|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-205 |
4.54e-101 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 290.55 E-value: 4.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIG 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQhWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTA 160
Cdd:PRK13538 81 HQPGIKTELTALENLR-FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2030133830 161 LDKKGVAMLQTQFQSHLDKGGAILLTTHQDLTAHFAQLQTLALEY 205
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-204 |
1.76e-92 |
|
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: 268.96 E-value: 1.76e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTA 160
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2030133830 161 LDKKGVAMLQTQFQSHLDKGGAILLTTHQDLTAHFAqlQTLALE 204
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA--RVLDLG 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-191 |
1.99e-71 |
|
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: 215.30 E-value: 1.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGH 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENVQHWLMVHGAQadEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGA--QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190
....*....|....*....|....*....|
gi 2030133830 162 DKKGVAMLQTQFQSHLDKGGAILLTTHQDL 191
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-191 |
2.78e-70 |
|
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: 212.74 E-value: 2.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGH 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENVQHWLMVHGaqadEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS----DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190
....*....|....*....|....*....|
gi 2030133830 162 DKKGVAMLQTQFQSHLDKGGAILLTTHQDL 191
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDL 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
1.97e-60 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 187.77 E-value: 1.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrdDYDSFAADLLFIG 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQHWLMVHGAqaDEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTA 160
Cdd:PRK13539 80 HRNAMKPALTVAENLEFWAAFLGG--EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 161 LDKKGVAMLQTQFQSHLDKGGAILLTTHQDL 191
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATHIPL 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-207 |
1.17e-49 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 160.12 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQHWLMVHGAQADEEEVYTLLaKLGliGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTA 160
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPGAVGITELCRLF-SLE--HLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2030133830 161 LDKKGVAMLQTQFQSHLDKGGAILLTTHQDLTAHFAQLQtlalEYRL 207
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYE----EYHL 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-188 |
4.36e-44 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 146.15 E-value: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-RDDYDSFAAdllFI 79
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtRGDRSRFMA---YL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTGVNQQLSAYENVQHWLMVHGAQAdEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFT 159
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLCGLHGRRA-KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180
....*....|....*....|....*....
gi 2030133830 160 ALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-189 |
1.41e-41 |
|
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: 140.76 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGlfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 159 TALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHI 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-188 |
6.63e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.96 E-value: 6.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGH 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFT 159
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGlpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180
....*....|....*....|....*....
gi 2030133830 160 ALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-159 |
9.29e-38 |
|
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: 128.15 E-value: 9.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 17 FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-RDDYDSFAADLLFIGHKTGVNQQLSAYENV 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 96 QHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVR----TLSAGQQRRVALVRLWLNQAKLWVLDEPFT 159
Cdd:pfam00005 81 RLGLLLKGlsKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-191 |
1.26e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYD-------SFA 73
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigyvpqRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 74 ADLLFighktgvnqQLSAYENV------QHWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLN 147
Cdd:COG1121 86 VDWDF---------PITVRDVVlmgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2030133830 148 QAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHqDL 191
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTH-DL 199
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-188 |
4.04e-33 |
|
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: 116.73 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGH 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENVQhwlmvhgaqadeeevytllaklgligledvpvrtLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:cd03230 81 EPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180
....*....|....*....|....*..
gi 2030133830 162 DKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSH 153
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-164 |
3.70e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.35 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-------RD------ 67
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRNvgmvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 68 DYDsfaadlLFiGHktgvnqqLSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLW 145
Cdd:COG3842 85 DYA------LF-PH-------LTVAENVAFGLRMRGVPKAEirARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170
....*....|....*....
gi 2030133830 146 LNQAKLWVLDEPFTALDKK 164
Cdd:COG3842 151 APEPRVLLLDEPLSALDAK 169
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-196 |
3.84e-30 |
|
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: 110.27 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADllFIGHKTG-VNQQ------LSAYE 93
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAA--FRRRHIGfVFQSfnllpdLTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 NVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK-GVAMLQ 170
Cdd:cd03255 102 NVELPLLLAGVPKKErrERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSEtGKEVME 181
|
170 180
....*....|....*....|....*.
gi 2030133830 171 TQFQSHLDKGGAILLTTHQDLTAHFA 196
Cdd:cd03255 182 LLRELNKEAGTTIVVVTHDPELAEYA 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-196 |
8.15e-30 |
|
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: 110.52 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRdDYDS--FAADLLF 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRreLARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHKTGVNQQLSAYENV-------QHWLMVHGAQaDEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKL 151
Cdd:COG1120 80 VPQEPPAPFGLTVRELValgryphLGLFGRPSAE-DREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2030133830 152 WVLDEPFTALD-KKGVAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFA 196
Cdd:COG1120 159 LLLDEPTSHLDlAHQLEVLELLRRLARERGRTVVMVLHDlNLAARYA 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-190 |
2.48e-29 |
|
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: 108.38 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDD----------YDS 71
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVpperrnigmvFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 FAadlLFighktgvnQQLSAYENVQHWLMVHGAQADEEE--VYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQA 149
Cdd:cd03259 81 YA---LF--------PHLTVAENIAFGLKLRGVPKAEIRarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2030133830 150 KLWVLDEPFTALDKKGVAMLQTQFQSHLDKGG--AILLTTHQD 190
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGitTIYVTHDQE 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-189 |
1.49e-28 |
|
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: 106.21 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIR-DDYDSFAadllFIG 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIG----YLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEarRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 159 TALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-188 |
2.03e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.10 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCT----KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsfaadl 76
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 lfIGHKTG-VNQQ------LSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLN 147
Cdd:COG1116 78 --PGPDRGvVFQEpallpwLTVLDNVALGLELRGVPKAErrERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2030133830 148 QAKLWVLDEPFTALDkkgvAM----LQTQFQSHLDKGG-AILLTTH 188
Cdd:COG1116 156 DPEVLLMDEPFGALD----ALtrerLQDELLRLWQETGkTVLFVTH 197
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-204 |
2.62e-28 |
|
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: 103.86 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 3 EIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRddydsfaadllfighk 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 83 tgvnqQLSAYENVQHWLMVHGaqadeeevytllaklgligledvpvrtLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd00267 65 -----KLPLEELRRRIGYVPQ---------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2030133830 163 KKGVAMLQTQFQSHLDKGGAILLTTHQDLTAHFAQLQTLALE 204
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-204 |
3.93e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 104.57 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFaadLLFIG 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQHWLMVHGAQadeEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTA 160
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNSA---ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2030133830 161 LDKKGVAMLQTQFQSHLDKGGAILLTTHQDltAHFAQLQTLALE 204
Cdd:PRK13541 154 LSKENRDLLNNLIVMKANSGGIVLLSSHLE--SSIKSAQILQLD 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-189 |
8.76e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.35 E-value: 8.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfaaDLLFIG 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE------DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 H---KTGVNQQLSAYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLD 155
Cdd:COG4152 75 YlpeERGLYPKMKVGEQLVYLARLKGlsKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190
....*....|....*....|....*....|....
gi 2030133830 156 EPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-197 |
1.10e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.36 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCT----KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADL 76
Cdd:COG1136 4 LLELRNLTKSygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 LfiGHKTG-VNQQ------LSAYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLN 147
Cdd:COG1136 84 R--RRHIGfVFQFfnllpeLTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 148 QAKLWVLDEPFTALDKK-GVAMLQTQFQSHLDKGGAILLTTHQDLTAHFAQ 197
Cdd:COG1136 162 RPKLILADEPTGNLDSKtGEEVLELLRELNRELGTTIVMVTHDPELAARAD 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-196 |
1.37e-27 |
|
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: 103.95 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCT-KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsfaADLLFIG 80
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK------KNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGV-----NQQL---SAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAK 150
Cdd:COG1122 75 RKVGLvfqnpDDQLfapTVEEDVAFGPENLGLPREEirERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2030133830 151 LWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFA 196
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELA 201
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-188 |
1.84e-27 |
|
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: 103.71 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 17 FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsfaadllfIGHKTGVNQQ-------L 89
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----------PGPDRGYVFQqdallpwL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 SAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkkgvA 167
Cdd:cd03293 89 TVLDNVALGLELQGVPKAEarERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALD----A 164
|
170 180
....*....|....*....|....*.
gi 2030133830 168 MLQTQFQSHL-----DKGGAILLTTH 188
Cdd:cd03293 165 LTREQLQEELldiwrETGKTVLLVTH 190
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-195 |
2.60e-27 |
|
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: 103.00 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAadllFIGHKTGVNQQ--LSAYENV-- 95
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIG----YVPQRRSIDRDfpISVRDVVlm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 96 ---QHWLMVHGA-QADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQT 171
Cdd:cd03235 94 glyGHKGLFRRLsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYE 173
|
170 180
....*....|....*....|....*..
gi 2030133830 172 QFQSHLDKGGAILLTTHqDL---TAHF 195
Cdd:cd03235 174 LLRELRREGMTILVVTH-DLglvLEYF 199
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-196 |
3.79e-27 |
|
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: 101.74 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 3 EIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddydsfaadllfighk 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 83 tgvnQQLSAYENVQHWLMVhgAQAdeeevytlLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03214 64 ----ASLSPKELARKIAYV--PQA--------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190
....*....|....*....|....*....|....*.
gi 2030133830 163 -KKGVAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFA 196
Cdd:cd03214 130 iAHQIELLELLRRLARERGKTVVMVLHDlNLAARYA 165
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-196 |
5.76e-27 |
|
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: 102.16 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 3 EIDAVTCT--KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfaaDLLFIG 80
Cdd:cd03225 1 ELKNLSFSypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL------SLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGV-----NQQLS----------AYENvqhwLMVHGAQAdEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLW 145
Cdd:cd03225 75 RKVGLvfqnpDDQFFgptveeevafGLEN----LGLPEEEI-EERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2030133830 146 LNQAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFA 196
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELA 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-188 |
1.15e-26 |
|
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: 101.29 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCL----FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADL 76
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 LFIGHKTGVNQQLSAYENVQHWLMVHGAQADEEE--VYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 2030133830 155 DEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTH 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-189 |
1.74e-26 |
|
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: 100.75 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDsfaaDLLFIG- 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE----ALRRIGa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 --HKTGVNQQLSAYENvqhwLMVHGAQAD--EEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDE 156
Cdd:cd03268 77 liEAPGFYPNLTAREN----LRLLARLLGirKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190
....*....|....*....|....*....|...
gi 2030133830 157 PFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-197 |
3.40e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.90 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCT-KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYdsfAADLLFI 79
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR---GRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTG-VNQQ------LSAYENVQH--------WLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALV 142
Cdd:COG3638 79 RRRIGmIFQQfnlvprLSVLTNVLAgrlgrtstWRSLLGlfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2030133830 143 RLWLNQAKLWVLDEPFTALD-KKGVAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFAQ 197
Cdd:COG3638 159 RALVQEPKLILADEPVASLDpKTARQVMDLLRRIAREDGITVVVNLHQvDLARRYAD 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-202 |
3.20e-25 |
|
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: 97.65 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGqIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGH 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENVQH--WLM-VHGAQADeEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:cd03264 80 EFGVYPNFTVREFLDYiaWLKgIPSKEVK-ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2030133830 159 TALDKKGvamlQTQFQSHLDKGGA---ILLTTHQ--DLTAHFAQLQTLA 202
Cdd:cd03264 159 AGLDPEE----RIRFRNLLSELGEdriVILSTHIveDVESLCNQVAVLN 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-163 |
3.80e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.17 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARAD---EGQIRYNSTDIrDDYDS------ 71
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL-TALPAeqrrig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 --FAADLLFighktgvnQQLSAYENVQHWL--MVHGAQADEEeVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLN 147
Cdd:COG4136 80 ilFQDDLLF--------PHLSVGENLAFALppTIGRAQRRAR-VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170
....*....|....*.
gi 2030133830 148 QAKLWVLDEPFTALDK 163
Cdd:COG4136 151 EPRALLLDEPFSKLDA 166
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-188 |
4.12e-25 |
|
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: 97.69 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddydsfaADLLfiGH 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--------TNLP--PH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQ---------QLSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAK 150
Cdd:cd03300 71 KRPVNTvfqnyalfpHLTVFENIAFGLRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2030133830 151 LWVLDEPFTALDKKgvamLQTQFQSHLDK-----GGAILLTTH 188
Cdd:cd03300 151 VLLLDEPLGALDLK----LRKDMQLELKRlqkelGITFVFVTH 189
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-158 |
8.73e-25 |
|
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: 96.74 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDSFAADLLFIGHK---TGVNQQLSAYEN 94
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPHEIARLGIGRTfqiPRLFPELTVLEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 95 VQ------------HWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:cd03219 96 VMvaaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-204 |
6.49e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 94.35 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCT-KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIR---YNSTDIRDDydsfaaDL 76
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngQDLSRLKRR------EI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 LFIGHKTGV---NQQL----SAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLN 147
Cdd:COG2884 75 PYLRRRIGVvfqDFRLlpdrTVYENVALPLRVTGKSRKEirRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 148 QAKLWVLDEPFTALDKK---GVAMLQTQFQshlDKGGAILLTTH-QDLTAHFAQlQTLALE 204
Cdd:COG2884 155 RPELLLADEPTGNLDPEtswEIMELLEEIN---RRGTTVLIATHdLELVDRMPK-RVLELE 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-189 |
7.38e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.44 E-value: 7.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLfdSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDS-------FA 73
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvsmlFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 74 ADLLFiGHktgvnqqLSAYENVQhwLMVHGA----QADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQA 149
Cdd:COG3840 79 ENNLF-PH-------LTVAQNIG--LGLRPGlkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2030133830 150 KLWVLDEPFTALD---KKGvaMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:COG3840 149 PILLLDEPFSALDpalRQE--MLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-188 |
3.35e-23 |
|
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: 92.61 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDSFAADLLFIGH---KTGVNQQLS 90
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARLGIGYlpqEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:cd03218 92 VEENILAVLEIRGLSKKEreEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQD 171
|
170 180
....*....|....*....|
gi 2030133830 169 LQTQFQSHLDKGGAILLTTH 188
Cdd:cd03218 172 IQKIIKILKDRGIGVLITDH 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-194 |
3.55e-23 |
|
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: 92.56 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDsfaADLLFIGH 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE---AELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQ-------LSAYENVQHWLMVHGaQADEEEVYTL-LAKLGLIGLEDV----PvRTLSAGQQRRVALVR-LWLNq 148
Cdd:cd03261 78 RMGMLFQsgalfdsLTVFENVAFPLREHT-RLSEEEIREIvLEKLEAVGLRGAedlyP-AELSGGMKKRVALARaLALD- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2030133830 149 AKLWVLDEPFTALDKKGVAMLQTQFQS-HLDKGGAILLTTHQDLTAH 194
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAF 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-158 |
4.27e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.79 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTctKQdrclF------DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI--RDDYDSF 72
Cdd:COG0411 4 LLEVRGLT--KR----FgglvavDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItgLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 73 AADL--------LFighktgvnQQLSAYENV-----------------QHWLMVHGAQADEEEVYTLLAKLGLIGLEDVP 127
Cdd:COG0411 78 RLGIartfqnprLF--------PELTVLENVlvaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEP 149
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 128 VRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-197 |
4.94e-23 |
|
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: 90.71 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDS---FAADLLF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHKTGVNQQLSAYENVQHwlmvhgaqadeeevytllaklgligledvpvrTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL--------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2030133830 159 TALDKKGVAMLQTQFQSHLDKGG-AILLTTH-QDLTAHFAQ 197
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGiTVVLVTHdLDEAARLAD 169
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-188 |
7.17e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGH 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENvqhwLMVHG------AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLD 155
Cdd:PRK13536 122 FDNLDLEFTVREN----LLVFGryfgmsTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190
....*....|....*....|....*....|...
