNGSGKSTLAKTIMG-HPKYEVTEGEI-------LFKGEDiTDLPPEERARL--GIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 438 DACAHPQFMSDVirplQIEQLMDQVVKTLSGGEKQRVAI-TLCLGKPaDIYLIDEPSAHLDseqrITASKVIKRFI--LH 514
Cdd:cd03217 81 LAFQYPPEIPGV----KNADFLRYVNEGFSGGEKKRNEIlQLLLLEP-DLAILDEPDSGLD----IDALRLVAEVInkLR 151
|
170 180 190
....*....|....*....|....*....|
gi 15231301 515 AKKTAF-IVEHDFIMATYL-ADRV-IVYEG 541
Cdd:cd03217 152 EEGKSVlIITHYQRLLDYIkPDRVhVLYDG 181
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
102-129 |
2.17e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.54 E-value: 2.17e-04
10 20
....*....|....*....|....*...
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKP 129
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTGILVP 74
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
364-542 |
2.50e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAG---AFPReeGVQSEI-----------PEF--NVSYKPQGNDSKRECT 427
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdGFHI--GVEGVItydgitpeeikKHYrgDVVYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 428 VRQLLHDKIRdaCAHPQFMSD-VIRPLQIEQLMDQVVKTL------------------SGGEKQRVAITLCLGKPADIYL 488
Cdd:TIGR00956 155 VGETLDFAAR--CKTPQNRPDgVSREEYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 489 IDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATY-LADRVIV-YEGQ 542
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVlYEGY 288
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
466-542 |
2.59e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.91 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqriTASKVIKRFILHAKK--TAFIVEHDFIMATYLADRV-IVYEGQ 542
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDP----VGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVaFLYLGK 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
354-499 |
2.70e-04 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 42.67 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEGV-----------QSEIPEF----- 411
Cdd:COG1126 6 NLHKSFGDLEvlkgisLDVEKGE-----VVVIIGPSGSGKSTLLRCINLLEEPDSGTitvdgedltdsKKDINKLrrkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 412 ----------------NVSYKPQ--GNDSKRECTVR--QLLH-----DKirdACAHPqfmsdvirplqieqlmdqvvKTL 466
Cdd:COG1126 81 mvfqqfnlfphltvleNVTLAPIkvKKMSKAEAEERamELLErvglaDK---ADAYP--------------------AQL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 467 SGGEKQRVAI--TLCLgKPaDIYLIDEP-SAhLDSE 499
Cdd:COG1126 138 SGGQQQRVAIarALAM-EP-KVMLFDEPtSA-LDPE 170
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
102-279 |
2.74e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.30 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILagklkpnLGRFNTPPDWEEILTHFRGSELQSYfirvveeNLKTAIKPQHVDYIKEVVR 181
Cdd:cd03289 29 PGQRVGLLGRTGSGKSTLLSAF-------LRLLNTEGDIQIDGVSWNSVPLQKW-------RKAFGVIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 182 GNLG-----------KMLEKLDERGLMEEICAdmELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVr 250
Cdd:cd03289 95 KNLDpygkwsdeeiwKVAEEVGLKSVIEQFPG--QLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP- 171
|
170 180 190
....*....|....*....|....*....|..
gi 15231301 251 qrlKAAQVIRSLLRH---DSYVIVVEHDLSVL 279
Cdd:cd03289 172 ---ITYQVIRKTLKQafaDCTVILSEHRIEAM 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
379-501 |
2.76e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.23 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 379 MLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEF--NVSYKPQGNDSKRECTVRQ--LLHDKIRDACAHP--Q 444
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGdatvagksILTNISDVhqNMGYCPQFDAIDDLLTGREhlYLYARLRGVPAEEieK 2049
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 445 FMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQR 501
Cdd:TIGR01257 2050 VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
8-74 |
2.77e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 43.70 E-value: 2.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 8 IAIVSEDRCKpkKCRQeCKKSCP-----VVKTGKlcievgstsksAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG1148 490 VAEVDPEKCT--GCGR-CVEVCPygaisIDEKGV-----------AEVNPALCKGCGTCAAACPSGAISLKG 547
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
94-248 |
2.78e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.17 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 94 LHRLPIPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRfntppdweeilTHFRGSelqsyfirvveenlkTAIKPQH 172
Cdd:TIGR00957 654 LNGITFSIPeGALVAVVGQVGCGKSSLLSALLAEMDKVEGH-----------VHMKGS---------------VAYVPQQ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 173 VDYIKEVVRGNL--GKMLEKLDERGLMEE--ICADMEL------NQVLEReARQVSGGELQRFAIAAVFVKKADIYMFDE 242
Cdd:TIGR00957 708 AWIQNDSLRENIlfGKALNEKYYQQVLEAcaLLPDLEIlpsgdrTEIGEK-GVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
....*.
