|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-233 |
2.20e-95 |
|
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: 283.47 E-value: 2.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:COG1120 2 LEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETP 165
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-220 |
4.72e-67 |
|
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: 208.44 E-value: 4.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISV 87
Cdd:cd03214 2 VENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 88 VLTekcdirnmsvveliglgrspytgfwgtlskedkavvdkSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVI 167
Cdd:cd03214 78 VPQ--------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 168 YLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLK 172
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-232 |
3.95e-60 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 193.31 E-value: 3.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:PRK11231 2 TLRTENLTVGY---GT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPED 232
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-233 |
2.03e-51 |
|
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: 170.21 E-value: 2.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTekcDIRN---MSVVE------LIGLGRSPytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:COG1122 78 GLVFQ---NPDDqlfAPTVEedvafgPENLGLPR---------EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-221 |
7.08e-51 |
|
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: 168.03 E-value: 7.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISV 87
Cdd:cd03225 2 LKNLSFSYPDGA--RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 88 VLtekcdiRN------MSVVE------LIGLGRSPytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVM 155
Cdd:cd03225 80 VF------QNpddqffGPTVEeevafgLENLGLPE---------EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-233 |
6.31e-49 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 164.49 E-value: 6.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:COG4604 2 IEIKNVSKRY---GG-KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SvVLTEKCDIrNM--SVVELIGLGRSPYTGfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQE 163
Cdd:COG4604 78 A-ILRQENHI-NSrlTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 164 TPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMdkANG--VTVGTPEDL 233
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM--KDGrvVAQGTPEEI 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-221 |
1.86e-48 |
|
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: 161.93 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 7 HIENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGeytdkQLSRVIS 86
Cdd:cd03235 1 EVEDLTVSY---GGHPVLED-VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 87 VVlTEKCDI---RNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQE 163
Cdd:cd03235 72 YV-PQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 164 TPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-233 |
8.42e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 8.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRvI 85
Cdd:COG1131 1 IEVRGLTKRY---GDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLgrspYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETP 165
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-233 |
8.50e-46 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 156.68 E-value: 8.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 9 ENLSIGYpGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVV 88
Cdd:PRK10253 11 EQLTLGY-GK---YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 89 LTEKCDIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIY 168
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 169 LDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-274 |
4.98e-45 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 158.47 E-value: 4.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKaVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:PRK09536 3 MIDVSDLSVEF---GDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSrQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLNGSLSNFF- 243
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFd 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2525300912 244 ARKGIAFDLETG------LFRVANEYTS---RIRLAGHGQ 274
Cdd:PRK09536 238 ARTAVGTDPATGaptvtpLPDPDRTEAAadtRVHVVGGGQ 277
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-232 |
2.08e-44 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 153.00 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 4 ETIHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSR 83
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 VISVvltekcdirnM----------SVVELIGLGRSPytgfWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQK 153
Cdd:PRK13548 77 RRAV----------LpqhsslsfpfTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 154 VMIAKALAQ------ETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTV 227
Cdd:PRK13548 143 VQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
....*
gi 2525300912 228 GTPED 232
Cdd:PRK13548 223 GTPAE 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-228 |
2.80e-44 |
|
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: 151.13 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVI 85
Cdd:cd03259 1 LELKGLSKTY---GSVRAL-DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSPytgfwGTLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKL-----RGVPKAEiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVG 228
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-233 |
3.71e-44 |
|
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: 158.53 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQP---KLGGNIFIEGKEIGEYTDKQLS 82
Cdd:COG1123 5 LEVRDLSVRYPG-GDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTEKCDIRNMSVVE------LIGLGRSPytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:COG1123 83 RRIGMVFQDPMTQLNPVTVGdqiaeaLENLGLSR---------AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-233 |
5.82e-43 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 149.17 E-value: 5.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVVLTEKCDIRNMSVVELIGLGRSPYTGF 114
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 115 WGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQ 194
Cdd:PRK10575 117 LGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
|
170 180 190
....*....|....*....|....*....|....*....
gi 2525300912 195 TDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK10575 197 RGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-233 |
2.15e-41 |
|
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: 144.63 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV- 84
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 --ISVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTL----SKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAK 158
Cdd:cd03256 78 rqIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 159 ALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-242 |
3.74e-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: 143.84 E-value: 3.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVi 85
Cdd:COG4555 2 IEVENLSKKY---GKVPAL-KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 sVVLTEKCDIR-NMSVVELIGLgrspYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:COG4555 77 -GVLPDERGLYdRLTVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLNGSLSNF 242
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-216 |
2.62e-40 |
|
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: 141.09 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV- 84
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ---ISVV-----LtekcdIRNMSV---VELIGLGRspytgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQK 153
Cdd:cd03255 81 rrhIGFVfqsfnL-----LPDLTAlenVELPLLLA-------GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 154 VMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELAlQIADKI 216
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRI 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-233 |
1.16e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.93 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGkeigeytdkq 80
Cdd:COG3842 1 MAMPALELENVSKRY---GDVTAL-DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 lsRVISVVLTEKcdiRN-------------MSVVELIGLG---RSpytgfwgtLSKED-KAVVDKSIALVGIPHLAHRMV 143
Cdd:COG3842 67 --RDVTGLPPEK---RNvgmvfqdyalfphLTVAENVAFGlrmRG--------VPKAEiRARVAELLELVGLEGLADRYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 144 HTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKAN 223
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
250
....*....|
gi 2525300912 224 GVTVGTPEDL 233
Cdd:COG3842 214 IEQVGTPEEI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-219 |
8.73e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.10 E-value: 8.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYP-GKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:COG1136 5 LELRNLTKSYGtGEGEVTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ----ISVV-----LtekcdIRNMSVVELIGLgrsPYTgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVM 155
Cdd:COG1136 84 rrrhIGFVfqffnL-----LPELTALENVAL---PLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELAlQIADKIWLM 219
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRL 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-224 |
1.19e-38 |
|
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: 136.45 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeytdKQLSRVI 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSpytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETP 165
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLE----LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANG 224
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-233 |
1.41e-38 |
|
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: 143.12 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYP--GKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTD---KQ 80
Cdd:COG1123 261 LEVRNLSKRYPvrGKGGVRAV-DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVV-------LTEKcdirnMSVVELIGLGRSPYtgfwGTLSKED-KAVVDKSIALVGI-PHLAHRMVHTLSDGER 151
Cdd:COG1123 340 LRRRVQMVfqdpyssLNPR-----MTVGDIIAEPLRLH----GLLSRAErRERVAELLERVGLpPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPE 231
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
..