gi 2030133830 156 EPFTALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-189 |
8.13e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 92.07 E-value: 8.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQ------IRYNSTDIRD-----DY 69
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWElrkriGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 70 DSFAADLLFIGHKTGVNQQLSAYENVQHwLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQA 149
Cdd:COG1119 83 VSPALQLRFPRDETVLDVVLSGFFDSIG-LYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2030133830 150 KLWVLDEPFTALDKKGVAMLqTQFQSHLDKGG--AILLTTHQ 189
Cdd:COG1119 162 ELLILDEPTAGLDLGARELL-LALLDKLAAEGapTLVLVTHH 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-188 |
8.78e-23 |
|
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: 91.28 E-value: 8.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGHKTGVNQQLSAYENVQH 97
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 98 WLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQS 175
Cdd:cd03265 97 HARLYGVPGAErrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEK 176
|
170
....*....|....
gi 2030133830 176 HLDKGG-AILLTTH 188
Cdd:cd03265 177 LKEEFGmTILLTTH 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-188 |
9.01e-23 |
|
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: 91.41 E-value: 9.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSfaadllfIGHKTGVNQQ-------LS 90
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-------ARQSLGYCPQfdalfdeLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRR----VALVrlwlNQAKLWVLDEPFTALDKK 164
Cdd:cd03263 92 VREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKlslaIALI----GGPSVLLLDEPTSGLDPA 167
|
170 180
....*....|....*....|....
gi 2030133830 165 GVAMLqTQFQSHLDKGGAILLTTH 188
Cdd:cd03263 168 SRRAI-WDLILEVRKGRSIILTTH 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-162 |
1.06e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.72 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsFAADLLfiG 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA----WSPWEL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQ-------LSAYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRV----ALVRLW-- 145
Cdd:COG4559 75 RRRAVLPQhsslafpFTVEEVVALGRAPHGssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVqlarVLAQLWep 154
|
170
....*....|....*...
gi 2030133830 146 -LNQAKLWVLDEPFTALD 162
Cdd:COG4559 155 vDGGPRWLFLDEPTSALD 172
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-162 |
1.47e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.90 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDirddydsfaadlLFIGH 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD------------LFTNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTG------VNQQ------LSAYENVQHWLMV--HGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLN 147
Cdd:COG1118 71 PPRerrvgfVFQHyalfphMTVAENIAFGLRVrpPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170
....*....|....*
gi 2030133830 148 QAKLWVLDEPFTALD 162
Cdd:COG1118 151 EPEVLLLDEPFGALD 165
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-191 |
2.13e-22 |
|
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: 93.81 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYdsfAADLLFIGHKTGV---------NQQ 88
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS---RRSLRELRRRVQMvfqdpysslNPR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 LSAYENVQHWLMVHG---AQADEEEVYTLLAKLGLI-GLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkk 164
Cdd:COG1123 359 MTVGDIIAEPLRLHGllsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD-- 436
|
170 180 190
....*....|....*....|....*....|..
gi 2030133830 165 gvAMLQTQFQSHLDK-----GGAILLTTHqDL 191
Cdd:COG1123 437 --VSVQAQILNLLRDlqrelGLTYLFISH-DL 465
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-162 |
2.17e-22 |
|
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: 90.81 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDsfAADLLFIG 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI-TGLS--EKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVN-QQ------LSAYENVQHWLMVHGaQADEEEVYTL-LAKLGLIGLEDV----PvRTLSAGQQRRVALVRLWLNQ 148
Cdd:COG1127 82 RRIGMLfQGgalfdsLTVFENVAFPLREHT-DLSEAEIRELvLEKLELVGLPGAadkmP-SELSGGMRKRVALARALALD 159
|
170
....*....|....
gi 2030133830 149 AKLWVLDEPFTALD 162
Cdd:COG1127 160 PEILLYDEPTAGLD 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-191 |
3.24e-22 |
|
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: 89.87 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddYDSFAADLLFIGHKTGV---------NQQ 88
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL---LKLSRRLRKIRRKEIQMvfqdpmsslNPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 LSAYENVQHWLMVHGAQADEEEVYTLLAKLgLIGLEDVPVR------TLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03257 99 MTIGEQIAEPLRIHGKLSKKEARKEAVLLL-LVGVGLPEEVlnryphELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
170 180 190
....*....|....*....|....*....|....
gi 2030133830 163 kkgvAMLQTQFQSHLDK-----GGAILLTTHqDL 191
Cdd:cd03257 178 ----VSVQAQILDLLKKlqeelGLTLLFITH-DL 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-188 |
3.61e-22 |
|
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: 89.24 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRddydsfAADLLfighKTG------VNQQL 89
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AKERR----KSIgyvmqdVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 ---SAYENVQHWLMvhGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGV 166
Cdd:cd03226 85 ftdSVREELLLGLK--ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180
....*....|....*....|..
gi 2030133830 167 AMLQTQFQSHLDKGGAILLTTH 188
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITH 184
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
18-164 |
5.20e-22 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 91.64 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD------DY----DSFAadlLFighktgvnQ 87
Cdd:TIGR03265 21 KDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlppqkrDYgivfQSYA---LF--------P 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030133830 88 QLSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK 164
Cdd:TIGR03265 90 NLTVADNIAYGLKNRGMGRAEvaERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-177 |
8.42e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.55 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-------RDDYDSFAA 74
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 75 DLLFighktgvnQQLSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLW 152
Cdd:PRK09452 95 YALF--------PHMTVFENVAFGLRMQKTPAAEitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180
....*....|....*....|....*
gi 2030133830 153 VLDEPFTALDKKgvamLQTQFQSHL 177
Cdd:PRK09452 167 LLDESLSALDYK----LRKQMQNEL 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-188 |
1.02e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNStDIR----------DDYDSfAADLLFIGHK 82
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLRigylpqepplDDDLT-VLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 83 ----------------TGVNQQLSAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGLE-DVPVRTLSAGQQRRVALVRLW 145
Cdd:COG0488 88 elraleaeleeleaklAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDlDRPVSELSGGWRRRVALARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2030133830 146 LNQAKLWVLDEPFTALDKKGVAMLQTQFQSHldkGGAILLTTH 188
Cdd:COG0488 168 LSEPDLLLLDEPTNHLDLESIEWLEEFLKNY---PGTVLVVSH 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-188 |
1.63e-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: 87.70 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD----------DYDS 71
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrdiamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 FAadlLFiGHKTgvnqqlsAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQA 149
Cdd:cd03301 81 YA---LY-PHMT-------VYDNIAFGLKLRKVPKDEidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2030133830 150 KLWVLDEPFTALDkkgvAMLQTQFQSHLDK-----GGAILLTTH 188
Cdd:cd03301 150 KVFLMDEPLSNLD----AKLRVQMRAELKRlqqrlGTTTIYVTH 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-188 |
2.42e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTdirddydsfaadlLFIG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-------------VKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 ----HKTGVNQQLSAYENVQHWlmvhGAQADEEEVYTLLAKLGLIGlEDV--PVRTLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:COG0488 382 yfdqHQEELDPDKTVLDELRDG----APGGTEQEVRGYLGRFLFSG-DDAfkPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2030133830 155 DEPFTALDkkgVAMLQ------TQFQshldkgGAILLTTH 188
Cdd:COG0488 457 DEPTNHLD---IETLEaleealDDFP------GTVLLVSH 487
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-188 |
3.85e-21 |
|
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: 90.66 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCT--KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAA---- 74
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRqigv 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 75 ----DLLFIGhktgvnqqlSAYENvqhwLMVHGAQADEEEVYTLLAKLGLigLEDV---------PV----RTLSAGQQR 137
Cdd:COG2274 554 vlqdVFLFSG---------TIREN----ITLGDPDATDEEIIEAARLAGL--HDFIealpmgydtVVgeggSNLSGGQRQ 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 138 RVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQsHLDKGGAILLTTH 188
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLR-RLLKGRTVIIIAH 668
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-188 |
4.99e-21 |
|
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: 86.58 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHA-----GQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFaaDLLFIGHKTG-VNQQ------ 88
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKI--NLPPQQRKIGlVFQQyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 LSAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180
....*....|....*....|.
gi 2030133830 169 LQTQFQS-HLDKGGAILLTTH 188
Cdd:cd03297 170 LLPELKQiKKNLNIPVIFVTH 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-188 |
5.62e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGH 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENvqhwLMVHG------AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLD 155
Cdd:PRK13537 88 FDNLDPDFTVREN----LLVFGryfglsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190
....*....|....*....|....*....|...
gi 2030133830 156 EPFTALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-164 |
9.26e-21 |
|
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: 86.58 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCT-KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydSFAADLLFI 79
Cdd:TIGR02315 1 MLEVENLSKVyPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITK---LRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTG-VNQQ------LSAYENVQH--------WLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALV 142
Cdd:TIGR02315 78 RRRIGmIFQHynlierLTVLENVLHgrlgykptWRSLLGrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180
....*....|....*....|..
gi 2030133830 143 RLWLNQAKLWVLDEPFTALDKK 164
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPK 179
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
14-188 |
1.33e-20 |
|
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: 85.79 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDD--YDSFAADLLFIGHKTGVNQQLSA 91
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARLGIGYLPQEASIFRKLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 YENVQHWLMVHG---AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:TIGR04406 94 EENIMAVLEIRKdldRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGD 173
|
170 180
....*....|....*....|
gi 2030133830 169 LQTQFQSHLDKGGAILLTTH 188
Cdd:TIGR04406 174 IKKIIKHLKERGIGVLITDH 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-189 |
2.08e-20 |
|
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: 84.85 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFigHKTGVNQQLSAYENVQHW 98
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAaPPADRPVSMLF--QENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 99 LM--VHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVA-MLQTQFQS 175
Cdd:cd03298 95 LSpgLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAeMLDLVLDL 174
|
170
....*....|....
gi 2030133830 176 HLDKGGAILLTTHQ 189
Cdd:cd03298 175 HAETKMTVLMVTHQ 188
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-188 |
3.71e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfAADLLFIG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP----GAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVQHWLMVHGAQADEEEVYT--LLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAhqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2030133830 159 TALDkkgvAMLQTQFQSHL-----DKGGAILLTTH 188
Cdd:PRK11248 157 GALD----AFTREQMQTLLlklwqETGKQVLLITH 187
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-188 |
3.87e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.30 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCT----KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfaadl 76
Cdd:COG4525 3 MLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 lfiGHKTGVNQQ-------LSAYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLN 147
Cdd:COG4525 75 ---GADRGVVFQkdallpwLNVLDNVAFGLRLRGvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2030133830 148 QAKLWVLDEPFTALDkkgvAMLQTQFQSHL-----DKGGAILLTTH 188
Cdd:COG4525 152 DPRFLLMDEPFGALD----ALTREQMQELLldvwqRTGKGVFLITH 193
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-197 |
4.61e-20 |
|
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: 84.54 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCT-KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSfaaDLLFIG 80
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGK---ALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTG-VNQQ------LSAYENVQH------------WLMVHGAqaDEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVAL 141
Cdd:cd03256 78 RQIGmIFQQfnlierLSVLENVLSgrlgrrstwrslFGLFPKE--EKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2030133830 142 VRLWLNQAKLWVLDEPFTALD-KKGVAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFAQ 197
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDpASSRQVMDLLKRINREEGITVIVSLHQvDLAREYAD 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
4.84e-20 |
|
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: 87.34 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDR-CLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFI 79
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTGVNQQlSAYENVQHWLmvhgAQADEEEVYTLLAKLGLIGLE-------DVPV----RTLSAGQQRRVALVRLWLNQ 148
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR----PDASDAEIREALERAGLDEFVaalpqglDTPIgeggAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2030133830 149 AKLWVLDEPFTALDKKGVAMLQTQFQShLDKGGAILLTTHQDLTAHFA 196
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLALAALA 523
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-162 |
7.64e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.44 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDS--FAADLLF 78
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-ADWSPaeLARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHKTGVNQQLSAYENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVR----LWL--NQAK 150
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGlsRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARvlaqLWEpdGPPR 160
|
170
....*....|..
gi 2030133830 151 LWVLDEPFTALD 162
Cdd:PRK13548 161 WLLLDEPTSALD 172
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-164 |
2.46e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 84.35 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-------RDdydsfaadllfIGHktgVNQQ-- 88
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN-----------IAM---VFQSya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 ----LSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVAL----VRlwlnQAKLWVLDEPF 158
Cdd:COG3839 86 lyphMTVYENIAFPLKLRKVPKAEidRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALgralVR----EPKVFLLDEPL 161
|
....*.
gi 2030133830 159 TALDKK 164
Cdd:COG3839 162 SNLDAK 167
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-196 |
3.58e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-------RDDYDSFAADLLFighktgvnQQLS 90
Cdd:PRK11432 23 DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrsiqqRDICMVFQSYALF--------PHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD------ 162
Cdd:PRK11432 95 LGENVGYGLKMLGVPKEErkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDanlrrs 174
|
170 180 190
....*....|....*....|....*....|....*
gi 2030133830 163 -KKGVAMLQTQFqshldkGGAILLTTHqDLTAHFA 196
Cdd:PRK11432 175 mREKIRELQQQF------NITSLYVTH-DQSEAFA 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-188 |
3.62e-19 |
|
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: 81.87 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRdDYDsfAADL------------LFIGhktgv 85
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR-QLD--PADLrrnigyvpqdvtLFYG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 86 nqqlSAYENvqhwLMVHGAQADEEEVytlLAKLGLIGLE----------DVPV----RTLSAGQQRRVALVRLWLNQAKL 151
Cdd:cd03245 93 ----TLRDN----ITLGAPLADDERI---LRAAELAGVTdfvnkhpnglDLQIgergRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 2030133830 152 WVLDEPFTALDKKGVAMLQTQFQSHLdKGGAILLTTH 188
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITH 197
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-177 |
4.88e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 83.31 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 34 GPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddydsfaadLLFIGHKTGVNQ---------QLSAYENVQHWLMVHGA 104
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----------TNVPPHLRHINMvfqsyalfpHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 105 QAdEEEVYTLLAKLGLIGLEDVPVR---TLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKgvamLQTQFQSHL 177
Cdd:TIGR01187 73 PR-AEIKPRVLEALRLVQLEEFADRkphQLSGGQQQRVALARALVFKPKILLLDEPLSALDKK----LRDQMQLEL 143
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-204 |
5.58e-19 |
|
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: 81.30 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLfigHKTGVNQQ-------LS 90
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR---RKIGVVFQdfrllpdRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMV--HGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:cd03292 95 VYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 2030133830 169 LQTQFQSHLDKGGAILLTTHQDLTAHFAQLQTLALE 204
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-162 |
6.78e-19 |
|
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: 81.04 E-value: 6.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfAADLLFIGHKTG-VNQQ------LS 90
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD----KKNINELRQKVGmVFQQfnlfphLT 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 91 AYENVQHWLM-VHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03262 93 VLENITLAPIkVKGMSKAEaeERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-164 |
7.99e-19 |
|
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: 81.23 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddydsfaADLLFIGHKTGVNQQ-------LS 90
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--------TNLPPEKRDISYVPQnyalfphMT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 91 AYENVQHWLMVHGAQ--ADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK 164
Cdd:cd03299 88 VYKNIAYGLKKRKVDkkEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-164 |
1.57e-18 |
|
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: 80.46 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDSFAADLLFIGHKTGVNQQLSAYENVQH 97
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030133830 98 WLMV-HGAQ---ADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK 164
Cdd:cd03296 98 GLRVkPRSErppEAEirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-196 |
1.96e-18 |
|
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: 78.58 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFIGHKTgvnqQL---SA 91
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQDP----FLfsgTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 YENVqhwlmvhgaqadeeevytllaklgligledvpvrtLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQT 171
Cdd:cd03228 93 RENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180
....*....|....*....|....*
gi 2030133830 172 QFQsHLDKGGAILLTTHQDLTAHFA 196
Cdd:cd03228 138 ALR-ALAKGKTVIVIAHRLSTIRDA 161
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-193 |
2.05e-18 |
|
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: 80.07 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFI-GHKTGVNQQLSAYENVQ 96
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 97 hwLMVHGAQADEEEVYTLLAKLG-LIGLE---DVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkkgvAMLQTQ 172
Cdd:cd03267 118 --LLAAIYDLPPARFKKRLDELSeLLDLEellDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD----VVAQEN 191
|
170 180
....*....|....*....|....*...