gi 15231301 243 PSSYLD 248
Cdd:TIGR00957 787 PLSAVD 792
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
7-86 |
2.95e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 43.97 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 7 RIAIVSEDRCK-PKKCRQ----ECKKSCPvvkTGKLcIEVGStskSAFISEELCIGCGICVKKCPFEAIQIINLP--KDL 79
Cdd:PRK12769 41 RITVIKHQQQRsAVTCHHcedaPCARSCP---NGAI-SHVDD---SIQVNQQKCIGCKSCVVACPFGTMQIVLTPvaAGK 113
|
....*..
gi 15231301 80 AKDTTHR 86
Cdd:PRK12769 114 VKATAHK 120
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
371-501 |
2.96e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 371 FTDSQII-------VMLGENGTGKTTFIR----MLAGAFPR---------------EEGVQSEIpEFNvsykpqgNDSKR 424
Cdd:cd03240 12 FHERSEIeffspltLIVGQNGAGKTTIIEalkyALTGELPPnskggahdpkliregEVRAQVKL-AFE-------NANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 425 ECTVRQLLHdkIRDACAHpqfmsdvIRPLQIEQLMDQVVKTLSGGEKQ------RVAITLCLGKPADIYLIDEPSAHLDS 498
Cdd:cd03240 84 KYTITRSLA--ILENVIF-------CHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
...
gi 15231301 499 EQR 501
Cdd:cd03240 155 ENI 157
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
466-542 |
3.01e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 42.50 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseQRiTASKVIKRF--ILHAKKTAF-IVEHDFIMATYLADRVIVYEGQ 542
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLD--AR-NADSIFQLLgeLNRLQGTAFlVVTHDLQLAKRMSRQLEMRDGR 222
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
18-85 |
4.09e-04 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 42.29 E-value: 4.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 18 PKKCRQEC------KKSCPVVktgklCIeVGSTSKSAFISEELCIGCGICVKKCPFEAIQIINLPKDLAKDTTH 85
Cdd:COG2878 132 PKGCEYGCigcgdcIKACPFD-----AI-VGAAKGMHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTVVVSSWD 199
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
465-538 |
4.23e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.43 E-value: 4.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231301 465 TLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEHDFIMATYlADRVIV 538
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIV 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
466-537 |
4.36e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.17 E-value: 4.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEqriTASKVIKrfILHAKK----TAFIVEHDFIMATYlADRVI 537
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSH---SGEEVMA--ILHQLRdrghTVIIVTHDPQVAAQ-AERVI 214
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
48-73 |
5.09e-04 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 38.42 E-value: 5.09e-04
10 20
....*....|....*....|....*.
gi 15231301 48 AFISEELCIGCGICVKKCPFEAIQII 73
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAI 26
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-538 |
5.15e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.38 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 330 TFRVSETTQENDGEVKSYARYKYpNMTKQLGDFKLEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG---VQS 406
Cdd:COG4586 10 TYRVYEKEPGLKGALKGLFRREY-REVEAVDDISFTIEPGE-----IVGFIGPNGAGKSTTIKMLTGILVPTSGevrVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 407 EIPefnvsYKpQGNDSKRECTV----R-QLLHD--------------KIRDAcAHPQFMSDVIRPLQIEQLMDQVVKTLS 467
Cdd:COG4586 84 YVP-----FK-RRKEFARRIGVvfgqRsQLWWDlpaidsfrllkaiyRIPDA-EYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 468 GGEKQR--VAITLcLGKPADIYLiDEPSAHLDseqrITASKVIKRFILHAKK----TAFIVEHDfiMA--TYLADRVIV 538
Cdd:COG4586 157 LGQRMRceLAAAL-LHRPKILFL-DEPTIGLD----VVSKEAIREFLKEYNRergtTILLTSHD--MDdiEALCDRVIV 227
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
211-275 |
6.59e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 211 EREARQVSGGELQ------RFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHD 275
Cdd:PRK03918 783 ERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
50-75 |
7.04e-04 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 40.30 E-value: 7.04e-04
10 20
....*....|....*....|....*.