gi 2525300912 232 DL 233
Cdd:COG1123 491 EV 492
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-233 |
4.37e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 136.09 E-value: 4.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVL---TEKCDIRnMSVVELIGlgrspyTGFWGTLSKEDKAVVDKSIALVGIP-HLAHRMVHTLSDGERQKVMIAKALA 161
Cdd:COG1124 82 QMVFqdpYASLHPR-HTVDRILA------EPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-221 |
6.24e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.99 E-value: 6.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeytdKQLSRVI 85
Cdd:COG1116 8 LELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVV---------LTekcdirnmsVVELIGLGRSpytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:COG1116 83 GVVfqepallpwLT---------VLDNVALGLE----LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-221 |
1.26e-37 |
|
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: 134.17 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLS--- 82
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTekcDIRN-----MSVVELIglgRSPYTgFWGTLSKEDKAVVDKSIALVGIP---HLAHRMVHTLSDGERQKV 154
Cdd:cd03257 82 KEIQMVFQ---DPMSslnprMTIGEQI---AEPLR-IHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-233 |
3.80e-37 |
|
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: 133.58 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGkgdVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03295 1 IEFENVTKRYGG---GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLgrSPYTGFWGtlSKEDKAVVDKSIALVGIP--HLAHRMVHTLSDGERQKVMIAKALAQE 163
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL--VPKLLKWP--KEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 164 TPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-219 |
1.26e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.98 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 4 ETIHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEI-GEYTDKqls 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 rviSVVLTEKCDIRNMSVVELIGLGRSpytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQ 162
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFGLR----LRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 163 ETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLM 219
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-221 |
1.35e-35 |
|
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: 127.13 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRvI 85
Cdd:cd03230 1 IEVRNLSKRY---GKKTAL-DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIglgrspytgfwgtlskedkavvdksialvgiphlahrmvhTLSDGERQKVMIAKALAQETP 165
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-233 |
2.12e-35 |
|
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: 128.01 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGeYTDKQLSRVI 85
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SV-----VLTEkcdirNMSVVELIGLgrspYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKAL 160
Cdd:cd03263 78 GYcpqfdALFD-----ELTVREHLRF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtdKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-243 |
3.40e-35 |
|
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: 128.28 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKL-GGNIFIEGKEIGEYTDKQLSRV 84
Cdd:COG1119 4 LELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVV---LTEKCDiRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALA 161
Cdd:COG1119 80 IGLVspaLQLRFP-RDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLNGSLSN 241
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSE 238
|
..
gi 2525300912 242 FF 243
Cdd:COG1119 239 AF 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-220 |
4.70e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.56 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVADgicAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVI 85
Cdd:COG3840 2 LRLDDLTYRY---GDFPLRFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEkcdirN-----MSVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKAL 160
Cdd:COG3840 74 SMLFQE-----NnlfphLTVAQNIGLGLRPG----LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVA 204
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
32-269 |
1.23e-34 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 129.97 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV----ISVVLTEKCDIRNMSVVELIGLG 107
Cdd:TIGR01186 16 IAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrrkkIGMVFQQFALFPHMTILQNTSLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 108 rsPYTGFWGTLSKEDKAVvdKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQL 187
Cdd:TIGR01186 96 --PELLGWPEQERKEKAL--ELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 188 LHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLNGS------------LSNFFARKGIAFDLETG 255
Cdd:TIGR01186 172 LKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPAneyveefigkvdLSQVFDAERIAQRMNTG 251
|
250
....*....|....
gi 2525300912 256 LFRVANEYTSRIRL 269
Cdd:TIGR01186 252 PITKTADKGPRSAL 265
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-234 |
2.10e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 132.19 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:COG4988 336 SIELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVltekcdirnmsvveliglGRSPYTgFWGTL-----------SKEDkavVDKSIALVGIPHLAHRM---VHT----- 145
Cdd:COG4988 413 IAWV------------------PQNPYL-FAGTIrenlrlgrpdaSDEE---LEAALEAAGLDEFVAALpdgLDTplgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 146 ---LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLELaLQIADKIWLMDKA 222
Cdd:COG4988 471 grgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILVLDDG 547
|
250
....*....|..
gi 2525300912 223 NGVTVGTPEDLS 234
Cdd:COG4988 548 RIVEQGTHEELL 559
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
3.93e-34 |
|
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: 125.31 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV- 84
Cdd:cd03261 1 IELRGLTKSF---GG-RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 --ISVVLTEKCDIRNMSVVELIGLGRSPYTgfwgTLSKE--DKAVVDKsIALVGIPHLAHRMVHTLSDGERQKVMIAKAL 160
Cdd:cd03261 77 rrMGMLFQSGALFDSLTVFENVAFPLREHT----RLSEEeiREIVLEK-LEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-233 |
3.74e-33 |
|
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: 122.83 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRV 84
Cdd:cd03296 2 SIEVRNVSKRF---GDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-221 |
4.96e-33 |
|
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: 120.04 E-value: 4.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 7 HIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVIS 86
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 87 vvltekcdirnmsvveliglgrspytgfwgtlskedkavvdksialvgiphlahrMVHTLSDGERQKVMIAKALAQETPV 166
Cdd:cd00267 77 -------------------------------------------------------YVPQLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 167 IYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-233 |
5.64e-33 |
|
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: 121.96 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVI 85
Cdd:cd03300 1 IELENVSKFY---GGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRspytgfwgTLSKEDKAV----VDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGL--------RLKKLPKAEikerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-174 |
5.79e-33 |
|
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: 119.67 E-value: 5.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVVLTEKCDIRNMSVVELIGLGRSpy 111
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLL-- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 112 tgFWGTLSKEDKAVVDKSIALVGIPHLAHRMV----HTLSDGERQKVMIAKALAQETPVIYLDEPTA 174
Cdd:pfam00005 86 --LKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-208 |
8.27e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.31 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLS--- 82
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTekcDIR---NMSVVE-----LIGLGRSPytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKV 154
Cdd:COG2884 79 RRIGVVFQ---DFRllpDRTVYEnvalpLRVTGKSR---------KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqTDKTIFLSTHDLEL 208
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLEL 199
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-233 |
1.43e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.10 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAF-QPKlGGNIFIEGKEIgeYTDkqLS- 82
Cdd:COG1118 2 SIEVRNISKRF---GSFTLLDD-VSLEIASGELVALLGPSGSGKTTLLRIIAGLeTPD-SGRIVLNGRDL--FTN--LPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 --RVISVV-----LtekcdIRNMSVVELI--GLGRSPytgfwgtLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQ 152
Cdd:COG1118 73 reRRVGFVfqhyaL-----FPHMTVAENIafGLRVRP-------PSKAEiRARVEELLELVQLEGLADRYPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 153 KVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPED 232
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
.
gi 2525300912 233 L 233
Cdd:COG1118 221 V 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-220 |
1.91e-32 |
|
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: 119.21 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTD--KQLSR 83
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 VISVVLTEKCDIRNMSVVELIGLGrspytgfwgtlskedkavvdksialvgiphlahrmvhtLSDGERQKVMIAKALAQE 163
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 164 TPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-236 |
3.80e-32 |
|
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: 120.83 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV----ISVVLTEKCDIRNMSVVELIGLG 107
Cdd:cd03294 47 VREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHRTVLENVAFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 108 RSpytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQL 187
Cdd:cd03294 127 LE----VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525300912 188 LHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLN 236
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-234 |
5.94e-32 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 119.52 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVI 85
Cdd:TIGR00968 1 IEIANISKRF---GSFQALDD-VNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARD--RKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLG----RSPytgfwgtlSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALA 161
Cdd:TIGR00968 75 GFVFQHYALFKHLTVRDNIAFGleirKHP--------KAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLS 234
Cdd:TIGR00968 147 VEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVY 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-245 |
1.24e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 124.49 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:COG4987 333 SLELEDVSFRYPGAG--RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVlTEKCDIRNMSVVELIGLGRspytgfwGTLSKED-KAVVDKsialVGIPHLAHRMVH-----------TLSDGERQ 152
Cdd:COG4987 411 IAVV-PQRPHLFDTTLRENLRLAR-------PDATDEElWAALER----VGLGDWLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 153 KVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLElALQIADKIWLMDKANGVTVGTPED 232
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEE 555
|
250
....*....|....