gi 2030133830 173 FQSHL-----DKGGAILLTTH--QDLTA 193
Cdd:cd03267 192 IRNFLkeynrERGTTVLLTSHymKDIEA 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-188 |
2.42e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.07 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddydsfaADL-------LFIGH---KTGVNQQLS 90
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--------THLpmhkrarLGIGYlpqEASIFRKLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:COG1137 95 VEDNILAVLELRKLSKKEreERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVAD 174
|
170 180
....*....|....*....|.
gi 2030133830 169 LQtQFQSHL-DKGGAILLTTH 188
Cdd:COG1137 175 IQ-KIIRHLkERGIGVLITDH 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-188 |
3.12e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.99 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYN--STDIRDDYDSFAADLLFIgHktgvnQ------QLSAY 92
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRSPRDAQAAGIAII-H-----QelnlvpNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 93 ENV--QHWLMVHG--------AQADEeevytLLAKLGL-IGLeDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:COG1129 98 ENIflGREPRRGGlidwramrRRARE-----LLARLGLdIDP-DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|
gi 2030133830 162 DKKGVAMLqtqFQ--SHL-DKGGAILLTTH 188
Cdd:COG1129 172 TEREVERL---FRiiRRLkAQGVAIIYISH 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-162 |
6.62e-18 |
|
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: 78.38 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGF-----ARADEGQIRYNSTDIRDDYDsfaaDLLFIGHKTG-VN 86
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV----DVLELRRRVGmVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 87 QQ-----LSAYENVQHWLMVHG---AQADEEEVYTLLAKLGLIGLED--VPVRTLSAGQQRRVALVRLWLNQAKLWVLDE 156
Cdd:cd03260 88 QKpnpfpGSIYDNVAYGLRLHGiklKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
....*.
gi 2030133830 157 PFTALD 162
Cdd:cd03260 168 PTSALD 173
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-188 |
8.45e-18 |
|
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: 76.33 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTdirddydsfaadlLFIGH 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------VKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 ktgVNQqlsayenvqhwlmvhgaqadeeevytllaklgligledvpvrtLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:cd03221 68 ---FEQ-------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180
....*....|....*....|....*..
gi 2030133830 162 DKKGVAMLQTQFQSHldkGGAILLTTH 188
Cdd:cd03221 102 DLESIEALEEALKEY---PGTVILVSH 125
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-189 |
1.39e-17 |
|
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: 77.62 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRC----LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddyDSFA-AD 75
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL----TLLSgKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 76 LLFIGHKTG-VNQQ---LS---AYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWL 146
Cdd:cd03258 77 LRKARRRIGmIFQHfnlLSsrtVFENVALPLEIAGVPKAEieERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2030133830 147 NQAKLWVLDEPFTALDKK---GVAMLQTQFQSHLdkGGAILLTTHQ 189
Cdd:cd03258 157 NNPKVLLCDEATSALDPEttqSILALLRDINREL--GLTIVLITHE 200
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-162 |
1.41e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 77.73 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTctKQ--DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfAADLLF 78
Cdd:COG1126 1 MIEIENLH--KSfgDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDS----KKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHKTG-VNQQ------LSAYENVQHWLM-VHG---AQAdEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVR-LWL 146
Cdd:COG1126 75 LRRKVGmVFQQfnlfphLTVLENVTLAPIkVKKmskAEA-EERAMELLERVGLADKADAYPAQLSGGQQQRVAIARaLAM 153
|
170
....*....|....*.
gi 2030133830 147 NqAKLWVLDEPFTALD 162
Cdd:COG1126 154 E-PKVMLFDEPTSALD 168
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-197 |
2.64e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARAdEGQIRYNSTDIRdDYDsfAADLlfIGHKTGVNQQLSAYEN--VQH 97
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLS-DWS--AAEL--ARHRAYLSQQQSPPFAmpVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 98 WLMVHG-AQADEEEVYTLLAKL-GLIGLEDV---PVRTLSAGQQRRVALVR----LW--LN-QAKLWVLDEPFTALDKKG 165
Cdd:COG4138 89 YLALHQpAGASSEAVEQLLAQLaEALGLEDKlsrPLTQLSGGEWQRVRLAAvllqVWptINpEGQLLLLDEPMNSLDVAQ 168
|
170 180 190
....*....|....*....|....*....|....
gi 2030133830 166 VAMLQTQFQSHLDKGGAILLTTHqDL--TAHFAQ 197
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSH-DLnhTLRHAD 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-162 |
3.14e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-----RDDYDS---- 71
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVrkrm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 ---FAADLLFighktgvnQQLSAYENVQHWLMVHGAQADEEEVYTLLAKL---GLIGLEDVPVRTLSAGQQRRVALVRLW 145
Cdd:PRK11831 87 smlFQSGALF--------TDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLeavGLRGAAKLMPSELSGGMARRAALARAI 158
|
170
....*....|....*..
gi 2030133830 146 LNQAKLWVLDEPFTALD 162
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQD 175
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-189 |
7.79e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.96 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDA---VTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFArADEGQIRYNSTDIRD-DYDSFAADLL 77
Cdd:PRK11174 348 VTIEAedlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 78 FIGHktgvNQQL---SAYENVqhwLMVHgAQADEEEVYTLLAK-----------LGLigleDVPVR----TLSAGQQRRV 139
Cdd:PRK11174 427 WVGQ----NPQLphgTLRDNV---LLGN-PDASDEQLQQALENawvseflpllpQGL----DTPIGdqaaGLSVGQAQRL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 140 ALVRLWLNQAKLWVLDEPFTALDKKG-VAMLQTQFQSHLDKggAILLTTHQ 189
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSeQLVMQALNAASRRQ--TTLMVTHQ 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-188 |
7.88e-17 |
|
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: 78.02 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCT--KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARAD---EGQIRYNSTDIRDdydsfaAD 75
Cdd:COG1123 4 LLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE------LS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 76 LLFIGHKTGVNQQ--------LSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLW 145
Cdd:COG1123 78 EALRGRRIGMVFQdpmtqlnpVTVGDQIAEALENLGLSRAEarARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2030133830 146 LNQAKLWVLDEPFTALDKKGVAM-LQTQFQSHLDKGGAILLTTH 188
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEiLDLLRELQRERGTTVLLITH 201
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-161 |
8.30e-17 |
|
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: 75.55 E-value: 8.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRdDYDSFAADLLFIGHktgVNQ------QL 89
Cdd:cd03224 16 LFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-GLPPHERARAGIGY---VPEgrrifpEL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 90 SAYENVQ---HWLMVHGAQADEEEVYTLLAKLGliGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:cd03224 91 TVEENLLlgaYARRRAKRKARLERVYELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-162 |
1.00e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.05 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-----RDDYDSFAAD- 75
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlhaRDRKVGFVFQh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 76 -LLFighktgvnQQLSAYENVQHWLMV------HGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQ 148
Cdd:PRK10851 83 yALF--------RHMTVFDNIAFGLTVlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170
....*....|....
gi 2030133830 149 AKLWVLDEPFTALD 162
Cdd:PRK10851 155 PQILLLDEPFGALD 168
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-189 |
1.06e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfAADLLFIG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDP----KVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTG-VNQQ------LSAYENVQHW-LMVHGA--QADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAK 150
Cdd:PRK09493 77 QEAGmVFQQfylfphLTALENVMFGpLRVRGAskEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2030133830 151 LWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-188 |
1.61e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.80 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTD----------IRDDYD 70
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshvppyqrpINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 71 SFAadlLFiGHKTgVNQQLsAYENVQHWLMVHGAQADEEEVytllakLGLIGLEDVPVR---TLSAGQQRRVALVRLWLN 147
Cdd:PRK11607 99 SYA---LF-PHMT-VEQNI-AFGLKQDKLPKAEIASRVNEM------LGLVHMQEFAKRkphQLSGGQRQRVALARSLAK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2030133830 148 QAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAI-LLTTH 188
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTcVMVTH 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-188 |
2.38e-16 |
|
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: 74.39 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAAdllFIGHKTGVNQQ-------L 89
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlDEDARAR---LRARHVGFVFQsfqllptL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 SAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK-GVAM 168
Cdd:COG4181 106 TALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAtGEQI 185
|
170 180
....*....|....*....|
gi 2030133830 169 LQTQFQSHLDKGGAILLTTH 188
Cdd:COG4181 186 IDLLFELNRERGTTLVLVTH 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-160 |
6.84e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYN--STDIRDDYDSFAADllfIGHktgVNQQ------L 89
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRIRSPRDAIALG---IGM---VHQHfmlvpnL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030133830 90 SAYENV-----QHWLMVHGAQADEEEVYTLLAKLGL-IGLeDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPfTA 160
Cdd:COG3845 96 TVAENIvlglePTKGGRLDRKAARARIRELSERYGLdVDP-DAKVEDLSVGEQQRVEILKALYRGARILILDEP-TA 170
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-162 |
8.66e-16 |
|
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: 74.37 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDaVTCTKQDRCLfdSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfaADLLF-- 78
Cdd:COG4148 2 MLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDS-----ARGIFlp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 -----IGHktgVNQQ------LSAYENVQ--HWLMVHGA-QADEEEVYTLlakLGLIGLEDVPVRTLSAGQQRRVALVRL 144
Cdd:COG4148 74 phrrrIGY---VFQEarlfphLSVRGNLLygRKRAPRAErRISFDEVVEL---LGIGHLLDRRPATLSGGERQRVAIGRA 147
|
170
....*....|....*...
gi 2030133830 145 WLNQAKLWVLDEPFTALD 162
Cdd:COG4148 148 LLSSPRLLLMDEPLAALD 165
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-188 |
1.08e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIR--DDYDSFAADLLFIGHKTGVNQQLSA 91
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 YENVQHWLMVH---GAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:PRK10895 96 YDNLMAVLQIRddlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180
....*....|....*....|
gi 2030133830 169 LQTQFQSHLDKGGAILLTTH 188
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITDH 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-188 |
1.21e-15 |
|
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: 71.58 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 12 QDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSfaadllfIGHKTGV-NQQLS 90
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-------LSSLISVlNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENvqhwlmvhgaqadeeevyTLLAKLGligledvpvRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQ 170
Cdd:cd03247 86 LFDT------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170
....*....|....*...
gi 2030133830 171 TQFQSHLdKGGAILLTTH 188
Cdd:cd03247 139 SLIFEVL-KDKTLIWITH 155
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-188 |
1.47e-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: 70.92 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNST--DIRDDYDSFAAdllfighktGVNqqlsayenv 95
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRA---------GIA--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 96 qhwlMVHgaQadeeevytllaklgligledvpvrtLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQS 175
Cdd:cd03216 79 ----MVY--Q-------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR 127
|
170
....*....|...
gi 2030133830 176 HLDKGGAILLTTH 188
Cdd:cd03216 128 LRAQGVAVIFISH 140
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-188 |
2.00e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.57 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrdDYDsfAADLLFIGHKTGV------NQQLSA-- 91
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI--DYS--RKGLMKLRESVGMvfqdpdNQLFSAsv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 YENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVA-M 168
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEvrKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeI 180
|
170 180
....*....|....*....|
gi 2030133830 169 LQTQFQSHLDKGGAILLTTH 188
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATH 200
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-189 |
2.22e-15 |
|
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: 71.53 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADE---GQIRYNSTDIRDDydsfaadlLFIGHKTGVNQQ------LS 90
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPD--------QFQKCVAYVRQDdillpgLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVH------GAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkK 164
Cdd:cd03234 98 VRETLTYTAILRlprkssDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD-S 176
|
170 180
....*....|....*....|....*.
gi 2030133830 165 GVAMLQTQFQSHLDKGG-AILLTTHQ 189
Cdd:cd03234 177 FTALNLVSTLSQLARRNrIVILTIHQ 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-162 |
2.42e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.54 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRclfdSLSFTLH--AGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDS------- 71
Cdd:PRK10771 1 MLKLTDITWLYHHL----PMRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 FAADLLFiGHKTgVNQQLSayenvqhwLMVH-GAQADEEEVYTLLAKLGLIGLEDVPVR---TLSAGQQRRVALVRLWLN 147
Cdd:PRK10771 77 FQENNLF-SHLT-VAQNIG--------LGLNpGLKLNAAQREKLHAIARQMGIEDLLARlpgQLSGGQRQRVALARCLVR 146
|
170
....*....|....*
gi 2030133830 148 QAKLWVLDEPFTALD 162
Cdd:PRK10771 147 EQPILLLDEPFSALD 161
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-162 |
3.90e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYD-SFAADLLFI 79
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 G--HKT--GVN-QQLSAYENvQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLW 152
Cdd:PRK11231 82 PqhHLTpeGITvRELVAYGR-SPWLSLWGrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170
....*....|
gi 2030133830 153 VLDEPFTALD 162
Cdd:PRK11231 161 LLDEPTTYLD 170
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-196 |
4.66e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrdDYDsfAADLLFIGHKTGV-----NQQLSA- 91
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI--KYD--KKSLLEVRKTVGIvfqnpDDQLFAp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 --YENVQHWLMVHGAQADEEE--VYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVA 167
Cdd:PRK13639 95 tvEEDVAFGPLNLGLSKEEVEkrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190
....*....|....*....|....*....|
gi 2030133830 168 MLQTQFQSHLDKGGAILLTTHQ-DLTAHFA 196
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDvDLVPVYA 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-189 |
6.83e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDsfaadllfIG 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS--------LS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQL-----------------SAYENVQHWLMVHGAQADEEEV---YTLLAKLGLIGLEDVPVRTLSAGQQRRVA 140
Cdd:PRK11264 75 QQKGLIRQLrqhvgfvfqnfnlfphrTVLENIIEGPVIVKGEPKEEATaraRELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2030133830 141 LVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-188 |
7.44e-15 |
|
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: 70.25 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 17 FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDirddydsfaADLLFIGhkTGVNQQLSAYENVQ 96
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLGLG--GGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 97 HWLMVHGAQADE-----EEVYtllaklGLIGLE---DVPVRTLSAGQQRRVAL-VRLWLNqAKLWVLDEPFTALDKKGVA 167
Cdd:cd03220 107 LNGRLLGLSRKEidekiDEII------EFSELGdfiDLPVKTYSSGMKARLAFaIATALE-PDILLIDEVLAVGDAAFQE 179
|
170 180
....*....|....*....|.
gi 2030133830 168 MLQTQFQSHLDKGGAILLTTH 188
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSH 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-162 |
9.26e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.12 E-value: 9.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFighktgVNQQ--- 88
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGV------VPQDtfl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 --LSAYENVQHWLmvhgAQADEEEVYTLLAKLGL---I-----GLeDVPV----RTLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:COG1132 426 fsGTIRENIRYGR----PDATDEEVEEAAKAAQAhefIealpdGY-DTVVgergVNLSGGQRQRIAIARALLKDPPILIL 500
|
....*...