gi 15231301 50 ISEELCIGCGICVKKCPFEAIQIINL 75
Cdd:cd10564 114 LDADACTGCGACVSVCPVGAITLTPL 139
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
103-281 |
7.08e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--NTPPDWEEI-LTHFRG-----SELQSYFIRVVEENLKTAIKP-QHV 173
Cdd:PTZ00265 411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIiiNDSHNLKDInLKWWRSkigvvSQDPLLFSNSIKNNIKYSLYSlKDL 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 174 DYIKE---------------------VVRGNLGKMLEKLDERGLME-----EICADMELNQVLER--------------- 212
Cdd:PTZ00265 491 EALSNyynedgndsqenknkrnscraKCAGDLNDMSNTTDSNELIEmrknyQTIKDSEVVDVSKKvlihdfvsalpdkye 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 213 -----EARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYV-IVVEHDLSVLDY 281
Cdd:PTZ00265 571 tlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRY 645
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
108-283 |
7.41e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 108 LVGTNGIGKSTALKILAGKLKPNLGR------FNTPPDWEEILTHFR---GSELQSYFIRVVEENLKTAIKpQHVDYIKE 178
Cdd:COG3593 28 LVGENNSGKSSILEALRLLLGPSSSRkfdeedFYLGDDPDLPEIEIEltfGSLLSRLLRLLLKEEDKEELE-EALEELNE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 VVRGNLGKMLEKLDER--GLMEEICADMELNQV----------------LEREARQVSGGELQRFAIAAVFV-------K 233
Cdd:COG3593 107 ELKEALKALNELLSEYlkELLDGLDLELELSLDeledllkslslriedgKELPLDRLGSGFQRLILLALLSAlaelkraP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15231301 234 KADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLS 283
Cdd:COG3593 187 ANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVP 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
102-278 |
7.49e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.40 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTP--------PDWEEIL--THFrGSELQSYFIrvveenLKTAIKPQ 171
Cdd:PRK10535 33 AGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAgqdvatldADALAQLrrEHF-GFIFQRYHL------LSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 172 HVDyIKEVVRGnlgkmLEKLDERGLMEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQ 251
Cdd:PRK10535 106 NVE-VPAVYAG-----LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180
....*....|....*....|....*..
gi 15231301 252 RLKAAQVIRSLLRHDSYVIVVEHDLSV 278
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
205-291 |
7.62e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.44 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 205 ELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKaaqvIRSL---LRHDSYVIVVEHDLSVLDY 281
Cdd:PRK14247 135 EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAK----IESLfleLKKDMTIVLVTHFPQQAAR 210
|
90
....*....|
gi 15231301 282 LSDFVCCLYG 291
Cdd:PRK14247 211 ISDYVAFLYK 220
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
20-67 |
7.95e-04 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 38.24 E-value: 7.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 20 KCRQeCKKSCPV--------VKTGKLCIEVGSTSKSAFISEEL-------CIGCGICVKKCPF 67
Cdd:pfam13484 3 SCGK-CIDACPTgaivgpegVLDARRCISYLTIEKKGLIPDELrcllgnrCYGCDICQDVCPW 64
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
3-76 |
8.08e-04 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 41.84 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 3 DRLTRIAIVSEDrcKPKKCRQECKKSCpvvkTG-KLCIEV---GSTSKS---AFISEELCIGCGICVKKCPFEAIQIINL 75
Cdd:PRK07118 191 SARVFVACNSKD--KGKAVKKVCEVGC----IGcGKCVKAcpaGAITMEnnlAVIDQEKCTSCGKCVEKCPTKAIRILNK 264
|
.
gi 15231301 76 P 76
Cdd:PRK07118 265 P 265
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-74 |
8.39e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 42.32 E-value: 8.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 2 SDRLTRIAIVSE-DRCKPKKCRQ----ECKKSCPvvkTGKLCIEvgstSKSAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:PRK12809 36 SDFRPRIHVVGKgQAANPVACHHcnnaPCVTACP---VNALTFQ----SDSVQLDEQKCIGCKRCAIACPFGVVEMVD 106
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
46-70 |
8.46e-04 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 40.70 E-value: 8.46e-04
10 20
....*....|....*....|....*
gi 15231301 46 KSAFISEELCIGCGICVKKCPFEAI 70
Cdd:PRK05113 107 KVAFIDEDNCIGCTKCIQACPVDAI 131
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
461-537 |
9.33e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 461 QVVKTLSGGEKQRVAITLCLGKPAD---IYLIDEPSA--HLDSEQRITAskVIKRfILHAKKTAFIVEHDF-IMATylAD 534
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTglHFHDVKKLLE--VLQR-LVDKGNTVVVIEHNLdVIKC--AD 239
|
...