gi 2525300912 233 L-SLNGSLSNFFAR 245
Cdd:COG4987 556 LlAQNGRYRQLYQR 569
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-220 |
1.31e-31 |
|
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: 117.58 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVi 85
Cdd:COG4133 3 LEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 sVVLTEKCDI-RNMSVVELIGLgrspYTGFWGTlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:COG4133 78 -AYLGHADGLkPELTVRENLRF----WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDlELALQIADKIWLMD 220
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ-PLELAAARVLDLGD 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-236 |
1.83e-31 |
|
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: 117.92 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEI-GEYTDKQLSRVIS 86
Cdd:cd03224 3 VENLNAGY---GKSQIL-FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 87 VVLTEKCDIRNMSVVELIGLGRSPYTGfwgtlsKEDKAVVDKSIALVgiPHLA---HRMVHTLSDGERQKVMIAKALAQE 163
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVYELF--PRLKerrKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 164 TPVIYLDEPTAFLDfPSKV-EMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLN 236
Cdd:cd03224 151 PKLLLLDEPSEGLA-PKIVeEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-233 |
2.78e-31 |
|
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: 117.77 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgkGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF---GD-RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRV---ISVV------LTekcdirNMSVVELIGLgrsP---YTGfwgtLSKED-KAVVDKSIALVGIPHLAHRMVHTLS 147
Cdd:COG1127 77 LYELrrrIGMLfqggalFD------SLTVFENVAF---PlreHTD----LSEAEiRELVLEKLELVGLPGAADKMPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 148 DGERQKVMIAKALAQETPVIYLDEPTAFLDfP-SKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVT 226
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLD-PiTSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
....*..
gi 2525300912 227 VGTPEDL 233
Cdd:COG1127 223 EGTPEEL 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-234 |
2.94e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.68 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCD-IRNMSVVELIGLGrsPYTgfWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:PRK13647 82 GLVFQDPDDqVFSSTVWDDVAFG--PVN--MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLS 234
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-233 |
8.17e-31 |
|
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: 115.93 E-value: 8.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKqLSRVI 85
Cdd:cd03265 1 IEVENLVKKY---GDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVE-LIGLGRspytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:cd03265 76 GIVFQDLSVDDELTGWEnLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-221 |
1.05e-30 |
|
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: 115.67 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGeyTDKQLSRVISVVLTEKCDIRNMSVVELIGLGRSPY 111
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 112 TgfwgTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQL 191
Cdd:cd03298 99 L----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|
gi 2525300912 192 SRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-209 |
1.62e-30 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 114.44 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 15 YPGKGDVkavADGICAGINSGELTCLLGANGVGKSTLLRTLSA-FQPKlGGNIFIEGKEIGeYTDKQLSRV---ISVVLT 90
Cdd:TIGR01166 1 YPGGPEV---LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQ-SGAVLIDGEPLD-YSRKGLLERrqrVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 91 EKCD-IRNMSVVELIGLGrsPYTgfWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYL 169
Cdd:TIGR01166 76 DPDDqLFAADVDQDVAFG--PLN--LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2525300912 170 DEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELA 209
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-233 |
1.90e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeyTDkqlsrv 84
Cdd:COG3839 3 SLELENVSKSY---GGVEAL-KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TD------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 isvVLTEKCDIR----------NMSVVELIGLG-RspytgfwgtLSKEDKAVVDKSI----ALVGIPHLAHRMVHTLSDG 149
Cdd:COG3839 70 ---LPPKDRNIAmvfqsyalypHMTVYENIAFPlK---------LRKVPKAEIDRRVreaaELLGLEDLLDRKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 150 ERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDkaNGVT--V 227
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMN--DGRIqqV 215
|
....*.
gi 2525300912 228 GTPEDL 233
Cdd:COG3839 216 GTPEEL 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-232 |
3.94e-30 |
|
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: 114.46 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIG-----EYTDKQLS 82
Cdd:cd03219 3 VRGLTKRF---GGLVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglpphEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 R---VISVVltekcdiRNMSVVELIGLG---RSPYTGFWGTLSKEDKAVVDK---SIALVGIPHLAHRMVHTLSDGERQK 153
Cdd:cd03219 79 RtfqIPRLF-------PELTVLENVMVAaqaRTGSGLLLARARREEREARERaeeLLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 154 VMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPED 232
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-252 |
1.03e-29 |
|
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: 119.55 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:COG2274 474 IELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEkCDIRNMSVVELIGLGRSpytgfwgTLSKEDkavVDKSIALVGI-------PHLAHRMV----HTLSDGERQKV 154
Cdd:COG2274 552 GVVLQD-VFLFSGTIRENITLGDP-------DATDEE---IIEAARLAGLhdfiealPMGYDTVVgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLELaLQIADKIWLMDKANGVTVGTPEDLs 234
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEEL- 696
|
250
....*....|....*...
gi 2525300912 235 lngslsnfFARKGIAFDL 252
Cdd:COG2274 697 --------LARKGLYAEL 706
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-221 |
1.47e-29 |
|
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: 111.32 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03228 1 IEFKNVSFSYPGRP--KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEkCDIRNMSVVELIglgrspytgfwgtlskedkavvdksialvgiphlahrmvhtLSDGERQKVMIAKALAQETP 165
Cdd:cd03228 79 AYVPQD-PFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLELaLQIADKIWLMDK 221
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLST-IRDADRIIVLDD 169
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-232 |
1.21e-28 |
|
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: 110.89 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAvaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVI 85
Cdd:cd03299 1 LKVENLSKDW---KEFKL--KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSpytgfwgtLSKEDKAVVDKSI----ALVGIPHLAHRMVHTLSDGERQKVMIAKALA 161
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLK--------KRKVDKKEIERKVleiaEMLGIDHLLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPED 232
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-220 |
1.70e-28 |
|
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: 109.65 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVI 85
Cdd:cd03301 1 VELENVTKRF---GNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRspytgfwgTLSKEDKAVVDKSI----ALVGIPHLAHRMVHTLSDGERQKVMIAKALA 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGL--------KLRKVPKDEIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMN 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-222 |
1.73e-28 |
|
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: 109.59 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvKAVaDGICAGINSGeLTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKqLSRVI 85
Cdd:cd03264 1 LQLENLTKRYGKK---RAL-DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGlgrspYTGFW-GTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLD-----YIAWLkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSrqTDKTIFLSTHDLELALQIADKIWLMDKA 222
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
2.10e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 2 NKETIHIENLSIGYPGkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQL 81
Cdd:PRK13632 4 KSVMIKVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 82 SRVISVVL----------TEKCDIRnmsvvelIGLGRSPYTgfwgtlSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGER 151
Cdd:PRK13632 82 RKKIGIIFqnpdnqfigaTVEDDIA-------FGLENKKVP------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQiADKIWLMDKANGVTVGTPE 231
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPK 227
|
..