gi 2030133830 155 DEPFTALD 162
Cdd:COG1132 501 DEATSALD 508
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-188 |
1.14e-14 |
|
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: 70.02 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCT-KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRddydsfAADLLFIG 80
Cdd:cd03295 1 IEFENVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR------EQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTG-VNQQ------LSAYENV------QHWlmvhGAQADEEEVYTLLAklgLIGLEDVPVR-----TLSAGQQRRVALV 142
Cdd:cd03295 75 RKIGyVIQQiglfphMTVEENIalvpklLKW----PKEKIRERADELLA---LVGLDPAEFAdryphELSGGQQQRVGVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2030133830 143 RLWLNQAKLWVLDEPFTALDKKGVAMLQTQF---QSHLDKggAILLTTH 188
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFkrlQQELGK--TIVFVTH 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-189 |
1.46e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 19 SLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAadllfigHKTG---VNQQ------L 89
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA-------HQLGiylVPQEpllfpnL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 SAYENVQHWLMVHgaQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAML 169
Cdd:PRK15439 102 SVKENILFGLPKR--QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERL 179
|
170 180
....*....|....*....|
gi 2030133830 170 QTQFQSHLDKGGAILLTTHQ 189
Cdd:PRK15439 180 FSRIRELLAQGVGIVFISHK 199
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-140 |
1.76e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 17 FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTdirddydsfAADLLFIGhkTGVNQQLSAYENVQ 96
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VSALLELG--AGFHPELTGRENIY 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 97 HWLMVHGAQADEEEvytllAKLGLI----GLE---DVPVRTLSAGQQRRVA 140
Cdd:COG1134 111 LNGRLLGLSRKEID-----EKFDEIvefaELGdfiDQPVKTYSSGMRARLA 156
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-204 |
1.88e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVT-CTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNStdirddydsfAADLLFI 79
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA----------GARVLFL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTGVN-----QQLsAYENvqhwlmvHGAQADEEEVYTLLAKLGLIGLE---DVPV---RTLSAGQQRRVALVRLWLNQ 148
Cdd:COG4178 432 PQRPYLPlgtlrEAL-LYPA-------TAEAFSDAELREALEAVGLGHLAerlDEEAdwdQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 149 AKLWVLDEPFTALDKKGVAMLQTQFQSHLdKGGAILLTTHQDLTAHFAQlQTLALE 204
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREEL-PGTTVISVGHRSTLAAFHD-RVLELT 557
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-185 |
3.66e-14 |
|
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: 67.46 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQdrclFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI--RDDYDSFAADLLF 78
Cdd:cd03215 4 VLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IG---HKTGVNQQLSAYENVqhwlmvhgaqadeeevytLLAKLgligledvpvrtLSAGQQRRVALVRlWLN-QAKLWVL 154
Cdd:cd03215 80 VPedrKREGLVLDLSVAENI------------------ALSSL------------LSGGNQQKVVLAR-WLArDPRVLIL 128
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 155 DEPFTALDKKGVAMLQTQFQSHLDKGGAILL 185
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLL 159
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-188 |
3.99e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTdirddydsfaadlLFIG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-------------LRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HktgVNQQLSAYE----NVQHWLMVHGAqADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDE 156
Cdd:PRK09544 71 Y---VPQKLYLDTtlplTVNRFLRLRPG-TKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|...
gi 2030133830 157 PFTALDKKG-VAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK09544 147 PTQGVDVNGqVALYDLIDQLRRELDCAVLMVSH 179
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-171 |
4.97e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.57 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFI 79
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTGVNQQLSAYENV--------QHWLmvhgAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRR--VALVrlwLNQA 149
Cdd:COG4604 81 RQENHINSRLTVRELVafgrfpysKGRL----TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAMV---LAQD 153
|
170 180
....*....|....*....|....
gi 2030133830 150 KLWV-LDEPFTALD-KKGVAMLQT 171
Cdd:COG4604 154 TDYVlLDEPLNNLDmKHSVQMMKL 177
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-164 |
9.48e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 9.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTC-----TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-------Rdd 68
Cdd:COG1101 1 MLELKNLSKtfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 69 ydsfAAdllFIGH-----KTGVNQQLSAYENV--------QHWLMVHGAQADEEEVYTLLAKLGLiGLED---VPVRTLS 132
Cdd:COG1101 79 ----AK---YIGRvfqdpMMGTAPSMTIEENLalayrrgkRRGLRRGLTKKRRELFRELLATLGL-GLENrldTKVGLLS 150
|
170 180 190
....*....|....*....|....*....|..
gi 2030133830 133 AGQQRRVALVRLWLNQAKLWVLDEPFTALDKK 164
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPK 182
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-157 |
1.56e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 66.93 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddyDSFAADLLF---IGHktgVNQ----- 87
Cdd:COG0410 19 LHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI----TGLPPHRIArlgIGY---VPEgrrif 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030133830 88 -QLSAYENvqhwLMV--------HGAQADEEEVYTLLAKLGliGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEP 157
Cdd:COG0410 91 pSLTVEEN----LLLgayarrdrAEVRADLERVYELFPRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-188 |
1.95e-13 |
|
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: 65.32 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI----RDDYDSFAA-----DLLFIGhktgvn 86
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsqwdPNELGDHVGylpqdDELFSG------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 87 qqlSAYENVqhwlmvhgaqadeeevytllaklgligledvpvrtLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGV 166
Cdd:cd03246 91 ---SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180
....*....|....*....|..
gi 2030133830 167 AMLQTQFQSHLDKGGAILLTTH 188
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAH 154
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-191 |
2.00e-13 |
|
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: 66.90 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydSFAADLLFI-GHKTG-VNQ------QLSAY 92
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA---MSRKELRELrRKKISmVFQsfallpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 93 ENVQHWLMVHG--AQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkkgvAMLQ 170
Cdd:cd03294 121 ENVAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD----PLIR 196
|
170 180
....*....|....*....|....*.
gi 2030133830 171 TQFQSHL-----DKGGAILLTTHqDL 191
Cdd:cd03294 197 REMQDELlrlqaELQKTIVFITH-DL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-189 |
2.09e-13 |
|
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: 65.65 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFAR--ADEGQIRYNSTDIRDdyDSFAADLLFIGHKTGVNQ 87
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDK--RSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 88 QLSAYENvqhwLMVHgaqadeeevytllAKLgligledvpvRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVA 167
Cdd:cd03213 96 TLTVRET----LMFA-------------AKL----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180
....*....|....*....|..
gi 2030133830 168 MLQTQFQSHLDKGGAILLTTHQ 189
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQ 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-189 |
2.60e-13 |
|
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: 68.12 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGHKTGVNQQLSAYE 93
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 NVQHWLMVHGAQADEE--EVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD---KKGVAM 168
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpysRRSIWD 1102
|
170 180
....*....|....*....|.
gi 2030133830 169 LQTQFQShldkGGAILLTTHQ 189
Cdd:TIGR01257 1103 LLLKYRS----GRTIIMSTHH 1119
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-189 |
2.62e-13 |
|
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: 64.87 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVT-CTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYnstdirddydSFAADLLFIG 80
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM----------PEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HK----TGVNQQLSAYEnvqhWLMVhgaqadeeevytllaklgligledvpvrtLSAGQQRRVALVRLWLNQAKLWVLDE 156
Cdd:cd03223 71 QRpylpLGTLREQLIYP----WDDV-----------------------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|....
gi 2030133830 157 PFTALDkkgvAMLQTQFQSHLDKGGAILLT-THQ 189
Cdd:cd03223 118 ATSALD----EESEDRLYQLLKELGITVISvGHR 147
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-201 |
4.08e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIR----DDYD-----S 71
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpEIYRqqvsyC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 FAADLLFiGHktgvnqqlSAYENVQHWLMVHGAQADEEEVYTLLAKLGL-IGLEDVPVRTLSAGQQRRVALVRLWLNQAK 150
Cdd:PRK10247 87 AQTPTLF-GD--------TVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 151 LWVLDEPFTALD---KKGVAMLQTQFQShlDKGGAILLTTH-QDLTAHFAQLQTL 201
Cdd:PRK10247 158 VLLLDEITSALDesnKHNVNEIIHRYVR--EQNIAVLWVTHdKDEINHADKVITL 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-189 |
1.09e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADE---------GQIRYNSTDIRDDYDS 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 FAADLLFIGHKTGVNQQLSAYENV--------QHW--LMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVAL 141
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVligalgstPFWrtCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2030133830 142 VRLWLNQAKLWVLDEPFTALDKKGVAM-LQTQFQSHLDKGGAILLTTHQ 189
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIvMDTLRDINQNDGITVVVTLHQ 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-196 |
1.59e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydSFAADLLFIGHKTGVNQQLSAYE 93
Cdd:PRK13649 21 RALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITST--SKNKDIKQIRKKVGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 NVQHWLM---VHGAQ----ADEEEVYTLLAKLGLIGL-EDVPVRT---LSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:PRK13649 98 LFEETVLkdvAFGPQnfgvSQEEAEALAREKLALVGIsESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190
....*....|....*....|....*....|....*
gi 2030133830 163 KKGVAMLQTQFQSHLDKGGAILLTTH-QDLTAHFA 196
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYA 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-162 |
1.67e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYN-STDI----RDDYDSFAADL 76
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSeNANIgyyaQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 lfighktgvnqqlsayeNVQHWlMVHGAQA--DEEEVYTLLAKLgLIGLEDV--PVRTLSAGQQRRVALVRLWLNQAKLW 152
Cdd:PRK15064 400 -----------------TLFDW-MSQWRQEgdDEQAVRGTLGRL-LFSQDDIkkSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|
gi 2030133830 153 VLDEPFTALD 162
Cdd:PRK15064 461 VMDEPTNHMD 470
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-197 |
1.84e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAA----DLLFIGHKTGVNQQLSAY 92
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALAQlrreHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 93 ENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQ 170
Cdd:PRK10535 105 QNVEVPAVYAGLERKQrlLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180
....*....|....*....|....*..
gi 2030133830 171 TQFQSHLDKGGAILLTTHQDLTAHFAQ 197
Cdd:PRK10535 185 AILHQLRDRGHTVIIVTHDPQVAAQAE 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-164 |
2.01e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.23 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCT--KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDSfaADLLfi 79
Cdd:PRK11160 339 LTLNNVSFTypDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSE--AALR-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTGVNQQ---LSAY--ENvqhwLMVHGAQADEEEVYTLLAKLGLIGLEDVPV----------RTLSAGQQRRVALVRL 144
Cdd:PRK11160 414 QAISVVSQRvhlFSATlrDN----LLLAAPNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARA 489
|
170 180
....*....|....*....|
gi 2030133830 145 WLNQAKLWVLDEPFTALDKK 164
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAE 509
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-162 |
3.13e-12 |
|
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: 64.57 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNST-------DIRDDYD---- 70
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklayvdQSRDALDpnkt 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 71 -----SFAADLLFIGhKTGVNQQlsAYENvqhWLMVHGaqADEEEvytllaklgligledvPVRTLSAGQQRRVALVRLW 145
Cdd:TIGR03719 403 vweeiSGGLDIIKLG-KREIPSR--AYVG---RFNFKG--SDQQK----------------KVGQLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 2030133830 146 LNQAKLWVLDEPFTALD 162
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-157 |
3.75e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKqdrcLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYN--STDIRDDYDSFAADLLF 78
Cdd:COG1129 256 VLEVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 I---GHKTGVNQQLSAYENV--------QHWLMVHGAQAdEEEVYTLLAKLGL-IGLEDVPVRTLSAGQQRRVALVRlWL 146
Cdd:COG1129 332 VpedRKGEGLVLDLSIRENItlasldrlSRGGLLDRRRE-RALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAK-WL 409
|
170
....*....|..
gi 2030133830 147 N-QAKLWVLDEP 157
Cdd:COG1129 410 AtDPKVLILDEP 421
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-191 |
4.22e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 19 SLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARAdEGQIRYNSTDIRdDYDsfAADLLFigHKTGVNQQLSAYEN--VQ 96
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLE-AWS--AAELAR--HRAYLSQQQTPPFAmpVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 97 HWLMVH-GAQADEEEVYTLLAKL-GLIGLEDV---PVRTLSAGQQRRVALV----RLW--LN-QAKLWVLDEPFTALDKK 164
Cdd:PRK03695 88 QYLTLHqPDKTRTEAVASALNEVaEALGLDDKlgrSVNQLSGGEWQRVRLAavvlQVWpdINpAGQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*..
gi 2030133830 165 GVAMLQTQFQSHLDKGGAILLTTHqDL 191
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSH-DL 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-188 |
4.29e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIR--DDYDSFAADLLFIGHKTGVNQQLSAYENV 95
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEMTVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 96 qhWL--------MVHGAQAdeeeVYTLLAKLGLIGLE---DVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK 164
Cdd:PRK11288 101 --YLgqlphkggIVNRRLL----NYEAREQLEHLGVDidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180
....*....|....*....|....
gi 2030133830 165 GVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-162 |
4.76e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 23 TLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQ------IRYNSTDIRDDYDsfaadllfighktgvnqqlsayENVQ 96
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpelkISYKPQYIKPDYD----------------------GTVE 418
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030133830 97 HWLMVHGAQADEEEVYTLLAK-LGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:PRK13409 419 DLLRSITDDLGSSYYKSEIIKpLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-188 |
4.97e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSfaaDLLFIGHKTGVNQQ----- 88
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR---EVPFLRRQIGMIFQdhhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 --LSAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIG-LEDVPVRtLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDK 163
Cdd:PRK10908 92 mdRTVYDNVAIPLIIAGASGDDirRRVSAALDKVGLLDkAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|....*
gi 2030133830 164 KGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-162 |
6.31e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.71 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDSFAADLLF-- 78
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVas 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHKTGVNQQLSAYENVQHWLMVH------GAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLW 152
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPHrsrfdtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170
....*....|
gi 2030133830 153 VLDEPFTALD 162
Cdd:PRK09536 162 LLDEPTASLD 171
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-162 |
9.49e-12 |
|
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: 62.57 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYnSTDIrddydSFAADLLFIGHKT-------GVnqqlsAY 92
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH-SGRI-----SFSSQFSWIMPGTikeniifGV-----SY 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 93 ENVQHWLMVHGAQADE------EEVYTLLAKLGLigledvpvrTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03291 125 DEYRYKSVVKACQLEEditkfpEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-188 |
9.63e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIrynstdirddydsfaaDLLFIGHKTGVNQQLSAY-------- 92
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI----------------SILGQPTRQALQKNLVAYvpqseevd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 93 -------ENV--------QHWLMVHGAQaDEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEP 157
Cdd:PRK15056 91 wsfpvlvEDVvmmgryghMGWLRRAKKR-DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 158 FTALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-169 |
1.44e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAG-FARAD-EGQIRYNSTDIRDDY--DSFAADLLFIGHKTGVNQQLSAYE 93
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTyEGEIIFEGEELQASNirDTERAGIAIIHQELALVKELSVLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 NVqhWL---MVHGAQADEEEVY----TLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGV 166
Cdd:PRK13549 102 NI--FLgneITPGGIMDYDAMYlraqKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESET 179
|
...