gi 15231301 535 RVI 537
Cdd:cd03271 240 WII 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
217-282 |
9.54e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 9.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 217 VSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQrlkAAQV----IRSLLRHDSYVIVVE--HDLSVLDYL 282
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV---GRQVfdkcIKDELRGKTRVLVTNqlHFLSQVDRI 809
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
25-74 |
9.83e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 42.29 E-value: 9.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15231301 25 CKKSCPVVktgklCIEVGSTSKSAFISEELCIGCGICVKKCPfeAIQIIN 74
Cdd:PRK13795 589 CVGACPTG-----AIRIEEGKRKISVDEEKCIHCGKCTEVCP--VVKYKD 631
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
466-539 |
1.01e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqriTASKVIKRFI--LHAKKTAFIVEHDFIMATYLADRVIVY 539
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP----TTTEKIEEFIrsLADRLTVIIVTHNLAQAARISDRAALF 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
451-501 |
1.06e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.93 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 451 RPLQIEQLMDQV---------VKTLSGGEKQRVAI--TLcLGKPADIyLIDEPSAHLDSEQR 501
Cdd:COG4136 110 RRARVEQALEEAglagfadrdPATLSGGQRARVALlrAL-LAEPRAL-LLDEPFSKLDAALR 169
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
50-70 |
1.06e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 36.44 E-value: 1.06e-03
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-542 |
1.06e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 41.19 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 454 QIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqrITASKVIKRFILHAKK--TAFIVEHDFIMATY 531
Cdd:PRK14246 142 EVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID----IVNSQAIEKLITELKNeiAIVIVSHNPQQVAR 217
|
90
....*....|..
gi 15231301 532 LADRV-IVYEGQ 542
Cdd:PRK14246 218 VADYVaFLYNGE 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
99-277 |
1.09e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 99 IPrPGQVLGLVGTNGIGKSTALKILAgklkpnlgRFnTPPDWEEILthFRGSELQSYFIRVVEENLktAIKPQHVDYIKE 178
Cdd:PRK11176 366 IP-AGKTVALVGRSGSGKSTIANLLT--------RF-YDIDEGEIL--LDGHDLRDYTLASLRNQV--ALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 179 VVRGNLGKMLEKLDERglmEEI--CADME------------LNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:PRK11176 432 TIANNIAYARTEQYSR---EQIeeAARMAyamdfinkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190
....*....|....*....|....*....|...
gi 15231301 245 SYLDVRQRlKAAQVIRSLLRHDSYVIVVEHDLS 277
Cdd:PRK11176 509 SALDTESE-RAIQAALDELQKNRTSLVIAHRLS 540
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
103-276 |
1.17e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.03 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFNTPPDWEEILT-HFRG-------SELQSYFIRV-VEENLKTAIKpqhv 173
Cdd:PRK10895 29 GEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARArrgigylPQEASIFRRLsVYDNLMAVLQ---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 174 dyikevVRGNLGKmlEKLDERGlmEEICADMELNQVLEREARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRL 253
Cdd:PRK10895 105 ------IRDDLSA--EQREDRA--NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180
....*....|....*....|...
gi 15231301 254 KAAQVIRSLLRHDSYVIVVEHDL 276
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNV 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
101-280 |
1.31e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 41.75 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAG------KLKPN---LGRFNtPPDWEEIL-------THFRGSelqsyfIRvveENL 164
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGflpyqgSLKINgieLRELD-PESWRKHLswvgqnpQLPHGT------LR---DNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 165 ---KTAIKPQHVD------YIKEVVrgnlgKMLEKlderGLMEEICadmelnqvlEREARqVSGGELQRFAIAAVFVKKA 235
Cdd:PRK11174 444 llgNPDASDEQLQqalenaWVSEFL-----PLLPQ----GLDTPIG---------DQAAG-LSVGQAQRLALARALLQPC 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15231301 236 DIYMFDEPSSYLDVRQrlkAAQVIRSLLR--HDSYVIVVEHDLSVLD 280
Cdd:PRK11174 505 QLLLLDEPTASLDAHS---EQLVMQALNAasRRQTTLMVTHQLEDLA 548
|
|
| IOR_alpha |
TIGR03336 |
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ... |
10-70 |
1.42e-03 |
|
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.
Pssm-ID: 274526 [Multi-domain] Cd Length: 595 Bit Score: 41.63 E-value: 1.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 10 IVSEDRCKpkKCRQeCKKS--CPVVKTGKLCIEVGStsksafiseeLCIGCGICVKKCPFEAI 70
Cdd:TIGR03336 546 KVDQDKCI--GCKK-CIKElgCPAIEPEDKEAVIDP----------LCTGCGVCAQICPFDAI 595
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
456-538 |
1.54e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.77 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 456 EQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfiLHAKK--TAFIVEHDFIMATYLA 533
Cdd:PRK13634 136 EELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK--LHKEKglTTVLVTHSMEDAARYA 213
|
....*
gi 15231301 534 DRVIV 538
Cdd:PRK13634 214 DQIVV 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
102-281 |
1.71e-03 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 40.09 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 102 PGQVLGLVGTNGIGKSTAlkILAgklkpnLGRFNtppDWEEILTHFRGSELQSYFIRVVEENLktAIKPQHVDYIKEVVR 181
Cdd:cd03369 33 AGEKIGIVGRTGAGKSTL--ILA------LFRFL---EAEEGKIEIDGIDISTIPLEDLRSSL--TIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 182 GNLGKMLEKLDErglmeEICADMELNQvlerEARQVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRS 261
Cdd:cd03369 100 SNLDPFDEYSDE-----EIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE 170
|
170 180
....*....|....*....|.