gi 2525300912 232 DL 233
Cdd:PRK13632 228 EI 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
2.40e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYPgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgEYTDK- 79
Cdd:PRK13636 1 MEDYILKVEELNYNYS---DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 --QLSRVISVVLTE-KCDIRNMSVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:PRK13636 77 lmKLRESVGMVFQDpDNQLFSASVYQDVSFGAVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-233 |
7.63e-28 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 109.53 E-value: 7.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 20 DVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQP--------KLGGNIFIEGKEIGEYTDKQLSRVISVVLTE 91
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 92 KCDIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETP------ 165
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 166 ---VIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13547 172 pprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-234 |
8.62e-28 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 108.77 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 27 GICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKlGGNIFIEGKEIGEYTDKQLSRVISVVLTEKCDIRNMSVVELIGL 106
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 107 GRSPytgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVI-------YLDEPTAFLDFP 179
Cdd:COG4138 93 HQPA-----GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTInpegqllLLDEPMNSLDVA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 180 SKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDK----ANGVT--VGTPEDLS 234
Cdd:COG4138 168 QQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQgklvASGETaeVMTPENLS 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-233 |
1.32e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.56 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRV 84
Cdd:PRK10851 2 SIEIANIKKSF---GRTQVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKCDIRNMSVVELIGLGRS--PYTgfwgtlSKEDKAVVDKSIA----LVGIPHLAHRMVHTLSDGERQKVMIAK 158
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGLTvlPRR------ERPNAAAIKAKVTqlleMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 159 ALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-221 |
2.73e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.44 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEkCDIRNMSVVELIglgRSPYTGFWGTLSKEDkavVDKSIALVGIPH-LAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:COG4619 77 AYVPQE-PALWGGTVRDNL---PFPFQLRERKFDRER---ALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-233 |
3.15e-27 |
|
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: 106.50 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRT---LSAFQPKL--GGNIFIEGKEIGE--YTD 78
Cdd:cd03260 1 IELRDLNVYY---GDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPGApdEGEVLLDGKDIYDldVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 79 KQLSRVISVVLtEKCDIRNMSVVELIGLGRSPYtGFWGTlsKEDKAVVDKSIALVGIPHLAHRMVH--TLSDGERQKVMI 156
Cdd:cd03260 77 LELRRRVGMVF-QKPNPFPGSIYDNVAYGLRLH-GIKLK--EELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTdkTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-236 |
4.64e-27 |
|
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: 106.51 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQL---S 82
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVV------LTEKCDIRNMSV-VELIGLGRspytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVM 155
Cdd:cd03258 82 RRIGMIfqhfnlLSSRTVFENVALpLEIAGVPK-----------AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSL 235
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 2525300912 236 N 236
Cdd:cd03258 231 N 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-228 |
8.42e-27 |
|
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: 105.14 E-value: 8.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGY-PGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLS-AFQPKlGGNIFIEGKEIGEyTDKQLSR 83
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAgLLEPD-AGFATVDGFDVVK-EPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 VISVVLTEKCDIRNMSVVELIGLgrspYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQE 163
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEY----FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 164 TPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVG 228
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-228 |
8.92e-27 |
|
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: 105.63 E-value: 8.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 26 DGICAGINSGELTCLLGANGVGKSTLLRTLSAF-QPKLGGnIFIEGKEIGEYTDKQLsrvisVVLTEKCDIRNMSVVELI 104
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGG-VILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 105 GLGRSPYTGfwgTLSK-EDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVE 183
Cdd:TIGR01184 76 ALAVDRVLP---DLSKsERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2525300912 184 MMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVG 228
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-231 |
8.97e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.64 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYPgkgDVKAVA-DGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDK 79
Cdd:PRK13635 1 MKEEIIRVEHISFRYP---DAATYAlKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 QLSRVISVVLtekcdirnmsvveliglgRSPYTGFWGTLSKEDKAV---------------VDKSIALVGIPHLAHRMVH 144
Cdd:PRK13635 78 DVRRQVGMVF------------------QNPDNQFVGATVQDDVAFglenigvpreemverVDQALRQVGMEDFLNREPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 145 TLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQiADKIWLMDKANG 224
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
....*..
gi 2525300912 225 VTVGTPE 231
Cdd:PRK13635 219 LEEGTPE 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-233 |
1.12e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 107.10 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGkgDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:COG1125 2 IEFENVTKRYPD--GTVAV-DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVltekcdIRN------MSVVELIG-----LGrspytgfWgtlSKED-KAVVDKSIALVGIP--HLAHRMVHTLSDGER 151
Cdd:COG1125 79 GYV------IQQiglfphMTVAENIAtvprlLG-------W---DKERiRARVDELLELVGLDpeEYRDRYPHELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPE 231
Cdd:COG1125 143 QRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPE 222
|
..
gi 2525300912 232 DL 233
Cdd:COG1125 223 EI 224
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
19-233 |
1.49e-26 |
|
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: 107.82 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 19 GDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVISVVLTEKCDIRNM 98
Cdd:TIGR03265 15 GAFTALKD-ISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK--RDYGIVFQSYALFPNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 99 SVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDF 178
Cdd:TIGR03265 92 TVADNIAYGLKNR----GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 179 PSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:TIGR03265 168 RVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-233 |
2.22e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.61 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVkavaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVI 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV----DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSPytgfwGTLSK-EDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQ-----DKLPKaEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-221 |
2.36e-26 |
|
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: 103.76 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEyTDKQLSRVI 85
Cdd:cd03262 1 IEIKNLHKSF---GD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVV--------LTEkcdirNMSVVELIGLGRSpytgfwgTLSKEDKAVVDKsIAL-----VGIPHLAHRMVHTLSDGERQ 152
Cdd:cd03262 76 QKVgmvfqqfnLFP-----HLTVLENITLAPI-------KVKGMSKAEAEE-RALellekVGLADKADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 153 KVMIAKALAQETPVIYLDEPTAFLDfPSKV-EMMQLLHQLSrQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALD-PELVgEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-216 |
2.55e-26 |
|
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: 106.29 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYP-GKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLG---GNIFIEGKEIGEYTDKQL 81
Cdd:COG0444 2 LEVRNLKVYFPtRRGVVKAV-DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 82 SRV----ISVV-----------LTekcdIRNmSVVELIGLgrspytgfWGTLSKED-KAVVDKSIALVGIPHLAHRMV-- 143
Cdd:COG0444 81 RKIrgreIQMIfqdpmtslnpvMT----VGD-QIAEPLRI--------HGGLSKAEaRERAIELLERVGLPDPERRLDry 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 144 -HTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKI 216
Cdd:COG0444 148 pHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRV 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-233 |
3.84e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.49 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 28 ICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEI-GEYTDKQLSRV---ISVV-------LTEKcdir 96
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLrkkVGIVfqfpehqLFEE---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 97 nmSVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPH-LAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAF 175
Cdd:PRK13634 102 --TVEKDICFGPMNF----GVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 176 LDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-229 |
1.19e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGkgdVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgEYTDKQLSRV--I 85
Cdd:COG1129 7 MRGISKSFGG---VKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQAagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSPYTGF---WGTLSKEDKAVVDKsialVGIPHLAHRMVHTLSDGERQKVMIAKALAQ 162
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLAR----LGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 163 ETPVIYLDEPTAFLDfPSKVEMM-QLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMdkANGVTVGT 229
Cdd:COG1129 158 DARVLILDEPTASLT-EREVERLfRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL--RDGRLVGT 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-249 |
1.21e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 103.24 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeyTDKQLSRvi 85
Cdd:PRK11248 2 LQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---EGPGAER-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSpytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETP 165
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQ----LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVgtpEDLSLNgslsnfFAR 245
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLN------FAR 219
|
....
gi 2525300912 246 KGIA 249
Cdd:PRK11248 220 RFVA 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
34-221 |
1.31e-25 |
|
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: 101.99 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 34 SGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEyTDKQL-----SRVISVVLTEKCDIRNMSVVELIGLGr 108
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 109 spytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLL 188
Cdd:cd03297 100 -----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|...
gi 2525300912 189 HQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-236 |
2.21e-25 |
|
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: 101.98 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV-IS 86
Cdd:COG0410 6 VENLHAGY---GGIHVL-HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 87 VVLtEKCDI-RNMSVVE--LIGLGRSPytgfwgtlskeDKAVVDKSIALV-GI-PHLA---HRMVHTLSDGERQKVMIAK 158
Cdd:COG0410 82 YVP-EGRRIfPSLTVEEnlLLGAYARR-----------DRAEVRADLERVyELfPRLKerrRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 159 ALAQETPVIYLDEPTAFLDfPSKV-EMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDkaNGVTV--GTPEDLSL 235
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLA-PLIVeEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLE--RGRIVleGTAAELLA 225
|
.