gi 2030133830 167 AML 169
Cdd:PRK13549 180 AVL 182
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-188 |
1.75e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNST---DIRDDYDSFAADLLF 78
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHKTGVNqqlsayeNVQhwLMVHGAQADEEevytlLAKLGLIGLEDV----PVrTLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:PRK11247 93 LPWKKVID-------NVG--LGLKGQWRDAA-----LQALAAVGLADRanewPA-ALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 2030133830 155 DEPFTALDkkgvAMLQTQFQSHLDK-----GGAILLTTH 188
Cdd:PRK11247 158 DEPLGALD----ALTRIEMQDLIESlwqqhGFTVLLVTH 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-193 |
1.88e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.03 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 3 EIDAVtctkqdrclfDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAAD--LLFiG 80
Cdd:COG4586 34 EVEAV----------DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRigVVF-G 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENvqhwLMVHGA-----QADEEEVYTLLAK-LGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:COG4586 103 QRSQLWWDLPAIDS----FRLLKAiyripDAEYKKRLDELVElLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2030133830 155 DEPFTALDkkgVAMlQTQFQSHL-----DKGGAILLTTH--QDLTA 193
Cdd:COG4586 179 DEPTIGLD---VVS-KEAIREFLkeynrERGTTILLTSHdmDDIEA 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-63 |
1.94e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 1.94e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNST 63
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET 386
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-162 |
2.16e-11 |
|
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: 62.24 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYnSTDIrddydSFAADLLFIGHKTGVNQQL--SAYENVQH 97
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH-SGRI-----SFSPQTSWIMPGTIKDNIIfgLSYDEYRY 518
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 98 WLMVHGAQADEEevYTLLAKLGLIGLEDVPVrTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:TIGR01271 519 TSVIKACQLEED--IALFPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-188 |
2.71e-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: 61.87 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 19 SLSFtlHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYnSTDIRDDYdsfaadllfIGHKTGVNQQLSAYENVQHW 98
Cdd:TIGR03719 25 SLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGIKVGY---------LPQEPQLDPTKTVRENVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 99 LM-VHGAQADEEEVYTLLA-------KL--------------GLIGLE---------------DVPVRTLSAGQQRRVAL 141
Cdd:TIGR03719 93 VAeIKDALDRFNEISAKYAepdadfdKLaaeqaelqeiidaaDAWDLDsqleiamdalrcppwDADVTKLSGGERRRVAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2030133830 142 VRLWLNQAKLWVLDEPFTALDKKGVAMLqtqfQSHL-DKGGAILLTTH 188
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWL----ERHLqEYPGTVVAVTH 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-162 |
2.87e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 4 IDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFIghk 82
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 83 tgvNQQLSAYENVQHWLMV-------HGA-----QADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAK 150
Cdd:PRK10575 91 ---PQQLPAAEGMTVRELVaigrypwHGAlgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170
....*....|..
gi 2030133830 151 LWVLDEPFTALD 162
Cdd:PRK10575 168 CLLLDEPTSALD 179
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-164 |
3.44e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsfaadllFIGHKT---GVN-------- 86
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG----------LPGHQIarmGVVrtfqhvrl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 87 -QQLSAYENV---QHWLM----VHG---------AQADE-EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQ 148
Cdd:PRK11300 92 fREMTVIENLlvaQHQQLktglFSGllktpafrrAESEAlDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170
....*....|....*.
gi 2030133830 149 AKLWVLDEPFTALDKK 164
Cdd:PRK11300 172 PEILMLDEPAAGLNPK 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-188 |
3.88e-11 |
|
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: 59.85 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFA--RADEGQIRYNSTDIRDdydsfaadllfi 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 ghktgvnqqLSAYENvqhwlmvhgaqadeeevytllAKLGlIGL-----EDVP-VRT----------LSAGQQRRVALVR 143
Cdd:cd03217 69 ---------LPPEER---------------------ARLG-IFLafqypPEIPgVKNadflryvnegFSGGEKKRNEILQ 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2030133830 144 LWLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-188 |
4.01e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARAD--EGQIRYNSTDIRD-DYDSFAADLL 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDlEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 78 FIGHK-----TGVNQQ---LSAYENVQHWLMVhgAQADEEEVYTLLA-KLGLIGLEDVPV-RTL----SAGQQRRVALVR 143
Cdd:CHL00131 87 FLAFQypieiPGVSNAdflRLAYNSKRKFQGL--PELDPLEFLEIINeKLKLVGMDPSFLsRNVnegfSGGEKKRNEILQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2030133830 144 LWLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-191 |
4.41e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFA--RADEGQIRYNSTDIrddydsfaadllfighktgvNQQLSAYE 93
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF--------------------GREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 NVqhwlmvhgaqADEEEVYTLLAKLGLIGLEDV-----PVRTLSAGQQRRVALVRLWLNQAKLWVLDEpFTA-LDKKGVA 167
Cdd:COG2401 105 AI----------GRKGDFKDAVELLNAVGLSDAvlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDRQTAK 173
|
170 180
....*....|....*....|....*.
gi 2030133830 168 MLQTQFQSHLDKGG--AILLTTHQDL 191
Cdd:COG2401 174 RVARNLQKLARRAGitLVVATHHYDV 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-162 |
5.46e-11 |
|
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: 60.11 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHA-------GQIMQIEGPNGAGKTSLLRIIAGFARADEGQ-------IRYNSTDIRDDYDSFAADLLFigHKTGVN 86
Cdd:cd03237 12 EFTLEVeggsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDieieldtVSYKPQYIKADYEGTVRDLLS--SITKDF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 87 QQLSAYENvqhwlmvhgaqadeeevyTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03237 90 YTHPYFKT------------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-188 |
6.26e-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: 59.79 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddyDSFAADLLFIGHKTGVNQQLSAYENVqh 97
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRMVVFQNYSLLPWLTVRENI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 98 WLMVHGAQAD------EEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkkgvAMLQT 171
Cdd:TIGR01184 76 ALAVDRVLPDlskserRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD----ALTRG 151
|
170 180
....*....|....*....|..
gi 2030133830 172 QFQSHL-----DKGGAILLTTH 188
Cdd:TIGR01184 152 NLQEELmqiweEHRVTVLMVTH 173
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-188 |
7.30e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGHKTG-VNQQ--- 88
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGmVFQQpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 ---LSAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGLE-------DVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:PRK14246 102 fphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWkevydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190
....*....|....*....|....*....|...
gi 2030133830 159 TALD---KKGVAMLQTQFQSHLdkggAILLTTH 188
Cdd:PRK14246 182 SMIDivnSQAIEKLITELKNEI----AIVIVSH 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-196 |
7.96e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.75 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQ------DRCLFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNstDIRDDYDSFAA 74
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfaSRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 75 DLLFIGHKTGVNQQLSAYENVQHWLM---VHGAQ----ADEEEVYTLLAKLGLIGL-----EDVPVRtLSAGQQRRVALV 142
Cdd:PRK13643 78 EIKPVRKKVGVVFQFPESQLFEETVLkdvAFGPQnfgiPKEKAEKIAAEKLEMVGLadefwEKSPFE-LSGGQMRRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 143 RLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTH-QDLTAHFA 196
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYA 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-185 |
8.70e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI--RDDYDSFAA-----------DLLFIGHKTG 84
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGLANgivyisedrkrDGLVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 85 VNQQLSAYENVQHwLMVHGAQADEEEVYTLLAKLGLIGL--EDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:PRK10762 349 ENMSLTALRYFSR-AGGSLKHADEQQAVSDFIRLFNIKTpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180
....*....|....*....|....*.
gi 2030133830 163 ---KKGVAMLQTQFQShldKGGAILL 185
Cdd:PRK10762 428 vgaKKEIYQLINQFKA---EGLSIIL 450
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-162 |
9.77e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAG------------FARAD---------EGQIRYNSTDIRDDY-- 69
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlFGRRRgsgetiwdiKKHIGYVSSSLHLDYrv 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 70 DSFAADLLFIGH--KTGVNQQLSayeNVQHWLmvhgaqADEeevytLLAKLGLIG-LEDVPVRTLSAGQQRRVALVRLWL 146
Cdd:PRK10938 352 STSVRNVILSGFfdSIGIYQAVS---DRQQKL------AQQ-----WLDILGIDKrTADAPFHSLSWGQQRLALIVRALV 417
|
170
....*....|....*.
gi 2030133830 147 NQAKLWVLDEPFTALD 162
Cdd:PRK10938 418 KHPTLLILDEPLQGLD 433
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
16-162 |
1.33e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQ--IRYNSTDIRDDYDSFAADLLfiGHKTG-VNQQ---- 88
Cdd:COG4161 18 LFD-INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlnIAGHQFDFSQKPSEKAIRLL--RQKVGmVFQQynlw 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030133830 89 --LSAYENVQH---WLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:COG4161 95 phLTVMENLIEapcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
18-162 |
1.58e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.32 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDSfaADLLFIGHKTG-VNQQ---LS--- 90
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSE--RELRAARRKIGmIFQHfnlLSsrt 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2030133830 91 AYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRV----ALVrlwlNQAKLWVLDEPFTALD 162
Cdd:COG1135 99 VAENVALPLEIAGVPKAEirKRVAELLELVGLSDKADAYPSQLSGGQKQRVgiarALA----NNPKVLLCDEATSALD 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-188 |
2.24e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNsTDI----------RDD----YDSFA------AD 75
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivarlqqdppRNVegtvYDFVAegieeqAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 76 LL----FIGHKTGVNQQ---LSAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGleDVPVRTLSAGQQRRVALVRLWLNQ 148
Cdd:PRK11147 97 YLkryhDISHLVETDPSeknLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2030133830 149 AKLWVLDEPFTALDKKGVAMLQtQFQshLDKGGAILLTTH 188
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLE-GFL--KTFQGSIIFISH 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-188 |
2.25e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.90 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLfiGHKTGVNQQL-------SAY 92
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR--NQKLGFIYQFhhllpdfTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 93 ENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGV-AML 169
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEinSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAdSIF 185
|
170
....*....|....*....
gi 2030133830 170 QTQFQSHLDKGGAILLTTH 188
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTH 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-194 |
2.67e-10 |
|
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: 59.07 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAG-FARAD-EGQIRYNSTDI--RDDYDSFAADL 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTwDGEIYWSGSPLkaSNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 LFIGHKTGVNQQLSAYENV--QHWLMVHGAQADEEEVY----TLLAKLGLIGLEDV-PVRTLSAGQQRRVALVRLWLNQA 149
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIflGNEITLPGGRMAYNAMYlrakNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2030133830 150 KLWVLDEPFTALDKKgvamlQTQfqshldkggaILLTTHQDLTAH 194
Cdd:TIGR02633 161 RLLILDEPSSSLTEK-----ETE----------ILLDIIRDLKAH 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-162 |
2.86e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 17 FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTD--IRDDYDSFAADLLFIgHKT----------- 83
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqLRDLYALSEAERRRL-LRTewgfvhqhprd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 84 GVNQQLSAYENVQHWLMVHG--------AQADE--EEVytllaKLGLIGLEDVPvRTLSAGQQRRVALVRLWLNQAKLWV 153
Cdd:PRK11701 101 GLRMQVSAGGNIGERLMAVGarhygdirATAGDwlERV-----EIDAARIDDLP-TTFSGGMQQRLQIARNLVTHPRLVF 174
|
....*....
gi 2030133830 154 LDEPFTALD 162
Cdd:PRK11701 175 MDEPTGGLD 183
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-189 |
3.76e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGHK--------TGVNQQ--- 88
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQlrllrtrlTMVFQHfnl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 ---LSAYENVQ----HWLMVHGAQADEEEVYtLLAKLGLIGLEDV--PVRtLSAGQQRRVALVRLWLNQAKLWVLDEPFT 159
Cdd:PRK10619 104 wshMTVLENVMeapiQVLGLSKQEARERAVK-YLAKVGIDERAQGkyPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190
....*....|....*....|....*....|
gi 2030133830 160 ALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:PRK10619 182 ALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-162 |
6.81e-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: 56.85 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADL--------LF---IG 80
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIgvvpqdtvLFndtIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTgvnqqlsAYENVqhwlmvhgaQADEEEVYTlLAKLGLI-----GLED-----VPVR--TLSAGQQRRVALVRLWLNQ 148
Cdd:cd03253 93 YNI-------RYGRP---------DATDEEVIE-AAKAAQIhdkimRFPDgydtiVGERglKLSGGEKQRVAIARAILKN 155
|
170
....*....|....
gi 2030133830 149 AKLWVLDEPFTALD 162
Cdd:cd03253 156 PPILLLDEATSALD 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-188 |
6.95e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 34 GPNGAGKTSLLRIIAGFARADEGQIRynstdirddydsfAADllfiGHKTGVNQQ-------LSAYENVQHWLM-VHGAQ 105
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEGEAR-------------PAP----GIKVGYLPQepqldpeKTVRENVEEGVAeVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 106 ADEEEVYTLLA--------------KL-------GLIGLE---------------DVPVRTLSAGQQRRVALVRLWLNQA 149
Cdd:PRK11819 103 DRFNEIYAAYAepdadfdalaaeqgELqeiidaaDAWDLDsqleiamdalrcppwDAKVTKLSGGERRRVALCRLLLEKP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2030133830 150 KLWVLDEPFTALDKKGVAMLqtqfQSHL-DKGGAILLTTH 188
Cdd:PRK11819 183 DMLLLDEPTNHLDAESVAWL----EQFLhDYPGTVVAVTH 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-162 |
9.23e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIrynstDIRDDYDSFAA-----DLLFIGHKTG-VNQQ- 88
Cdd:PRK11124 18 LFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----NIAGNHFDFSKtpsdkAIRELRRNVGmVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 -----LSAYENVQHWLM-VHG-------AQADEeevytLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLD 155
Cdd:PRK11124 92 nlwphLTVQQNLIEAPCrVLGlskdqalARAEK-----LLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
....*..
gi 2030133830 156 EPFTALD 162
Cdd:PRK11124 167 EPTAALD 173
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-197 |
9.40e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.67 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRddydsfAADLLFIGHKTGV-----NQQL--- 89
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN------AENEKWVRSKVGLvfqdpDDQVfss 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 SAYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVA 167
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEveRRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 168 MLQTQFQSHLDKGGAILLTTHQ-DLTAHFAQ 197
Cdd:PRK13647 176 TLMEILDRLHNQGKTVIVATHDvDLAAEWAD 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-162 |
1.01e-09 |
|
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: 57.10 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 23 TLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQ------IRYNSTDIRDDYDSFAADLLFIGHKTGVNqqlSAYENVQ 96
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedlkISYKPQYISPDYDGTVEEFLRSANTDDFG---SSYYKTE 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 97 hwlmvhgaqadeeevytLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:COG1245 439 -----------------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-170 |
1.09e-09 |
|
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: 56.08 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRdDYD------SFAA----DLLFIGhktgvnqql 89
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISrkslrsMIGVvlqdTFLFSG--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 SAYENVQhwlmVHGAQADEEEVYTLLAKLGLI--------GLEDVPV---RTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:cd03254 92 TIMENIR----LGRPNATDEEVIEAAKEAGAHdfimklpnGYDTVLGengGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170
....*....|..
gi 2030133830 159 TALDKKGVAMLQ 170
Cdd:cd03254 168 SNIDTETEKLIQ 179
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-189 |
1.32e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 27 GQIMQIEGPNGAGKTSLLRIIAGFARAD---EGQIRYNSTDIrdDYDSFAA-------DLLFIGHktgvnqqLSAYENVQ 96
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI--DAKEMRAisayvqqDDLFIPT-------LTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 97 ---HWLMVHGAQADE--EEVYTLLAKLGL-------IGLEDvPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK 164
Cdd:TIGR00955 122 fqaHLRMPRRVTKKEkrERVDEVLQALGLrkcantrIGVPG-RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180
....*....|....*....|....*
gi 2030133830 165 GVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQ 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-193 |
1.77e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 27 GQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI-RDDYDSFAA----DLLFIGHKTGVNQQLSAYENVQHWLMV 101
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhQMDEEARAKlrakHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 102 HGAQADE--EEVYTLLAKLGL-IGLEDVPVRtLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK-GVAMLQTQFQSHL 177
Cdd:PRK10584 116 RGESSRQsrNGAKALLEQLGLgKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQtGDKIADLLFSLNR 194
|
170
....*....|....*.