gi 15231301 262 LLRhDSYVIVVEHDL-SVLDY 281
Cdd:cd03369 171 EFT-NSTILTIAHRLrTIIDY 190
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-497 |
1.96e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 40.48 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 354 NMTKQLGDFK------LEVMEGEftdsqIIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEfNVSYKPQ- 418
Cdd:COG4152 6 GLTKRFGDKTavddvsFTVPKGE-----IFGLLGPNGAGKTTTIRIILGILAPDSGevlwdgepLDPEDRR-RIGYLPEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 419 -GNDSKRecTVR-QL-----LHDKIRDAcAHPQfMSDVIRPLQIEQLMDQVVKTLSGGEKQRV--AITLcLGKPaDIYLI 489
Cdd:COG4152 80 rGLYPKM--KVGeQLvylarLKGLSKAE-AKRR-ADEWLERLGLGDRANKKVEELSKGNQQKVqlIAAL-LHDP-ELLIL 153
|
....*...
gi 15231301 490 DEPSAHLD 497
Cdd:COG4152 154 DEPFSGLD 161
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
50-70 |
2.21e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 36.38 E-value: 2.21e-03
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
376-541 |
2.29e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 40.25 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 376 IIVMLGENGTGKTTFIRMLAGAFPREEG--------VQSEIPEFNVSYKPQGNDSKRECTVrqLLHDKI----------- 436
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLASGkisilgqpTRQALQKNLVAYVPQSEEVDWSFPV--LVEDVVmmgryghmgwl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 437 RDACAHP-QFMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLD--SEQRITAskvIKRFIL 513
Cdd:PRK15056 113 RRAKKRDrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvkTEARIIS---LLRELR 189
|
170 180
....*....|....*....|....*...
gi 15231301 514 HAKKTAFIVEHDFIMATYLADRVIVYEG 541
Cdd:PRK15056 190 DEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
210-275 |
2.47e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 210 LEREARQVSGGELQRFAIAAVFvkKADI----YMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHD 275
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHL--GAELigitYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
101-127 |
2.58e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.20 E-value: 2.58e-03
10 20
....*....|....*....|....*..
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKL 127
Cdd:PRK13547 25 EPGRVTALLGRNGAGKSTLLKALAGDL 51
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
4-73 |
2.67e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319889 [Multi-domain] Cd Length: 138 Bit Score: 38.44 E-value: 2.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 4 RLTRIAIVSEDRCKPKKCRQ----ECKKSCPV-----VKTGKLCIEvgstsksafiseELCIGCGICVKKCPFEAIQII 73
Cdd:cd16367 40 RLDRNGLRFGNLLVPTACRHcvdpVCMIGCPTgaihrDDGGEVVIS------------DACCGCGNCASACPYGAIQMV 106
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
456-546 |
2.75e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.11 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 456 EQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfiLHAK-KTAFIVEHdfIM---ATY 531
Cdd:PRK13649 136 ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK--LHQSgMTIVLVTH--LMddvANY 211
|
90
....*....|....*
gi 15231301 532 lADRVIVYEGQPAVK 546
Cdd:PRK13649 212 -ADFVYVLEKGKLVL 225
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
18-66 |
2.78e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 36.46 E-value: 2.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15231301 18 PKKCRQ--ECKKSCPVVKTGKLCIEVGSTSKSAFISEELCIGCGICVKKCP 66
Cdd:pfam13237 6 PDKCIGcgRCTAACPAGLTRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
466-522 |
2.87e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.37 E-value: 2.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 466 LSGGEKQRVAITLCLG----KPADIYLIDEPSAHLDSE--QRItaSKVIKRFilhAKKTAFIV 522
Cdd:cd03278 114 LSGGEKALTALALLFAifrvRPSPFCVLDEVDAALDDAnvERF--ARLLKEF---SKETQFIV 171
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
103-244 |