gi 2525300912 236 N 236
Cdd:COG0410 226 D 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-239 |
2.73e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.57 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISV 87
Cdd:PRK13652 4 IETRDLCYSYSGSKEAL-NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 88 VLTEKCD-IRNMSVVELIGLGRSpytgfwgTLSKEDKAV---VDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQE 163
Cdd:PRK13652 83 VFQNPDDqIFSPTVEQDIAFGPI-------NLGLDEETVahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 164 TPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLNGSL 239
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-232 |
6.49e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 6.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK09452 10 SLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 lsRVISVVLTEKCDIRNMSVVELIGLG----RSPytgfwgtlSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:PRK09452 86 --RHVNTVFQSYALFPHMTVFENVAFGlrmqKTP--------AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPED 232
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
32-216 |
7.64e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.24 E-value: 7.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAF-----QPK-----LGGNIFIEGKEIGeytDKQLSRVISVVLTEKCDIRN-MSV 100
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGshielLGRTVQREGRLAR---DIRKSRANTGYIFQQFNLVNrLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 101 VE--LIG-LGRSPytgFWGT----LSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPT 173
Cdd:PRK09984 104 LEnvLIGaLGSTP---FWRTcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2525300912 174 AFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKI 216
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-233 |
7.85e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.31 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgEYTDKQLSRV- 84
Cdd:PRK13639 2 LETRDLKYSYP---DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 --ISVVLTEKCD-IRNMSVVELIGLGrsPYTGfwgTLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKAL 160
Cdd:PRK13639 78 ktVGIVFQNPDDqLFAPTVEEDVAFG--PLNL---GLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-229 |
9.56e-25 |
|
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: 98.27 E-value: 9.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 19 GDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeytdkqlsrvisvvltekcdirnm 98
Cdd:cd03216 11 GGVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 99 svveligLGRSPytgfwgtlskedkavvDKSIALvGIphlahRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDf 178
Cdd:cd03216 65 -------SFASP----------------RDARRA-GI-----AMVYQLSVGERQMVEIARALARNARLLILDEPTAALT- 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 179 PSKVEMM-QLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDkaNGVTVGT 229
Cdd:cd03216 115 PAEVERLfKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLR--DGRVVGT 163
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-240 |
1.52e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEigeYTDKQLS-RVISVVLTEKCDIRNMSVVELIGLGRSP 110
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSrRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 111 ytGFwgTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQ 190
Cdd:PRK10771 99 --GL--KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525300912 191 LSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLsLNGSLS 240
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL-LSGKAS 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-235 |
3.87e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.68 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ-LSRV 84
Cdd:PRK13644 2 IRLENVSYSYP---DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLtekcdirnmsvveliglgRSPYTGFWGTLSKEDKAV---------------VDKSIALVGIPHLAHRMVHTLSDG 149
Cdd:PRK13644 79 VGIVF------------------QNPETQFVGRTVEEDLAFgpenlclppieirkrVDRALAEIGLEKYRHRSPKTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 150 ERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLElALQIADKIWLMDKANGVTVGT 229
Cdd:PRK13644 141 QGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGE 218
|
250
....*....|
gi 2525300912 230 PE----DLSL 235
Cdd:PRK13644 219 PEnvlsDVSL 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-244 |
9.00e-24 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 98.08 E-value: 9.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 28 ICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKlGGNIFIEGKEIGEYTDKQLSRVISVVLTEKCDIRNMSVVELIGLG 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 108 RSPytgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVI-------YLDEPTAFLDFPS 180
Cdd:PRK03695 94 QPD-----KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 181 KVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMdkANGVTV--GTPEDLSLNGSLSNFFA 244
Cdd:PRK03695 169 QAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLL--KQGKLLasGRRDEVLTPENLAQVFG 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-221 |
2.61e-23 |
|
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: 96.25 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 12 SIGYPGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRvISVVLTE 91
Cdd:cd03267 25 SLFKRKYREVEAL-KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 92 KCD-IRNMSVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLD 170
Cdd:cd03267 103 KTQlWWDLPVIDSFYLLAAIY----DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 171 EPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-219 |
2.78e-23 |
|
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: 100.44 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKGdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVlTEKCDIRNMSVVELIGLGRSPYTGfwgtlskedkAVVDKSIALVG-------IPHLAHRMV----HTLSDGERQK 153
Cdd:TIGR02857 398 IAWV-PQHPFLFAGTIAENIRLARPDASD----------AEIREALERAGldefvaaLPQGLDTPIgeggAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 154 VMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLELALQiADKIWLM 219
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-233 |
4.63e-23 |
|
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: 97.56 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 40 LLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVISVVLTEKCDIRNMSVVELIGLGRSpytgFWGTLS 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGLK----MRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 120 KEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTI 199
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....
gi 2525300912 200 FLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-206 |
6.04e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 99.36 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:TIGR02868 334 TLELRDLSAGYPGA---PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVlTEKCDIRNMSVVELIGLGRSPYTG--FWGTLSKedkavVDKSIALVGIPHLAHRMVH----TLSDGERQKVMIAK 158
Cdd:TIGR02868 411 VSVC-AQDAHLFDTTVRENLRLARPDATDeeLWAALER-----VGLADWLRALPDGLDTVLGeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2525300912 159 ALAQETPVIYLDEPTAFLDFPSKVEMMQLLhqLSRQTDKTIFLSTHDL 206
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-216 |
1.74e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 19 GDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEI-----------GeytdkqlsrvISV 87
Cdd:COG3845 16 GGVVAN-DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprdaialG----------IGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 88 V-----LtekcdIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSiALVGIPHLAHRMVHTLSDGERQKVMIAKALAQ 162
Cdd:COG3845 85 VhqhfmL-----VPNLTVAENIVLGLEPTKGGRLDRKAARARIRELS-ERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 163 ETPVIYLDEPTAFLDfPSKV-EMMQLLHQLSRQtDKTIFLSTHDLELALQIADKI 216
Cdd:COG3845 159 GARILILDEPTAVLT-PQEAdELFEILRRLAAE-GKSIIFITHKLREVMAIADRV 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-208 |
1.78e-22 |
|
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: 93.63 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGkgDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ---LS 82
Cdd:cd03292 1 IEFINVTKTYPN--GTAAL-DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTEKCDIRNMSVVELIGL-----GRSPytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIA 157
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFalevtGVPP---------REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 158 KALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQlSRQTDKTIFLSTHDLEL 208
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKEL 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-233 |
1.83e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.67 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF---GGLLAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRvISVVLTEKcDIR---NMSVVE--LIGLGRSPYTGFWGTLSK-------EDKAVVDKSIAL--VGIPHLAHRMVHTL 146
Cdd:PRK11300 77 IAR-MGVVRTFQ-HVRlfrEMTVIEnlLVAQHQQLKTGLFSGLLKtpafrraESEALDRAATWLerVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 147 SDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVT 226
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
....*..
gi 2525300912 227 VGTPEDL 233
Cdd:PRK11300 235 NGTPEEI 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-206 |
4.05e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.79 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 34 SGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLsrVISVVLTEKCDIRNMSVVE-LIGLGRSPYT 112
Cdd:PRK15056 32 GGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--VAYVPQSEEVDWSFPVLVEdVVMMGRYGHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 113 GFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLs 192
Cdd:PRK15056 110 GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL- 188
|
170
....*....|....