gi 2030133830 178 DKGGAILLTTHQDLTA 193
Cdd:PRK10584 195 EHGTTLILVTHDLQLA 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-189 |
1.82e-09 |
|
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: 55.17 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYN-------------STDIRDDydsfaadLLFiGHK 82
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPgsiayvsqepwiqNGTIREN-------ILF-GKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 83 tgVNQQLsaYENVQHW--------LMVHGaqaDEEEVytllaklGLIGLedvpvrTLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:cd03250 92 --FDEER--YEKVIKAcalepdleILPDG---DLTEI-------GEKGI------NLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 2030133830 155 DEPFTALDKK-GVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:cd03250 152 DDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-161 |
4.38e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRY--NSTDIRDDYDSFAADLLFIGHKTGVNQQLSAYENV 95
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAENI 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2030133830 96 ------------QHWLMVHgAQADEeevytLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:PRK10762 101 flgrefvnrfgrIDWKKMY-AEADK-----LLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-162 |
5.32e-09 |
|
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: 55.22 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTC---TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAG-FARADEGQIRYNS--TDIRDDYDSFAA 74
Cdd:TIGR02633 257 ILEARNLTCwdvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGkpVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 75 DLLFIGH---KTGVNQQLSAYENVQ-------HWLMVHGAQADEEEVYTLLAKLGLIGLE-DVPVRTLSAGQQRRVALVR 143
Cdd:TIGR02633 337 GIAMVPEdrkRHGIVPILGVGKNITlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAK 416
|
170
....*....|....*....
gi 2030133830 144 LWLNQAKLWVLDEPFTALD 162
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVD 435
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-157 |
6.38e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDS--FAADLLF 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHKTGVNQQLSAYENvqhwLMVHGAQADEEE-------VYTLLAKLgligLEDVPVR--TLSAGQQRRVALVRLWLNQA 149
Cdd:PRK11614 85 VPEGRRVFSRMTVEEN----LAMGGFFAERDQfqerikwVYELFPRL----HERRIQRagTMSGGEQQMLAIGRALMSQP 156
|
....*...
gi 2030133830 150 KLWVLDEP 157
Cdd:PRK11614 157 RLLLLDEP 164
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-188 |
7.73e-09 |
|
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: 55.02 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGHKTGVNQQLSAYENVQH 97
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 98 WLMVHGAQADEEEVYT--LLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQS 175
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVAnwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170
....*....|...
gi 2030133830 176 HLDKGGAILLTTH 188
Cdd:TIGR01257 2116 IIREGRAVVLTSH 2128
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-188 |
8.76e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 19 SLSFTLHAGQIMQIEGPNGAGKTSLLRIIAgfaRADE--------GQIRYNSTDIRddydSFAADLLFIGHKTG-VNQQ- 88
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSIN---RMNDlnpevtitGSIVYNGHNIY----SPRTDTVDLRKEIGmVFQQp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 ----LSAYENVQHWLMVHGAQadEEEVYTLLAKLGLIGL---EDVPVR------TLSAGQQRRVALVRLWLNQAKLWVLD 155
Cdd:PRK14239 96 npfpMSIYENVVYGLRLKGIK--DKQVLDEAVEKSLKGAsiwDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|...
gi 2030133830 156 EPFTALDKKGVAMLQTQFQShLDKGGAILLTTH 188
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLG-LKDDYTMLLVTR 205
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-190 |
8.89e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIrYNSTDIR---------DDYDSFAADLLFIGHktgvn 86
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRmavfsqhhvDGLDLSSNPLLYMMR----- 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 87 qqlsAYENVQhwlmvhgaqadEEEVYTLLAKLGLIG-LEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKG 165
Cdd:PLN03073 598 ----CFPGVP-----------EQKLRAHLGSFGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
170 180
....*....|....*....|....*...
gi 2030133830 166 V-AMLQ--TQFQshldkgGAILLTTHQD 190
Cdd:PLN03073 663 VeALIQglVLFQ------GGVLMVSHDE 684
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-192 |
9.22e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNS--------TDIRDDY--------DSFAADLLFIGH 81
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitddnfEKLRKHIgivfqnpdNQFVGSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 KTGVNQQLSAYENVQhwlmvhgaqadeEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:PRK13648 106 AFGLENHAVPYDEMH------------RRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190
....*....|....*....|....*....|..
gi 2030133830 162 DKKGVAMLQTQFQS-HLDKGGAILLTTHqDLT 192
Cdd:PRK13648 174 DPDARQNLLDLVRKvKSEHNITIISITH-DLS 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-162 |
1.25e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQI--------RYNSTDIRDDYDSFAADLLFIGHKTgvNQQL 89
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqHYASKEVARRIGLLAQNATTPGDIT--VQEL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2030133830 90 SAYENVQHW-LMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:PRK10253 102 VARGRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-196 |
1.26e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.49 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDsLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDsfAADLLFIGHKTGVNQQLSaye 93
Cdd:PRK13634 21 RALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK--NKKLKPLRKKVGIVFQFP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 nvQHWLMVHGAQAD-----------EEEVYTLLAK-LGLIGL-EDVPVRT---LSAGQQRRVALVRLWLNQAKLWVLDEP 157
Cdd:PRK13634 95 --EHQLFEETVEKDicfgpmnfgvsEEDAKQKAREmIELVGLpEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2030133830 158 FTALDKKG-VAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFA 196
Cdd:PRK13634 173 TAGLDPKGrKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYA 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-197 |
1.39e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.15 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI----RDDYDSFAAD--LLFIGHKT 83
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDiqMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 84 GVNQQLSA----YENVQHWLMVHGAqADEEEVYTLLAKLGL-IGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:PRK10419 101 AVNPRKTVreiiREPLRHLLSLDKA-ERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2030133830 159 TALDKkgvaMLQTQFQSHLDK-----GGAILLTTHQ-DLTAHFAQ 197
Cdd:PRK10419 180 SNLDL----VLQAGVIRLLKKlqqqfGTACLFITHDlRLVERFCQ 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-188 |
2.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 29 IMQIEGPNGAGKTSLLRIiagFARADE--GQIRYNSTDIRDDYDSFAADLLFIGHKTGVNQQ-------LSAYENVQHWL 99
Cdd:PRK14247 31 ITALMGPSGSGKSTLLRV---FNRLIElyPEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpipnLSIFENVALGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 100 ----MVHGAQADEEEVYTLLAKLGLigLEDV------PVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAML 169
Cdd:PRK14247 108 klnrLVKSKKELQERVRWALEKAQL--WDEVkdrldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170
....*....|....*....
gi 2030133830 170 QTQFQsHLDKGGAILLTTH 188
Cdd:PRK14247 186 ESLFL-ELKKDMTIVLVTH 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-196 |
2.94e-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: 52.36 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARA---DEGQIRYNSTDIRD-------DY----------DSFAA-DL 76
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekelrKIrgreiqmifqDPMTSlNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 77 LF-IGhktgvnQQLSayENVQHWLMVHGAQAdEEEVYTLLAKLGLigleDVPVRT-------LSAGQQRRVALVRLWLNQ 148
Cdd:COG0444 102 VMtVG------DQIA--EPLRIHGGLSKAEA-RERAIELLERVGL----PDPERRldrypheLSGGMRQRVMIARALALE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 149 AKLWVLDEPFTALDkkgvAMLQTQFQSHLDK-----GGAILLTTHqDLT--AHFA 196
Cdd:COG0444 169 PKLLIADEPTTALD----VTIQAQILNLLKDlqrelGLAILFITH-DLGvvAEIA 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-162 |
4.08e-08 |
|
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: 51.85 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFighktgVNQQL-----SA 91
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL------VSQDVflfndTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 YENVqhwlmVHGA-QADEEEVYTlLAKLG-----LIGLED-----VPVR--TLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:cd03251 93 AENI-----AYGRpGATREEVEE-AARAAnahefIMELPEgydtvIGERgvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
....
gi 2030133830 159 TALD 162
Cdd:cd03251 167 SALD 170
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-188 |
4.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.97 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfAADLLFIGHKTGVNQQLSAYenvqh 97
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK----KVKLSDIRKKVGLVFQYPEY----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 98 wlmvhgaQADEEEVYTLLA----KLGL---------------IGL--EDVPVRT---LSAGQQRRVALVRLWLNQAKLWV 153
Cdd:PRK13637 95 -------QLFEETIEKDIAfgpiNLGLseeeienrvkramniVGLdyEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 2030133830 154 LDEPFTALDKKGVAMLQTQFQS-HLDKGGAILLTTH 188
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKElHKEYNMTIILVSH 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-191 |
5.85e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDD-----YDSFAADLLF-------------I 79
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkeKEKVLEKLVIqktrfkkikkikeI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTGVNQQLSAYENVQHWL---MVHGAQA---DEEEVYTLLAK-LGLIGL-EDVPVRT---LSAGQQRRVALVRLWLNQ 148
Cdd:PRK13651 104 RRRVGVVFQFAEYQLFEQTIekdIIFGPVSmgvSKEEAKKRAAKyIELVGLdESYLQRSpfeLSGGQKRRVALAGILAME 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2030133830 149 AKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHqDL 191
Cdd:PRK13651 184 PDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH-DL 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-188 |
7.29e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIrynstDIRDdydsfAADLLFIGhkTGVNQQLSAYENVQ- 96
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG-----SAALIAIS--SGLNGQLTGIENIEl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 97 HWLMVHGAQADEEEVYTLLAKLGLIG-LEDVPVRTLSAGQQRRVAL-VRLWLNQAKLwVLDEPFTALDKKGVAMLQTQFQ 174
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGkFIYQPVKTYSSGMKSRLGFaISVHINPDIL-VIDEALSVGDQTFTKKCLDKMN 187
|
170
....*....|....
gi 2030133830 175 SHLDKGGAILLTTH 188
Cdd:PRK13545 188 EFKEQGKTIFFISH 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-157 |
7.93e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTC---TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAG-FARADEGQIRYNS--TDIRDDYDSFAA 74
Cdd:PRK13549 259 ILEVRNLTAwdpVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGkpVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 75 D---------------LLFIGHktgvNQQLSAYENVQHWLMVHGAqADEEEVYTLLAKLGL-IGLEDVPVRTLSAGQQRR 138
Cdd:PRK13549 339 GiamvpedrkrdgivpVMGVGK----NITLAALDRFTGGSRIDDA-AELKTILESIQRLKVkTASPELAIARLSGGNQQK 413
|
170
....*....|....*....
gi 2030133830 139 VALVRLWLNQAKLWVLDEP 157
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEP 432
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-162 |
8.84e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 19 SLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQI------------RYNSTDIRddydsfaadLLFIGHKTGVN 86
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdySYRSQRIR---------MIFQDPSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 87 --QQLSAYENVQHWLMVH-GAQADEEEVYTLLAKLGLigLEDVPV---RTLSAGQQRRVALVRLWLNQAKLWVLDEPFTA 160
Cdd:PRK15112 102 prQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGL--LPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
..
gi 2030133830 161 LD 162
Cdd:PRK15112 180 LD 181
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-205 |
9.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSfaADLLFIGHKTGVNQQLS------- 90
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGN--KNLKKLRKKVSLVFQFPeaqlfen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 -AYENVQHWLMVHGAQADEEEVYTL--LAKLGLIglEDVPVRT---LSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKK 164
Cdd:PRK13641 102 tVLKDVEFGPKNFGFSEDEAKEKALkwLKKVGLS--EDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2030133830 165 GVAMLQTQFQSHLDKGGAILLTTHQ-DLTAHFAQlQTLALEY 205
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYAD-DVLVLEH 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-189 |
1.04e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 51.26 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRdDYDSFaadllFIGHKTGVNQQL 89
Cdd:TIGR00958 490 NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHH-----YLHRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 ------SAYENVQHWLmvhgAQADEEEVyTLLAKLG----LIGLEDVPVRT--------LSAGQQRRVALVRLWLNQAKL 151
Cdd:TIGR00958 564 pvlfsgSVRENIAYGL----TDTPDEEI-MAAAKAAnahdFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190
....*....|....*....|....*....|....*...
gi 2030133830 152 WVLDEPFTALDkkgVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:TIGR00958 639 LILDEATSALD---AECEQLLQESRSRASRTVLLIAHR 673
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-162 |
1.52e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 24 LHAGQIMQIEGPNGAGKTSLLRIIA----GFARADEGQIRYNSTDIRDDYDSFAADLLFIGhKTGVN-QQLSAYENVQHW 98
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNA-ETDVHfPHLTVGETLDFA 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030133830 99 LMVHGAQAD----EEEVYT------LLAKLGLIGLEDVPV-----RTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:TIGR00956 163 ARCKTPQNRpdgvSREEYAkhiadvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-188 |
1.59e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 19 SLSFTLHAgqIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrdDYDSFAadLLFIGHKTGV-----NQQLSAYE 93
Cdd:PRK13638 21 NLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSKRG--LLALRQQVATvfqdpEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 ---NVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:PRK13638 95 idsDIAFSLRNLGVPEAEitRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180
....*....|....*....|
gi 2030133830 169 LQTQFQSHLDKGGAILLTTH 188
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSH 194
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-170 |
1.82e-07 |
|
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: 49.78 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD-DYDSFAADLLFIGHK----TG 84
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEpvlfAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 85 VNQQLSAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVR--TLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03248 103 SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
....*...
gi 2030133830 163 KKGVAMLQ 170
Cdd:cd03248 183 AESEQQVQ 190
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-162 |
1.82e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDaVTCTKQDRCLfdSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYD--SFAADLLF 78
Cdd:PRK11144 1 MLELN-FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IGHktgVNQ--QLSAYENVQHWL---MVHGAQADEEEVYTLLaklgliGLEDVPVR---TLSAGQQRRVALVRLWLNQAK 150
Cdd:PRK11144 78 IGY---VFQdaRLFPHYKVRGNLrygMAKSMVAQFDKIVALL------GIEPLLDRypgSLSGGEKQRVAIGRALLTAPE 148
|
170
....*....|..
gi 2030133830 151 LWVLDEPFTALD 162
Cdd:PRK11144 149 LLLMDEPLASLD 160
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-164 |
1.85e-07 |
|
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: 50.06 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHA------GQIMQIEGPNGAGKTSLLRIIAGFARADEGqiRYNSTDIRDD-YDSFAADLLFIGHKTGVNQQLSAYE 93
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWDEiLDEFRGSELQNYFTKLLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 94 NVQHWLMVHGA----------QADEEEVY-TLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03236 92 KPQYVDLIPKAvkgkvgellkKKDERGKLdELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
..
gi 2030133830 163 KK 164
Cdd:cd03236 172 IK 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-188 |
1.95e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 17 FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIrynstdIRDDYdSFAADLLFIGH------KTGVNQQLS 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT------IVGDY-AIPANLKKIKEvkrlrkEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVHGA------QADEEEVYTLLAKL-GLIGL-EDVPVRT---LSAGQQRRVALVRLWLNQAKLWVLDEPFT 159
Cdd:PRK13645 100 EYQLFQETIEKDIAfgpvnlGENKQEAYKKVPELlKLVQLpEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190
....*....|....*....|....*....|
gi 2030133830 160 ALDKKGVAMLQTQFQS-HLDKGGAILLTTH 188
Cdd:PRK13645 180 GLDPKGEEDFINLFERlNKEYKKRIIMVTH 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-189 |
2.09e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 8 TCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARAD--EGQIRYNSTDIRDDydsfaadllfIGHKTGV 85
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ----------ILKRTGF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 86 NQQ-------LSAYENVQHWLMVHGAQADEEEVYTLLA-----KLGLIGLEDVPV-----RTLSAGQQRRVALVRLWLNQ 148
Cdd:PLN03211 145 VTQddilyphLTVRETLVFCSLLRLPKSLTKQEKILVAesvisELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2030133830 149 AKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-179 |
2.58e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.03 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 34 GPNGAGKTSLLRIIAGFARADEGQirynstdirddydsfaadlLFIGH---------KTGVNQ---------QLSAYENV 95
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGD-------------------LFIGEkrmndvppaERGVGMvfqsyalypHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 96 QHWLMVHGAQADE-----EEVYTLL--AKLgligLEDVPvRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkkgvAM 168
Cdd:PRK11000 97 SFGLKLAGAKKEEinqrvNQVAEVLqlAHL----LDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD----AA 167
|
170
....*....|.