2.90e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 39.86 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF----NTPPDW-------EEILTHFRGSELqsyFIRV-VEENLKT---- 166
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgKDITDWqtakimrEAVAIVPEGRRV---FSRMtVEENLAMggff 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 167 AIKPQHVDYIKEVVrgnlgKMLEKLDERGLmeeicadmelnqvleREARQVSGGELQRFAIAAVFVKKADIYMFDEPS 244
Cdd:PRK11614 108 AERDQFQERIKWVY-----ELFPRLHERRI---------------QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
101-290 |
2.94e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 101 RPGQVLGLVGTNGIGKSTALKILAGKlkpnlgrfntpPDWE----EILthFRGSELQSY-------------FIRVVE-- 161
Cdd:PRK09580 25 RPGEVHAIMGPNGSGKSTLSATLAGR-----------EDYEvtggTVE--FKGKDLLELspedragegifmaFQYPVEip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 162 --EN---LKTAIKpqhvdyikeVVRGNLGKM-LEKLDERGLMEEICADMELNQVLEREARQV--SGGELQRFAIAAVFVK 233
Cdd:PRK09580 92 gvSNqffLQTALN---------AVRSYRGQEpLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 234 KADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLS-DFVCCLY 290
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
103-281 |
2.97e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 40.00 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 103 GQVLGLVGTNGIGKSTALKILAGKLKPNlgrfNTPPDWEEILTH-----------FRGSELQSYFI----------RVVE 161
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLITGD----KSAGSHIELLGRtvqregrlardIRKSRANTGYIfqqfnlvnrlSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 162 ENLKTAI--KPQHVDYIKEVVRGNLGKMLEKLDERGLMeeicadmelnQVLEREARQVSGGELQRFAIAAVFVKKADIYM 239
Cdd:PRK09984 106 NVLIGALgsTPFWRTCFSWFTREQKQRALQALTRVGMV----------HFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15231301 240 FDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEhdLSVLDY 281
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVT--LHQVDY 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
353-556 |
3.09e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 39.15 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 353 PNMTKQLgdfkLEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGafpREEG--VQSEI--------PEFN--VSYKPQgN 420
Cdd:cd03232 16 KGGKRQL----LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG---RKTAgvITGEIlingrpldKNFQrsTGYVEQ-Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 421 DSKREC-TVRQLLhdkirdacahpQFmSDVIRPLQIEQlmdqvvktlsggeKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:cd03232 88 DVHSPNlTVREAL-----------RF-SALLRGLSVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 500 qritASKVIKRFIlhaKKtafivehdfimatyLADrvivyEGQpAVKCIAHSPQSLL 556
Cdd:cd03232 143 ----AAYNIVRFL---KK--------------LAD-----SGQ-AILCTIHQPSASI 172
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
54-74 |
3.19e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 40.36 E-value: 3.19e-03
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
91-286 |
3.23e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 91 GFKLHRLPIpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FNTppdwEEILTHFRGSELQSYFIRVVEENLKTAI 168
Cdd:PRK15439 278 GFRNISLEV-RAGEILGLAGVVGAGRTELAETLYGLRPARGGRimLNG----KEINALSTAQRLARGLVYLPEDRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 169 kpqHVDY-----IKEVVRGNLGKMLEKLDERGLMEEICADM--ELNQvLEREARQVSGGELQRFAIAAVFVKKADIYMFD 241
Cdd:PRK15439 353 ---YLDAplawnVCALTHNRRGFWIKPARENAVLERYRRALniKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15231301 242 EPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLDYLSDFV 286
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
5-73 |
3.24e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 38.09 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 5 LTRIAIV-SEDRCKPKKCRQ--ECKKSCPVV-----KTG------KLCIEVGST-----SKSAFISEEL-----CIGCGI 60
Cdd:cd16372 32 KSCIRITeTEGGYAINVCNQcgECIDVCPTGaitrdANGvvminkKLCVGCLMCvgfcpEGAMFKHEDYpepfkCIACGI 111
|
90
....*....|...