gi 2525300912 193 RQTDKTIFLSTHDL 206
Cdd:PRK15056 189 RDEGKTMLVSTHNL 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-173 |
5.15e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 96.61 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 15 YPGkgdVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV-ISVVLTEKC 93
Cdd:PRK10762 14 FPG---VKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 94 DIRNMSVVELIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPT 173
Cdd:PRK10762 90 LIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
26-209 |
6.83e-22 |
|
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: 92.50 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 26 DGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV----ISVV-----LtekcdIR 96
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLrarhVGFVfqsfqL-----LP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 97 NMSVVELIGL-----GRspytgfwgtlsKEDKAVVDKSIALVGiphLAHRMVH---TLSDGERQKVMIAKALAQETPVIY 168
Cdd:COG4181 104 TLTALENVMLplelaGR-----------RDARARARALLERVG---LGHRLDHypaQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2525300912 169 LDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELA 209
Cdd:COG4181 170 ADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
5-220 |
1.02e-21 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 91.62 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSiGYPGKGDV-KAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEI---GEYTDKQ 80
Cdd:TIGR02982 1 VISIRNLN-HYYGHGSLrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgaSKKQLVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVV---------LTEKCDIRnMSVvELIglgrsPYTGFwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGER 151
Cdd:TIGR02982 80 LRRRIGYIfqahnllgfLTARQNVQ-MAL-ELQ-----PNLSY-----QEARERARAMLEAVGLGDHLNYYPHNLSGGQK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELaLQIADKIWLMD 220
Cdd:TIGR02982 148 QRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRI-LDVADRILQME 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-233 |
1.64e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 93.63 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 24 VADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVISVVLTEKCDIRNMSVVEL 103
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 104 IGLGRSpytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVE 183
Cdd:PRK11432 99 VGYGLK----MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525300912 184 MMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK11432 175 MREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-221 |
1.73e-21 |
|
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: 90.99 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 9 ENLSIGYPGKGDVKaVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVV 88
Cdd:cd03248 15 QNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 89 LTEKCdIRNMSVVELI--GLGRSPYtgfwgtlsKEDKAVVDKSIALVGIPHLAH-------RMVHTLSDGERQKVMIAKA 159
Cdd:cd03248 94 GQEPV-LFARSLQDNIayGLQSCSF--------ECVKEAAQKAHAHSFISELASgydtevgEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 160 LAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLELaLQIADKIWLMDK 221
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLST-VERADQILVLDG 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
1.79e-21 |
|
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: 95.14 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETI-HIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKS----TLLRTLSAFQPKLGGNIFIEGKEIGE 75
Cdd:COG4172 1 MMSMPLlSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 76 YTDKQLSRV----ISVVLTEKcdirnMS-----------VVELIGLGRSpytgfwgtLSKedKAVVDKSIAL---VGIPH 137
Cdd:COG4172 81 LSERELRRIrgnrIAMIFQEP-----MTslnplhtigkqIAEVLRLHRG--------LSG--AAARARALELlerVGIPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 138 LAHRMV---HTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIAD 214
Cdd:COG4172 146 PERRLDaypHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFAD 225
|
250
....*....|....*....
gi 2525300912 215 KIWLMDKANGVTVGTPEDL 233
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAEL 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-258 |
1.79e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.33 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 31 GINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV----ISVVLTEKCDIRNMSVVELIGL 106
Cdd:PRK10070 50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTVLDNTAF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 107 GRSpytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQ 186
Cdd:PRK10070 130 GME----LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 187 LLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLNGS------------LSNFFARKGIAFDLET 254
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrtffrgvdISQVFSAKDIARRTPN 285
|
....
gi 2525300912 255 GLFR 258
Cdd:PRK10070 286 GLIR 289
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-232 |
6.76e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.88 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGY-PGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeyTDKQLSr 83
Cdd:PRK13637 2 SIKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI---TDKKVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 visvvLTekcDIRNMsvvelIGL--GRSPYTGFWGTLSK--------------EDKAVVDKSIALVGIPH--LAHRMVHT 145
Cdd:PRK13637 78 -----LS---DIRKK-----VGLvfQYPEYQLFEETIEKdiafgpinlglseeEIENRVKRAMNIVGLDYedYKDKSPFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGV 225
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
....*..
gi 2525300912 226 TVGTPED 232
Cdd:PRK13637 225 LQGTPRE 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-209 |
8.03e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 22 KAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGeytdkqLSRVISVV--LTEK--CDiRN 97
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------DPDVAEAChyLGHRnaMK-PA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 98 MSVVELIGlgrspytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLD 177
Cdd:PRK13539 88 LTVAENLE--------FWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|...
gi 2525300912 178 fPSKVEMMQLLHQLSRQTDKTIFLSTH-DLELA 209
Cdd:PRK13539 160 -AAAVALFAELIRAHLAQGGIVIAATHiPLGLP 191
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-234 |
1.40e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 89.48 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYP-----GKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRV---ISVVLTEKCDIRN--MSVVELIGLGRSPYTgfwgTLSK-EDKAVVDKSIALVGI-PHLAHRMVHTLSDGERQK 153
Cdd:TIGR02769 83 RRAFrrdVQLVFQDSPSAVNprMTVRQIIGEPLRHLT----SLDEsEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 154 VMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGV-TVGTPED 232
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVeECDVAQL 238
|
..
gi 2525300912 233 LS 234
Cdd:TIGR02769 239 LS 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-228 |
1.62e-20 |
|
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: 88.11 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTdkqlSRVI 85
Cdd:cd03269 1 LEVENVTKRF---GRVTAL-DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVE-LIGLGRspytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:cd03269 73 GYLPEERGLYPKMKVIDqLVYLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 165 PVIYLDEPTAFLDfPSKVE-MMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVG 228
Cdd:cd03269 148 ELLILDEPFSGLD-PVNVElLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-233 |
2.99e-20 |
|
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: 87.67 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCdIRNMSVVELIGLGRsPYTgfwgtlskeDKAVVDKSIALVGIPHLAHRMV-----------HTLSDGERQKV 154
Cdd:cd03254 80 GVVLQDTF-LFSGTIMENIRLGR-PNA---------TDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDfpskVEMMQLLHQ--LSRQTDKTIFLSTHDLElALQIADKIWLMDKANGVTVGTPED 232
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNID----TETEKLIQEalEKLMKGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDE 223
|
.
gi 2525300912 233 L 233
Cdd:cd03254 224 L 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-233 |
5.35e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.98 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGK-GDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:COG1135 2 IELENLSKTFPTKgGPVTAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ---ISVV------LTEKcdirnmSV-------VELIGLGRspytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSD 148
Cdd:COG1135 81 rrkIGMIfqhfnlLSSR------TVaenvalpLEIAGVPK-----------AEIRKRVAELLELVGLSDKADAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 149 GERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVG 228
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
....*
gi 2525300912 229 TPEDL 233
Cdd:COG1135 224 PVLDV 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-233 |
7.52e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.22 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 3 KETIHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLS 82
Cdd:COG1132 337 RGEIEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLtEKCDIRNMSVVELIGLGRSPYTgfwgtlskedKAVVDKSIALVGiphlAHRMVH---------------TLS 147
Cdd:COG1132 414 RQIGVVP-QDTFLFSGTIRENIRYGRPDAT----------DEEVEEAAKAAQ----AHEFIEalpdgydtvvgergvNLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 148 DGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLElALQIADKIWLMDKANGVTV 227
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRIVEQ 555
|
....*.
gi 2525300912 228 GTPEDL 233
Cdd:COG1132 556 GTHEEL 561
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
32-233 |
1.39e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAF-QPKLG----GNIFI----EGKEIgeytdKQLSRVISVVLT-EKCDIRNMSVV 101
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGkvtvGDIVVsstsKQKEI-----KPVRKKVGVVFQfPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 102 ELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIP-HLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPS 180
Cdd:PRK13643 104 KDVAFGPQNF----GIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 181 KVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-224 |
1.68e-19 |
|
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: 84.29 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLS-AFQPKLGgNIFIEGKEIGEYtDKQLSRV 84
Cdd:cd03247 1 LSINNVSFSYPEQE--QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTgDLKPQQG-EITLDGVPVSDL-EKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVvltekcdirnmsvveligLGRSPYTgFWGTLSKEdkavvdksialVGIPhlahrmvhtLSDGERQKVMIAKALAQET 164
Cdd:cd03247 77 ISV------------------LNQRPYL-FDTTLRNN-----------LGRR---------FSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLeLALQIADKIWLMDkaNG 224
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLE--NG 172
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-233 |
1.87e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeyTDKQLSRv 84
Cdd:COG4152 1 MLELKGLTKRF---GDKTAV-DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 isvvltekcdI----------RNMSVVE-LIGLGRspytgFWGtLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQ 152
Cdd:COG4152 73 ----------IgylpeerglyPKMKVGEqLVYLAR-----LKG-LSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 153 KVMIAKALAQETPVIYLDEPTAFLDfPSKVEMM-QLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPE 231
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLD-PVNVELLkDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
..