gi 2030133830 169 LQTQFQSHLDK 179
Cdd:PRK11000 168 LRVQMRIEISR 178
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-189 |
2.64e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.85 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGHK----------TGVNQ 87
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKiknfkelrrrVSMVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 88 QLSAYE----NVQHWLM-------VHGAQADEEEVYtLLAKLGLIG--LEDVPVRtLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:PRK13631 123 QFPEYQlfkdTIEKDIMfgpvalgVKKSEAKKLAKF-YLNKMGLDDsyLERSPFG-LSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190
....*....|....*....|....*....|....*
gi 2030133830 155 DEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-176 |
3.15e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 19 SLSFTLHAGQIMQIEGPNGAGKTS----LLRIIAGfaradEGQIRYNSTDIrddyDSFA-ADLLFIGHKTGV-------- 85
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPL----HNLNrRQLLPVRHRIQVvfqdpnss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 86 -NQQLSAYENVQHWLMVH----GAQADEEEVYTLLAKLGLigleDVPVR-----TLSAGQQRRVALVRLWLNQAKLWVLD 155
Cdd:PRK15134 375 lNPRLNVLQIIEEGLRVHqptlSAAQREQQVIAVMEEVGL----DPETRhrypaEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180
....*....|....*....|....*
gi 2030133830 156 EPFTALDK----KGVAMLQTQFQSH 176
Cdd:PRK15134 451 EPTSSLDKtvqaQILALLKSLQQKH 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-170 |
4.53e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAG------------FAR-------------ADEGQirYNSTDI----RDDYDS 71
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqFSHitrlsfeqlqklvSDEWQ--RNNTDMlspgEDDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 FAADLLFIGHKtgvnqqlsayenvqhwlmvhgaqaDEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKL 151
Cdd:PRK10938 101 TTAEIIQDEVK------------------------DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
|
170
....*....|....*....
gi 2030133830 152 WVLDEPFTALDKKGVAMLQ 170
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLA 175
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-185 |
5.05e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQD-RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDD--YDSFAADLLF 78
Cdd:COG3845 258 LEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLspRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 79 IG---HKTGVNQQLSAYENvqhwlMVHGAQADEEevytlLAKLGLI--------------------GLEDVPVRTLSAGQ 135
Cdd:COG3845 338 IPedrLGRGLVPDMSVAEN-----LILGRYRRPP-----FSRGGFLdrkairafaeelieefdvrtPGPDTPARSLSGGN 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2030133830 136 QRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILL 185
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-198 |
5.15e-07 |
|
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: 48.01 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 11 KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGfaRADEGQIRynstdirddydsfaADLLFIGHKTGVN-QQL 89
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT--------------GEILINGRPLDKNfQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 SAYenVQHwLMVHGAQADEEEVYTLLAKLgligledvpvRTLSAGQQRRVAL-VRLwlnQAK--LWVLDEPFTALDKKGV 166
Cdd:cd03232 81 TGY--VEQ-QDVHSPNLTVREALRFSALL----------RGLSVEQRKRLTIgVEL---AAKpsILFLDEPTSGLDSQAA 144
|
170 180 190
....*....|....*....|....*....|....*
gi 2030133830 167 AMLQTQFQSHLDKGGAILLTTHQ---DLTAHFAQL 198
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIHQpsaSIFEKFDRL 179
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-162 |
8.98e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.11 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDsLSFTLHAGQIMQIEGPNGAGKTSLLR-------IIAGfARAdEGQIRYNSTDIRDDydsfAADLLFIGHKTG-VNQ 87
Cdd:COG1117 27 LKD-INLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG-ARV-EGEILLDGEDIYDP----DVDVVELRRRVGmVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 88 Q-----LSAYENVQHWLMVHG----AQADeEEVYTLLAKLGLigLEDV------PVRTLSAGQQRRVALVRLWLNQAKLW 152
Cdd:COG1117 100 KpnpfpKSIYDNVAYGLRLHGikskSELD-EIVEESLRKAAL--WDEVkdrlkkSALGLSGGQQQRLCIARALAVEPEVL 176
|
170
....*....|
gi 2030133830 153 VLDEPFTALD 162
Cdd:COG1117 177 LMDEPTSALD 186
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-162 |
9.17e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.42 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsfaADLLFIGHKTGVNQQ------LSA 91
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT------VTRASLRRNIAVVFQdaglfnRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 YENVQhwlmVHGAQADEEEVYTLL---AKLGLI-----GLEDVP---VRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTA 160
Cdd:PRK13657 426 EDNIR----VGRPDATDEEMRAAAeraQAHDFIerkpdGYDTVVgerGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
..
gi 2030133830 161 LD 162
Cdd:PRK13657 502 LD 503
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-165 |
1.00e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.80 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 12 QDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDydsfaaDLLFIGHKTGV------ 85
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE------NVWDIRHKIGMvfqnpd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 86 NQQLSAY--ENVQHWLMVHGAqADEEEVYTLLAKLGLIGLEDV----PVRtLSAGQQRRVALVRLWLNQAKLWVLDEPFT 159
Cdd:PRK13650 92 NQFVGATveDDVAFGLENKGI-PHEEMKERVNEALELVGMQDFkerePAR-LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
....*.
gi 2030133830 160 ALDKKG 165
Cdd:PRK13650 170 MLDPEG 175
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-207 |
1.01e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGqIRYNSTDIRDDYDSFA-ADLLFIGHKTGVNQQ---- 88
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSIFNyRDVLEFRRRVGMLFQrpnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 --LSAYENVQHWLMVHGAQADEEEVYTLLAKLGLIGL--------EDVPVRtLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:PRK14271 113 fpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavkdrlSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2030133830 159 TALDKKGVAMLQTQFQSHLDKGGAILLTTHQDLTAHFAQLQTLALEYRL 207
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-196 |
1.16e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.88 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 11 KQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQI--------RYNSTDIRDdydsfaadllFIG-- 80
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitKENIREVRK----------FVGlv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 --------HKTGVNQQLsAYENVQHWLmvhgaqaDEEEV-YTLLAKLGLIGLEDVPVRT---LSAGQQRRVALVRLWLNQ 148
Cdd:PRK13652 84 fqnpddqiFSPTVEQDI-AFGPINLGL-------DEETVaHRVSSALHMLGLEELRDRVphhLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 149 AKLWVLDEPFTALDKKGVAMLqTQFQSHLDK--GGAILLTTHQ-DLTAHFA 196
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKEL-IDFLNDLPEtyGMTVIFSTHQlDLVPEMA 205
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-162 |
1.21e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 3 EIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNS---TDIRDDY---------- 69
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQLDSwrsrlavvsq 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 70 ------DSFAADLLfIGHKTGVNQQLsayENVQHWLMVHG-----AQADEEEVytllaklgliGLEDVpvrTLSAGQQRR 138
Cdd:PRK10789 397 tpflfsDTVANNIA-LGRPDATQQEI---EHVARLASVHDdilrlPQGYDTEV----------GERGV---MLSGGQKQR 459
|
170 180
....*....|....*....|....
gi 2030133830 139 VALVRLWLNQAKLWVLDEPFTALD 162
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVD 483
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
28-195 |
2.01e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.08 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 28 QIMQIEGPNGAGKTSLLR-------IIAGFaRAdEGQIRYNSTDIrddYDSfAADLLFIGHKTGVNQQL------SAYEN 94
Cdd:PRK14243 37 QITAFIGPSGCGKSTILRcfnrlndLIPGF-RV-EGKVTFHGKNL---YAP-DVDPVEVRRRIGMVFQKpnpfpkSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 95 VQHWLMVHGAQADEEE-VYTLLA----------KLGLIGLedvpvrTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDK 163
Cdd:PRK14243 111 IAYGARINGYKGDMDElVERSLRqaalwdevkdKLKQSGL------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2030133830 164 kgVAMLQTQFQSH-LDKGGAILLTTHQ--------DLTAHF 195
Cdd:PRK14243 185 --ISTLRIEELMHeLKEQYTIIIVTHNmqqaarvsDMTAFF 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-162 |
2.17e-06 |
|
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: 47.49 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRY-------NSTDIRDDYDSFAADLLFIGHktgvnQQLS 90
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKPGPDGRGRAKRYIGILH-----QEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AY------ENVQHW--LMVHGAQADEEEVYTLLAklglIGLEDVPVR--------TLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:TIGR03269 376 LYphrtvlDNLTEAigLELPDELARMKAVITLKM----VGFDEEKAEeildkypdELSEGERHRVALAQVLIKEPRIVIL 451
|
....*...
gi 2030133830 155 DEPFTALD 162
Cdd:TIGR03269 452 DEPTGTMD 459
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-197 |
2.67e-06 |
|
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: 46.99 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKT----SLLRIIAGFARADEGQIRYNSTDIRDDYDsfaADLLFI-GHKTG-------- 84
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE---RELRRIrGNRIAmifqepmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 85 -------VNQQLSayENVQHWLMVHGAQAdEEEVYTLLAklgLIGLEDVPVR------TLSAGQQRRV----ALvrlwLN 147
Cdd:COG4172 104 slnplhtIGKQIA--EVLRLHRGLSGAAA-RARALELLE---RVGIPDPERRldayphQLSGGQRQRVmiamAL----AN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030133830 148 QAKLWVLDEPFTALDkkgV----------AMLQTQFqshldkGGAILLTTHqDLT--AHFAQ 197
Cdd:COG4172 174 EPDLLIADEPTTALD---VtvqaqildllKDLQREL------GMALLLITH-DLGvvRRFAD 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-161 |
3.98e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGF--ARADEGQIRYNST-----DIRddyDSFAADLLFIGHKTGVNQQLS 90
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEvcrfkDIR---DSEALGIVIIHQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYEN-----------VQHWLMVHgAQADEeevytLLAKLGLIGLEDVPVRTLSAGQQRRV----ALVRlwlnQAKLWVLD 155
Cdd:NF040905 95 IAENiflgnerakrgVIDWNETN-RRARE-----LLAKVGLDESPDTLVTDIGVGKQQLVeiakALSK----DVKLLILD 164
|
....*.
gi 2030133830 156 EPFTAL 161
Cdd:NF040905 165 EPTAAL 170
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-191 |
4.00e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.26 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKT----SLLRIIAGFARAdEGQIRYNSTDI----RDDYDSFAAD---LLFIGHKTGVNQQ 88
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREIlnlpEKELNKLRAEqisMIFQDPMTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 LSAYENVQHWLMVH----GAQADEEEVYTLLA--------KLGLIGLEdvpvrtLSAGQQRRVALVRLWLNQAKLWVLDE 156
Cdd:PRK09473 114 MRVGEQLMEVLMLHkgmsKAEAFEESVRMLDAvkmpearkRMKMYPHE------FSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2030133830 157 PFTALDkkgvAMLQTQFQSHLDK-----GGAILLTTHqDL 191
Cdd:PRK09473 188 PTTALD----VTVQAQIMTLLNElkrefNTAIIMITH-DL 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-179 |
4.12e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.57 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAAD-----LLFIGHKTGVNQQLSAYENV 95
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 96 QHWLMVHGAQADEEEVYTLLAkLGLIGLEDVP---VRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDkkgvAMLQTQ 172
Cdd:PRK10070 128 AFGMELAGINAEERREKALDA-LRQVGLENYAhsyPDELSGGMRQRVGLARALAINPDILLMDEAFSALD----PLIRTE 202
|
....*..
gi 2030133830 173 FQSHLDK 179
Cdd:PRK10070 203 MQDELVK 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-188 |
4.40e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 3 EIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYnSTDIRDDY-DSFAADLlfigh 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYfDQHRAEL----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 82 ktgvNQQLSAYENV---QHWLMVHGAqadEEEVytllakLGLigLED---------VPVRTLSAGQQRRVALVRLWLNQA 149
Cdd:PRK11147 395 ----DPEKTVMDNLaegKQEVMVNGR---PRHV------LGY--LQDflfhpkramTPVKALSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2030133830 150 KLWVLDEPFTALDKKGVAMLQ---TQFQshldkgGAILLTTH 188
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLEellDSYQ------GTVLLVSH 495
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-189 |
4.63e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrDDYDSFAADLLFIG---HKTGVNQQLSAYEN 94
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-NKLDHKLAAQLGIGiiyQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 95 -------VQHWLMVHGAQADEEEVYT--LLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKG 165
Cdd:PRK09700 101 lyigrhlTKKVCGVNIIDWREMRVRAamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
|
170 180
....*....|....*....|....
gi 2030133830 166 VAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:PRK09700 181 VDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
14-163 |
5.16e-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: 45.29 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGqIMQIEGPNGAGKTSLLRII--AGFARADegqiryNSTDIRDDYDSFAA--------DLLF---IG 80
Cdd:cd03240 10 RSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEALkyALTGELP------PNSKGGAHDPKLIRegevraqvKLAFenaNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 HKTGVNQQLSAYENVqhwLMVHgaqadEEEVYTLLAKlgligledvPVRTLSAGQQRRVALV-RLWLNQA-----KLWVL 154
Cdd:cd03240 83 KKYTITRSLAILENV---IFCH-----QGESNWPLLD---------MRGRCSGGEKVLASLIiRLALAETfgsncGILAL 145
|
....*....
gi 2030133830 155 DEPFTALDK 163
Cdd:cd03240 146 DEPTTNLDE 154
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-162 |
5.56e-06 |
|
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: 46.22 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSL----LRIIAGfaradEGQIRYNSTDIR-------------------DDYDSFaa 74
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDglsrralrplrrrmqvvfqDPFGSL-- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 75 dllfighktgvNQQLSAYENVQHWLMVHGAQADEEE----VYTLLAKLGLigleDVPVRT-----LSAGQQRRVALVRLW 145
Cdd:COG4172 376 -----------SPRMTVGQIIAEGLRVHGPGLSAAErrarVAEALEEVGL----DPAARHrypheFSGGQRQRIAIARAL 440
|
170
....*....|....*..
gi 2030133830 146 LNQAKLWVLDEPFTALD 162
Cdd:COG4172 441 ILEPKLLVLDEPTSALD 457
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-162 |
6.10e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.95 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIrddyDSF-AADLLFIGHKTGVNQQ----LS-- 90
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDL----TALsEKELRKARRQIGMIFQhfnlLSsr 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 91 -AYENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:PRK11153 98 tVFDNVALPLELAGTPKAEikARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-168 |
6.51e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRynstdirddydsfaadllfIGHKTgVNQ------------ 87
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW-------------------IGGRV-VNElepadrdiamvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 88 -------QLSAYENVQHWLMVHG-AQADEEEVYTLLAK-LGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:PRK11650 83 qnyalypHMSVRENMAYGLKIRGmPKAEIEERVAEAARiLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170
....*....|.