gi 15231301 61 CVKKCPFEAIQII 73
Cdd:cd16372 112 CVKACPTGALELV 124
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
350-541 |
3.33e-03 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 39.38 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 350 YKYPNM--TKQLGDFKLEVMEGEFTdsqiiVMLGENGTGKTTFIRMLAGAFPREEG-----------------------V 404
Cdd:cd03248 19 FAYPTRpdTLVLQDVSFTLHPGEVT-----ALVGPSGSGKSTVVALLENFYQPQGGqvlldgkpisqyehkylhskvslV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 405 QSEIPEF------NVSYKPQGNDSKRECTVRQLLHdkirdacAHpQFMSDVirPLQIEQLMDQVVKTLSGGEKQRVAITL 478
Cdd:cd03248 94 GQEPVLFarslqdNIAYGLQSCSFECVKEAAQKAH-------AH-SFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 479 CLGKPADIYLIDEPSAHLDSEQRITASKVIKRFilHAKKTAFIVEHDfIMATYLADRVIVYEG 541
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDW--PERRTVLVIAHR-LSTVERADQILVLDG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
374-542 |
3.59e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 39.38 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 374 SQIIVMLGENGTGKTTFIRMLAGAfprEEGVQSEIPEFNVSYKPQGNDSKRECTVRQ----------------------- 430
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGL---DDGSSGEVSLVGQPLHQMDEEARAKLRAKHvgfvfqsfmliptlnalenvelp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 431 -LLHDKiRDACAHPQfMSDVIRPLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDseqRITASKVIK 509
Cdd:PRK10584 113 aLLRGE-SSRQSRNG-AKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD---RQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 15231301 510 -RFIL---HAkKTAFIVEHDFIMATYLADRVIVYEGQ 542
Cdd:PRK10584 188 lLFSLnreHG-TTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
218-284 |
3.88e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 3.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 218 SGGELQRFAIAAVFVKKAD---IYMFDEPSSYL---DVRQRLKaaqVIRSLLRHDSYVIVVEHDLSVL---DYLSD 284
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIRKLLE---VLHRLVDKGNTVVVIEHNLDVIktaDWIID 904
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
465-534 |
3.88e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 3.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 465 TLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRfiLHAKKTAFIVEHDFIMATYLAD 534
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE--LKEQYTIIIVTHNMQQAARVSD 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
465-499 |
4.30e-03 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 39.06 E-value: 4.30e-03
10 20 30
....*....|....*....|....*....|....*
gi 15231301 465 TLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSE 499
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
42-75 |
4.71e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 38.01 E-value: 4.71e-03
10 20 30
....*....|....*....|....*....|....
gi 15231301 42 GSTSKSAFISeeLCIGCGICVKKCPFEAIQIINL 75
Cdd:cd16373 5 GALDEEEFLA--LCIRCGLCVEACPTGVIQPAGL 36
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
452-524 |
4.77e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 452 PLQIEQLMDQVVKTLSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSEQRITASKVIKRFILHAKKTAFIVEH 524
Cdd:PTZ00265 566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
216-284 |
4.89e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.31 E-value: 4.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231301 216 QVSGGELQRFAIAAVFVKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSyVIVVEHDLSVLDYLSD 284
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISD 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
379-524 |
5.01e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 379 MLGENGTGKTTFIRMLA----GAFPR---------------------------------EEGV-----QSEIPEFNVSYK 416
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAmhaiDGIPKncqilhveqevvgddttalqcvlntdiertqllEEEAqlvaqQRELEFETETGK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 417 PQG--NDSKRECTVRQLLHDKIR-----DACAHPQFMSDVIRPLQIEQLMD-QVVKTLSGGEKQRVAITLCLGKPADIYL 488
Cdd:PLN03073 288 GKGanKDGVDKDAVSQRLEEIYKrleliDAYTAEARAASILAGLSFTPEMQvKATKTFSGGWRMRIALARALFIEPDLLL 367
|
170 180 190
....*....|....*....|....*....|....*.
gi 15231301 489 IDEPSAHLDseqrITASKVIKRFILHAKKTAFIVEH 524
Cdd:PLN03073 368 LDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
461-522 |
5.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 461 QVVKTLSGGEKQRVAITLCLG----KPADIYLIDEPSAHLDSeqrITASKVIKRFILHAKKTAFIV 522
Cdd:TIGR02169 1070 QRLEAMSGGEKSLTALSFIFAiqryKPSPFYAFDEVDMFLDG---VNVERVAKLIREKAGEAQFIV 1132
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
466-524 |
5.18e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 39.07 E-value: 5.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231301 466 LSGGEKQRVAITLCLGKPADIYLIDEPSAHLDSeqrITaSKVIKRFILHAKKTAFIV--EH 524
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP---IT-YQVIRKTLKQAFADCTVIlsEH 195
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
44-70 |
5.73e-03 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 38.91 E-value: 5.73e-03
10 20
....*....|....*....|....*..