gi 2525300912 232 DL 233
Cdd:COG4152 215 EI 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-230 |
1.88e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 24 VADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgEYTDKQLSRVISVVLTEKCD--------- 94
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDpeqqifytd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 95 --------IRNMSVVEliglgrspytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPV 166
Cdd:PRK13638 95 idsdiafsLRNLGVPE-----------------AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 167 IYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIfLSTHDLELALQIADKIWLMDKANGVTVGTP 230
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVI-ISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-233 |
1.93e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 2 NKETIHIENLSIGY--PGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDK 79
Cdd:PRK13633 1 MNEMIKCKNVSYKYesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 QlsrvisvvltekcDIRNMS---------------VVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVH 144
Cdd:PRK13633 81 W-------------DIRNKAgmvfqnpdnqivatiVEEDVAFGPENL----GIPPEEIRERVDESLKKVGMYEYRRHAPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 145 TLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQiADKIWLMDKANG 224
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
....*....
gi 2525300912 225 VTVGTPEDL 233
Cdd:PRK13633 223 VMEGTPKEI 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-233 |
2.10e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.11 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLS-AFQPKlGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:PRK11160 339 LTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQ-QGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVlTEKCDIrnmsvveliglgrspytgFWGTL---------SKEDKAVVDksiAL--VGIPHLAH------------- 140
Cdd:PRK11160 416 ISVV-SQRVHL------------------FSATLrdnlllaapNASDEALIE---VLqqVGLEKLLEddkglnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 141 RmvhTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLeLALQIADKIWLMD 220
Cdd:PRK11160 474 R---QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL-TGLEQFDRICVMD 547
|
250
....*....|...
gi 2525300912 221 KANGVTVGTPEDL 233
Cdd:PRK11160 548 NGQIIEQGTHQEL 560
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-219 |
2.34e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKS----TLLRTLSAfqPK---LGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS--PPvvyPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRV----ISVVLTEKCDIRN------MSVVELIGLGRspytgfwGTLSKEDKAVVDKSIALVGIPHLAHRMV---HTLS 147
Cdd:PRK15134 86 LRGVrgnkIAMIFQEPMVSLNplhtleKQLYEVLSLHR-------GMRREAARGEILNCLDRVGIRQAAKRLTdypHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 148 DGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLM 219
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
32-233 |
3.42e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRVISVVLTEKCDIRNMSVVELIGLGRSpy 111
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYPHLSVAENMSFGLK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 112 tgfwgtLSKEDKAVVDKSIALVG-IPHLAH---RMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQL 187
Cdd:PRK11000 102 ------LAGAKKEEINQRVNQVAeVLQLAHlldRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2525300912 188 LHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK11000 176 ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
3.68e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.57 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQY--QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVVLtekcdirnmsvveliglgRSPYTGFWGTLSKEDKA---------------VVDKSIALVGIPHLAHRMVHT 145
Cdd:PRK13648 81 LRKHIGIVF------------------QNPDNQFVGSIVKYDVAfglenhavpydemhrRVSEALKQVDMLERADYEPNA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQiADKIWLMDKANGV 225
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVY 221
|
....*...
gi 2525300912 226 TVGTPEDL 233
Cdd:PRK13648 222 KEGTPTEI 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-221 |
3.99e-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: 84.56 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03245 3 IEFRNVSFSYPN--QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEkcdirnmsvVELiglgrspytgFWGTL---------SKEDKAVVdKSIALVGI-------PHLAHRMV----HT 145
Cdd:cd03245 81 GYVPQD---------VTL----------FYGTLrdnitlgapLADDERIL-RAAELAGVtdfvnkhPNGLDLQIgergRG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKvemMQLLHQLSRQT-DKTIFLSTHDLELaLQIADKIWLMDK 221
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQLLgDKTLIIITHRPSL-LDLVDRIIVMDS 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-221 |
4.73e-19 |
|
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: 84.24 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 9 ENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLG---GNIFIEGKEIgeyTDKQLSRVI 85
Cdd:cd03234 7 WDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIglgrsPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMV-HT----LSDGERQKVMIAKAL 160
Cdd:cd03234 84 AYVRQDDILLPGLTVRETL-----TYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIgGNlvkgISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqTDKTIFLSTH----DLelaLQIADKIWLMDK 221
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHqprsDL---FRLFDRILLLSS 219
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-233 |
4.82e-19 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 84.34 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 26 DGICAGINSGELTCLLGANGVGKSTLLRTLSAFQP----KLGGNIFIEGKEIGE--YTDKQLSRVISVVLTEKCDIRNMS 99
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPlsIRGRHIATIMQNPRTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 100 --VVELIGLGrspytgfwGTLSKEDKAVVDKSIALVGIPH---LAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTA 174
Cdd:TIGR02770 83 nhAIETLRSL--------GKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 175 FLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-220 |
5.97e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.12 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYP-----GKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 ---LSRVISVVLTEKCDIRN--MSVVELIGLGRSPYTgfwgTLSKEDKAV-VDKSIALVGI-PHLAHRMVHTLSDGERQK 153
Cdd:PRK10419 84 rkaFRRDIQMVFQDSISAVNprKTVREIIREPLRHLL----SLDKAERLArASEMLRAVDLdDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 154 VMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-237 |
7.26e-19 |
|
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: 84.20 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03251 1 VEFKNVTFRYPGDGP--PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCdIRNMSVVELIGLGRSPYTgfwgtlskeDKAVVDKSialvgipHLAHRM---------VHT--------LSD 148
Cdd:cd03251 79 GLVSQDVF-LFNDTVAENIAYGRPGAT---------REEVEEAA-------RAANAHefimelpegYDTvigergvkLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 149 GERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLElALQIADKIWLMDKANGVTVG 228
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERG 218
|
250
....*....|
gi 2525300912 229 TPEDL-SLNG 237
Cdd:cd03251 219 THEELlAQGG 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-252 |
7.61e-19 |
|
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: 84.13 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKaVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03249 1 IEFKNVSFRYPSRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKcDIRNMSVVELIGLGRSPytgfwGTLSKEDKAVVDKSIA--LVGIPHLAHRMV----HTLSDGERQKVMIAKA 159
Cdd:cd03249 80 GLVSQEP-VLFDGTIAENIRYGKPD-----ATDEEVEEAAKKANIHdfIMSLPDGYDTLVgergSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 160 LAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLeLALQIADKIWLMDKANGVTVGTPEDLslngsl 239
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDEL------ 224
|
250
....*....|...