gi 2030133830 159 TALDKK-GVAM 168
Cdd:PRK11650 163 SNLDAKlRVQM 173
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-162 |
6.98e-06 |
|
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: 44.95 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARAD---EGQIRYNSTDIRDDYDSFAADLLFighktgVNQQlsay 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIY------VSEE---- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 93 envqhwlMVHGAQADEEEvyTLLAKLGLIGleDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALD 162
Cdd:cd03233 92 -------DVHFPTLTVRE--TLDFALRCKG--NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-162 |
1.05e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGfARA-DEGQIRYNSTDIRDDydsfaadllfiGHKTGVNQQ-------- 88
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG-ARKiQQGRVEVLGGDMADA-----------RHRRAVCPRiaympqgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 -------LSAYENVQHW--LMVHGAQADEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRV----ALVrlwlNQAKLWVLD 155
Cdd:NF033858 86 gknlyptLSVFENLDFFgrLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLglccALI----HDPDLLILD 161
|
....*..
gi 2030133830 156 EPFTALD 162
Cdd:NF033858 162 EPTTGVD 168
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-165 |
1.75e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 44.24 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 12 QDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDD--YDsfaadllfIGHKTGV---- 85
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvWD--------VRRQVGMvfqn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 86 --NQQLSAY--ENVQHWLMVHGAQADE--EEVYTLLAKLGLIG-LEDVPVRtLSAGQQRRVALVRLWLNQAKLWVLDEPF 158
Cdd:PRK13635 90 pdNQFVGATvqDDVAFGLENIGVPREEmvERVDQALRQVGMEDfLNREPHR-LSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
....*..
gi 2030133830 159 TALDKKG 165
Cdd:PRK13635 169 SMLDPRG 175
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-67 |
1.79e-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: 44.81 E-value: 1.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 13 DRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRD 67
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD 424
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-162 |
1.92e-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: 44.90 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFArADEGQIR-----YNSTDIRDDYDSFAA--DLLFIGHK 82
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQidgvsWNSVTLQTWRKAFGVipQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 83 TgVNQQLSAYEnvqhwlmvhgaQADEEEVYTLLAKLGLIG-LEDVPVR----------TLSAGQQRRVALVRLWLNQAKL 151
Cdd:TIGR01271 1307 T-FRKNLDPYE-----------QWSDEEIWKVAEEVGLKSvIEQFPDKldfvlvdggyVLSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|.
gi 2030133830 152 WVLDEPFTALD 162
Cdd:TIGR01271 1375 LLLDEPSAHLD 1385
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-156 |
2.02e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI----RDDYDS-FAA---DL-LFighktgvnqqls 90
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqPEDYRKlFSAvftDFhLF------------ 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2030133830 91 ayenvQHWLMVHGAQADEEEVYTLLAKLGL---IGLEDVPVRT--LSAGQQRRVALVRLWLNQAKLWVLDE 156
Cdd:PRK10522 410 -----DQLLGPEGKPANPALVEKWLERLKMahkLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-175 |
2.02e-05 |
|
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: 44.55 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 20 LSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNST--------DIRDDYDSFAAD-LLFIGHKTGVNQQLS 90
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLniakiglhDLRFKITIIPQDpVLFSGSLRMNLDPFS 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVHGAQAdEEEVYTLLAKLGLIGLEDVpvRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQ 170
Cdd:TIGR00957 1385 QYSDEEVWWALELAHL-KTFVSALPDKLDHECAEGG--ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
....*....
gi 2030133830 171 ----TQFQS 175
Cdd:TIGR00957 1462 stirTQFED 1470
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-191 |
3.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.54 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 17 FDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRddydsfAADLLFIGHKTGV------NQQLS 90
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT------AENVWNLRRKIGMvfqnpdNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 A-YENVQHWLMVHGAQADEEEVYTLLAKLGLIGLEDVPVRT---LSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGV 166
Cdd:PRK13642 97 AtVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREparLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180
....*....|....*....|....*
gi 2030133830 167 AMLQTQFQSHLDKGGAILLTTHQDL 191
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDL 201
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-162 |
3.55e-05 |
|
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: 43.30 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsfaADLLFIGHKTGVNQQ- 88
Cdd:cd03249 12 SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD------LNLRWLRSQIGLVSQe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 -----LSAYENVQhwLMVHGAQADEEEVYTLLAKLG--LIGLED-----VPVR--TLSAGQQRRVALVRLWLNQAKLWVL 154
Cdd:cd03249 86 pvlfdGTIAENIR--YGKPDATDEEVEEAAKKANIHdfIMSLPDgydtlVGERgsQLSGGQKQRIAIARALLRNPKILLL 163
|
....*...
gi 2030133830 155 DEPFTALD 162
Cdd:cd03249 164 DEATSALD 171
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-179 |
4.22e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 5 DAVTCTKQDRCLF--DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNstdirddydsfaADLLFIGHK 82
Cdd:PRK13546 26 DALIPKHKNKTFFalDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN------------GEVSVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 83 TGVNQQLSAYENVQHWLMVHGAQadEEEVYTLLAKlgLIGLEDV------PVRTLSAGQQRRVAL-VRLWLNQAKLwVLD 155
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGFK--RKEIKAMTPK--IIEFSELgefiyqPVKKYSSGMRAKLGFsINITVNPDIL-VID 168
|
170 180
....*....|....*....|....
gi 2030133830 156 EPFTALDkkgvamlQTQFQSHLDK 179
Cdd:PRK13546 169 EALSVGD-------QTFAQKCLDK 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-189 |
4.50e-05 |
|
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: 42.78 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI--------RDDYDSFAAD-LLFIGhktGVNQQ 88
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstipledlRSSLTIIPQDpTLFSG---TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 89 LSAYEnvqhwlmvhgaQADEEEVYTLLaKLGLIGLedvpvrTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAM 168
Cdd:cd03369 102 LDPFD-----------EYSDEEIYGAL-RVSEGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180
....*....|....*....|.
gi 2030133830 169 LQTQFQSHLdKGGAILLTTHQ 189
Cdd:cd03369 164 IQKTIREEF-TNSTILTIAHR 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-162 |
5.32e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAG--FARADEGQIRYNStDIRDDYDSFAA-DLL 77
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTG-DVTLNGEPLAAiDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 78 FIGHKTGVNQQ-------LSAYENVQHWLMVHGAQA------DEEEVYTLLAKLGLIGLEDVPVRTLSAGQQRRV----A 140
Cdd:PRK13547 80 RLARLRAVLPQaaqpafaFSAREIVLLGRYPHARRAgalthrDGEIAWQALALAGATALVGRDVTTLSGGELARVqfarV 159
|
170 180
....*....|....*....|....*..
gi 2030133830 141 LVRLW-----LNQAKLWVLDEPFTALD 162
Cdd:PRK13547 160 LAQLWpphdaAQPPRYLLLDEPTAALD 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-188 |
5.91e-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: 41.59 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 27 GQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDDYDSFAADLLFIGHKTGVNQQlsayenvqhwlmvhgaqa 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 107 deeevytllaklgligledvpvrtlsaGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQ------TQFQSHLDKG 180
Cdd:smart00382 64 ---------------------------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLLLLLKSEKN 116
|
....*...
gi 2030133830 181 GAILLTTH 188
Cdd:smart00382 117 LTVILTTN 124
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-188 |
8.68e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 29 IMQIEGPNGAGKTSLLRIIAGF------ARAdEGQIRYNSTDIRddydSFAADLLFIGHKTGVNQQ-------LSAYENV 95
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLlelneeARV-EGEVRLFGRNIY----SPDVDPIEVRREVGMVFQypnpfphLTIYDNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 96 QHWL----MVHGAQADEEEVYTLLAKLGLIG-----LEDVPvRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGV 166
Cdd:PRK14267 107 AIGVklngLVKSKKELDERVEWALKKAALWDevkdrLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180
....*....|....*....|..
gi 2030133830 167 AMLQtQFQSHLDKGGAILLTTH 188
Cdd:PRK14267 186 AKIE-ELLFELKKEYTIVLVTH 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-187 |
1.07e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI--RDDYDSFAADLLFIGH---KTG 84
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITEsrrDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 85 VNQQLSAYENVQ--------HWLMVHGAQADEEEVYTLLAKLGLIGLE----DVPVRTLSAGQQRRVALVRLWLNQAKLW 152
Cdd:PRK09700 352 FFPNFSIAQNMAisrslkdgGYKGAMGLFHEVDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190
....*....|....*....|....*....|....*
gi 2030133830 153 VLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTT 187
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-188 |
2.47e-04 |
|
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: 41.33 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 2 LEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGF--ARADEGQIRYNStdirddydSFAADLLFI 79
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHV--------ALCEKCGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 80 GHKTGVNQQLS------AYENVQHW---------------LM------VHGAQADEEEVYTLLAKLGLIGLEDVP----- 127
Cdd:TIGR03269 73 ERPSKVGEPCPvcggtlEPEEVDFWnlsdklrrrirkriaIMlqrtfaLYGDDTVLDNVLEALEEIGYEGKEAVGravdl 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 128 -------------VRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHL-DKGGAILLTTH 188
Cdd:TIGR03269 153 iemvqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSH 227
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-188 |
2.60e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYnSTDIRDDYdsFAADLLfig 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGY--FAQHQL--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 81 hktgvnQQLSAYEN-VQHwLMVHGAQADEEEVYTLLAKLGLIGlEDV--PVRTLSAGQQRRVALVRLWLNQAKLWVLDEP 157
Cdd:PRK10636 386 ------EFLRADESpLQH-LARLAPQELEQKLRDYLGGFGFQG-DKVteETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190
....*....|....*....|....*....|.
gi 2030133830 158 FTALDkkgVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK10636 458 TNHLD---LDMRQALTEALIDFEGALVVVSH 485
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-195 |
2.77e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 10 TKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGfaraDEGQIRYNSTDIRDDYdSFAADLLFIGHKTGVNQQL 89
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG----ELSHAETSSVVIRGSV-AYVPQVSWIFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 90 --SAYENVQHW--LMVHGAQADEEevytLLA--KLGLIGLEDVpvrTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDK 163
Cdd:PLN03232 701 fgSDFESERYWraIDVTALQHDLD----LLPgrDLTEIGERGV---NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190
....*....|....*....|....*....|..
gi 2030133830 164 KGVAMLQTQFQSHLDKGGAILLTTHQdltAHF 195
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTNQ---LHF 802
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-157 |
2.88e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 21 SFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNS--TDIRDDYDSFAADLLFI-----------GHKTGVNQ 87
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCpedrkaegiipVHSVADNI 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030133830 88 QLSAYENVQHWLMVHGAQADEEEVYTLLAKLGL-IGLEDVPVRTLSAGQQRRVALVRlWLNQA-KLWVLDEP 157
Cdd:PRK11288 353 NISARRHHLRAGCLINNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGR-WLSEDmKVILLDEP 423
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-189 |
4.85e-04 |
|
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: 39.27 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLR-IIAGFARADEGQIRYNSTDIRddydsfaadllfighktgvnqQLSAY 92
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaIGLALGGAQSATRRRSGVKAG---------------------CIVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 93 ENVQHWLMVHGAQADEEEVYTLLAKLGLIGLEDVPvrtlsagqqrrvalvrlwlnqakLWVLDEPFTALDKKGVAMLQTQ 172
Cdd:cd03227 67 VSAELIFTRLQLSGGEKELSALALILALASLKPRP-----------------------LYILDEIDRGLDPRDGQALAEA 123
|
170
....*....|....*..
gi 2030133830 173 FQSHLDKGGAILLTTHQ 189
Cdd:cd03227 124 ILEHLVKGAQVIVITHL 140
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-49 |
4.88e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.50 E-value: 4.88e-04
10 20 30
....*....|....*....|....*....|....
gi 2030133830 16 LFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAG 49
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE 500
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-188 |
5.21e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.07 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDIRDdydsfAADLLFIGHKTGV------NQQLSA 91
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD-----EENLWDIRNKAGMvfqnpdNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 92 Y--ENVQHWLMVHGAQADE--EEVYTLLAKLGLIGLEDVPVRTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKG-V 166
Cdd:PRK13633 102 IveEDVAFGPENLGIPPEEirERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGrR 181
|
170 180
....*....|....*....|..
gi 2030133830 167 AMLQTQFQSHLDKGGAILLTTH 188
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITH 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-188 |
7.51e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 39.38 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNSTDI----RDDYdsfaadLLFIGHKTGVNQQL---S 90
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKY------IRPVRKRIGMVFQFpesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 91 AYENVQHWLMVHGAQ---ADEEEV----YTLLAKLGLIG--LEDVPVRtLSAGQQRRVALVRLWLNQAKLWVLDEPFTAL 161
Cdd:PRK13646 98 LFEDTVEREIIFGPKnfkMNLDEVknyaHRLLMDLGFSRdvMSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190
....*....|....*....|....*....|
gi 2030133830 162 DKKG---VAMLQTQFQshLDKGGAILLTTH 188
Cdd:PRK13646 177 DPQSkrqVMRLLKSLQ--TDENKTIILVSH 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
129-186 |
2.32e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 2.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2030133830 129 RTLSAGQQRRVALVRLWLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLT 186
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-67 |
2.54e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 37.85 E-value: 2.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030133830 1 MLEIDAVTCTKQDRCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFA--RADEGQIRYNSTDIRD 67
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLE 69
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-190 |
2.77e-03 |
|
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: 37.30 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 18 DSLSFTLHAgqIMQIEGPNGAGKTSLLRiiAGFARadEGQIRYNSTDIRDDYDSfaadLLFIGhktgvnqQLSAyenvqh 97
Cdd:cd03238 14 LDVSIPLNV--LVVVTGVSGSGKSTLVN--EGLYA--SGKARLISFLPKFSRNK----LIFID-------QLQF------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 98 wlmvhgaqadeeevytlLAKLGLIGLE-DVPVRTLSAGQQRRVALVR-LWLNQAK-LWVLDEPFTALDKKGVAMLQTQFQ 174
Cdd:cd03238 71 -----------------LIDVGLGYLTlGQKLSTLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIK 133
|
170
....*....|....*.
gi 2030133830 175 SHLDKGGAILLTTHQD 190
Cdd:cd03238 134 GLIDLGNTVILIEHNL 149
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
127-188 |
3.01e-03 |
|
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: 38.07 E-value: 3.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030133830 127 PVRTLSAGQQRRVALVRLWLNQAK---LWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTH 188
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
34-66 |
3.43e-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: 37.37 E-value: 3.43e-03
10 20 30
....*....|....*....|....*....|...
gi 2030133830 34 GPNGAGKTSLLRIIAGFARADEGQIRYNSTDIR 66
Cdd:pfam13304 6 GPNGSGKSNLLEALRFLADFDALVIGLTDERSR 38
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
17-59 |
3.86e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.28 E-value: 3.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2030133830 17 FDSLSFTLHAG-QIMQIEGPNGAGKTSLLRIIAGFARADEGQIR 59
Cdd:COG3950 14 FEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
127-189 |
6.46e-03 |
|
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: 36.44 E-value: 6.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030133830 127 PVRTLSAGQQRRVALVRLWLNQAK---LWVLDEPFTALDKKGVAMLQTQFQSHLDKGGAILLTTHQ 189
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-188 |
7.96e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 36.69 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 14 RCLFDSLSFTLHAGQIMQIEGPNGAGKTSLLRIIAGFARADEGQIRYNST----------------------DIRDDYDS 71
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalpqpaleyviDGDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030133830 72 FAADLLFI-----GHKTG-VNQQLSAyenVQHWLMVHGAQadeeevyTLLAKLGLIGLE-DVPVRTLSAGQQRRVALVRL 144
Cdd:PRK10636 94 LEAQLHDAnerndGHAIAtIHGKLDA---IDAWTIRSRAA-------SLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2030133830 145 WLNQAKLWVLDEPFTALDKKGVAMLQTQFQSHldkGGAILLTTH 188
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLILISH 204
|
|
| |