gi 15231301 44 TSKSAFISEELCIGCGICVKKCPFEAI 70
Cdd:cd03110 55 GGKKAFIDQEKCIRCGNCERVCKFGAI 81
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
176-295 |
5.83e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 176 IKEVVRGNLGKMLE-----KLDERG------LMEEICADME-LNQV------LEREARQVSGGELQRFAIAA------VF 231
Cdd:COG0178 427 IAELTALSIDEALEffenlELTEREaeiaerILKEIRSRLGfLVDVgldyltLDRSAGTLSGGEAQRIRLATqigsglVG 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 232 VkkadIYMFDEPSSYLDVR--QRLkaaqvIRSL--LR-HDSYVIVVEHDLSVL---DYLSDFvcclyGkPGA 295
Cdd:COG0178 507 V----LYVLDEPSIGLHQRdnDRL-----IETLkrLRdLGNTVIVVEHDEDTIraaDYIIDI-----G-PGA 563
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
81-133 |
6.19e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 6.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15231301 81 KDTTHRYGANGFKLH--RLPIPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGR 133
Cdd:PRK10522 326 RNVTFAYQDNGFSVGpiNLTIKR-GELLFLIGGNGSGKSTLAMLLTGLYQPQSGE 379
|
|
| DMSOR_beta_like |
cd16374 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
18-72 |
6.31e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319896 [Multi-domain] Cd Length: 139 Bit Score: 37.25 E-value: 6.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231301 18 PKKCRQeCKKSCpvvktgklCIEV---GSTSKSA----FISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd16374 40 PVRCRH-CEDAP--------CMEVcptGAIYRDEdgavLVDPDKCIGCGMCAMACPFGVPRF 92
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
364-509 |
6.39e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 364 LEVMEGEFTDSQIIVMLGENGTGKTTFIRMLAGAF---------------PREEGVQSEIpefnvSYKPQGNDSKRECTV 428
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgvitggdrlvngrPLDSSFQRSI-----GYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 429 RQLLhdKIRDACAHPQFMSD---------VIRPLQIEQLMDQVVKT----LSGGEKQRVAITLCL-GKPADIYLIDEPSA 494
Cdd:TIGR00956 854 RESL--RFSAYLRQPKSVSKsekmeyveeVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELvAKPKLLLFLDEPTS 931
|
170
....*....|....*
gi 15231301 495 HLDSEqriTASKVIK 509
Cdd:TIGR00956 932 GLDSQ---TAWSICK 943
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
211-280 |
7.59e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 7.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231301 211 EREARQVSGGELQRFAIAAVF---VKKADIYMFDEPSSYLDVRQRLKAAQVIRSLLRHDSYVIVVEHDLSVLD 280
Cdd:pfam13304 231 ELPAFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
464-558 |
7.66e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231301 464 KTLSGGEKQRVAITLCLGkp--adIYLIDEPSA--HldseQRITAsKVIKrfILHAKK----TAFIVEHD--FIMAtylA 533
Cdd:COG0178 484 GTLSGGEAQRIRLATQIGsglvgvLYVLDEPSIglH----QRDND-RLIE--TLKRLRdlgnTVIVVEHDedTIRA---A 553
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15231301 534 DRVI-------------VYEGQPAVkcIAHSPQSL----LSG 558
Cdd:COG0178 554 DYIIdigpgagehggevVAQGTPEE--ILKNPDSLtgqyLSG 593
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
461-522 |
7.87e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 37.67 E-value: 7.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231301 461 QVVKTLSGGEKQRVAITLCLG----KPADIYLIDEPSAHLDSEQRITASKVIKRfilHAKKTA-FIV 522
Cdd:cd03239 90 KVEQILSGGEKSLSALALIFAlqeiKPSPFYVLDEIDAALDPTNRRRVSDMIKE---MAKHTSqFIV 153
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
1-72 |
8.33e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 38.51 E-value: 8.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231301 1 MSD-RLTRIAIVSEDrCKpkKCRQeCKKSCPV---VKTGKLcievgstsksafISEElCIGCGICVKKCPFEAIQI 72
Cdd:COG0348 197 LSDlSTLRVRYDRGD-CI--DCGL-CVKVCPMgidIRKGEI------------NQSE-CINCGRCIDACPKDAIRF 255
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
9-66 |
8.43e-03 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 34.95 E-value: 8.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15231301 9 AIVSEDRCKpkKCRQeCKKSCPVvkTGKLCIeVGSTSKSAFISEELCIGCGICVKKCP 66
Cdd:pfam14697 1 ARIDEDTCI--GCGK-CYIACPD--TSHQAI-VGDGKRHHTVIEDECTGCNLCVSVCP 52
|
|
| PhsB_like |
cd10553 |
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ... |
24-71 |
8.58e-03 |
|
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319875 [Multi-domain] Cd Length: 146 Bit Score: 36.96 E-value: 8.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15231301 24 ECKKSCPvvkTGKLcievgsTSKSA----FISEELCIGCGICVKKCPFEAIQ 71
Cdd:cd10553 65 WCVKACP---TGAM------QKREKdgivYVDQELCIGCKACIEACPWGIPQ 107
|
|
| |