gi 2525300912 240 snfFARKGIAFDL 252
Cdd:cd03249 225 ---MAQKGVYAKL 234
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-209 |
1.68e-18 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 82.78 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 9 ENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISV- 87
Cdd:TIGR02211 5 ENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 88 ---------VLTEKCDIRNMSVVELIGlgrspytgfwgTLSKEDKAvvDKSIALVGIPHLAHRMVH---TLSDGERQKVM 155
Cdd:TIGR02211 85 lgfiyqfhhLLPDFTALENVAMPLLIG-----------KKSVKEAK--ERAYEMLEKVGLEHRINHrpsELSGGERQRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELA 209
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
118-298 |
2.08e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 118 LSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDK 197
Cdd:PRK11144 101 MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 198 TIFLSTHDLELALQIADKIWLMDKANgvtvgtpedLSLNGSLSNFFA----RKGIAFDLETGLFRVaneytsriRLAGHG 273
Cdd:PRK11144 181 PILYVSHSLDEILRLADRVVVLEQGK---------VKAFGPLEEVWAssamRPWLPKEEQSSILKV--------TVLEHH 243
|
170 180
....*....|....*....|....*
gi 2525300912 274 QKYAMVRKALQRNGILANRnVESEI 298
Cdd:PRK11144 244 PHYAMTALALGDQHLWVNK-LDAPL 267
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-229 |
2.20e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.75 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQ-PKLG-----GNIFIEGKEIGEYTD 78
Cdd:PRK11124 2 SIQLNGINCFY---GAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEmPRSGtlniaGNHFDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 79 KQLSRVISVVLTEKCDIRNMSVVE-LIG-----LGrspytgfwgtLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGER 151
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQnLIEapcrvLG----------LSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSrQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGT 229
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-237 |
2.69e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYPGkgdVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKS-VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRV-ISVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTLS---KEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:PRK09700 77 AAQLgIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLN 236
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
.
gi 2525300912 237 G 237
Cdd:PRK09700 236 D 236
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-245 |
2.78e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.67 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPkLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:PRK11174 349 TIEAEDLEILSP---DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVV-----LTEKcdirnmSVVELIGLGRSpytgfwgTLSKED-KAVVDKSIALVGIPHLAHRMVHTLSD-------GER 151
Cdd:PRK11174 425 LSWVgqnpqLPHG------TLRDNVLLGNP-------DASDEQlQQALENAWVSEFLPLLPQGLDTPIGDqaaglsvGQA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtdKTIFLSTHDLElALQIADKIWLMDKANGVTVGTPE 231
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYA 568
|
250
....*....|....
gi 2525300912 232 DLSLNGslsNFFAR 245
Cdd:PRK11174 569 ELSQAG---GLFAT 579
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-216 |
3.18e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 10 NLSIGYPGkgdVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIG-EYTDKQLSRVISVV 88
Cdd:PRK11288 9 GIGKTFPG---VKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 89 LTEKCDIRNMSVVELIGLGRSPYTGfwGTLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVI 167
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPHKG--GIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525300912 168 YLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKI 216
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAI 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-233 |
3.92e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.60 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 22 KAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV---ISVVLTEKCDIRN- 97
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 98 -MSVVELIGlgrSPYTGFWGTLSKED-KAVVDKSIALVGI-PHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTA 174
Cdd:PRK15079 114 rMTIGEIIA---EPLRTYHPKLSRQEvKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 175 FLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-233 |
5.42e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 24 VADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEI--GEYTDKQLSRVISVVLTEKCDIRNMSVV 101
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 102 ELIGLGRSPYTGfwgtLSKED-KAVVDKSIALVGiphLAHRMVH---TLSDGERQKVMIAKALAQETPVIYLDEPTAFLD 177
Cdd:PRK09493 96 ENVMFGPLRVRG----ASKEEaEKQARELLAKVG---LAERAHHypsELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 178 FPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK09493 169 PELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-233 |
6.28e-18 |
|
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: 81.44 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 22 KAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV-ISVVLTEKCDIRNMSV 100
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 101 VELIGLgrspYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPS 180
Cdd:cd03218 93 EENILA----VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 181 KVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03218 169 VQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-216 |
7.67e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.39 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISV 87
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 88 ----------VLTEKCDIRNMSVVELiglgrspYTGfwgtlsKEDKAVVDKSIALVGIPHLAHRMVH---TLSDGERQKV 154
Cdd:PRK10535 87 hfgfifqryhLLSHLTAAQNVEVPAV-------YAG------LERKQRLLRAQELLQRLGLEDRVEYqpsQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQiADKI 216
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERV 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-236 |
7.96e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.48 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYT-DKQLSR 83
Cdd:PRK10895 3 TLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 VISVVLTEKCDIRNMSVVE-LIGLG--RSPYTgfwgTLSKEDKAvvDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKAL 160
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDnLMAVLqiRDDLS----AEQREDRA--NELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLN 236
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-233 |
1.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLRtlsafqpklggniFIEGKEIGEYTDKQ 80
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSK--KPALNDISFSIPRGSWTALIGHNGSGKSTISK-------------LINGLLLPDDNPNS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVVLTEKC--DIRnmsvvELIGL-GRSPYTGFWGTLSKEDKA---------------VVDKSIALVGIPHLAHRM 142
Cdd:PRK13640 66 KITVDGITLTAKTvwDIR-----EKVGIvFQNPDNQFVGATVGDDVAfglenravprpemikIVRDVLADVGMLDYIDSE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 143 VHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQiADKIWLMDKA 222
Cdd:PRK13640 141 PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDG 219
|
250
....*....|.
gi 2525300912 223 NGVTVGTPEDL 233
Cdd:PRK13640 220 KLLAQGSPVEI 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-220 |
1.42e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 22 KAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDkqlsrvisvvltekcDIRNM--- 98
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE---------------DTRLMfqd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 99 -------SVVELIGLGRSpytGFWgtlskEDKAVvdKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDE 171
Cdd:PRK11247 90 arllpwkKVIDNVGLGLK---GQW-----RDAAL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525300912 172 PTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIE 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-239 |
1.69e-17 |
|
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: 80.35 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVlTEKCDIRNMSVVELIGLGRSpytgfwgTLSKED------KAVVDKSIalVGIPHLAHRMVH----TLSDGERQKVM 155
Cdd:cd03253 78 GVV-PQDTVLFNDTIGYNIRYGRP-------DATDEEvieaakAAQIHDKI--MRFPDGYDTIVGerglKLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSrqTDKTIFLSTHDLELALQiADKIWLMDKANGVTVGTPEDLSL 235
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
....
gi 2525300912 236 NGSL 239
Cdd:cd03253 225 KGGL 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-233 |
2.00e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKeTIHIENLSIGYPGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK13642 1 MNK-ILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVVLTEKCD-IRNMSVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKA 159
Cdd:PRK13642 79 LRRKIGMVFQNPDNqFVGATVEDDVAFGMENQ----GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 160 LAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQiADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-233 |
2.82e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.31 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 19 GDVKAVADgICAGINSGELTCLLGANGVGKSTL---LRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV----ISVVLTE 91
Cdd:PRK09473 27 GDVTAVND-LNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNGREILNLPEKELNKLraeqISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 92 KCDIRN--MSV----VELIGLGRSpytgfwgtLSKEDkaVVDKSIAL---VGIPHLAHRMV---HTLSDGERQKVMIAKA 159
Cdd:PRK09473 106 PMTSLNpyMRVgeqlMEVLMLHKG--------MSKAE--AFEESVRMldaVKMPEARKRMKmypHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 160 LAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-219 |
2.96e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVVLTEKcdiRNMSVVEL---IGLGR 108
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPED---RQSSGLYLdapLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 109 SPYT----GFWgTLSKEDKAVVDKSIALVGIpHLAH--RMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKV 182
Cdd:PRK15439 363 CALThnrrGFW-IKPARENAVLERYRRALNI-KFNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190
....*....|....*....|....*....|....*..
gi 2525300912 183 EMMQLLHQLSRQTDKTIFLSThDLELALQIADKIWLM 219
Cdd:PRK15439 441 DIYQLIRSIAAQNVAVLFISS-DLEEIEQMADRVLVM 476
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-243 |
4.73e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY---GKIQAL-HEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSR-VISVVLTEKCDIRNMSVVELIGLGrspytGFWGtlskeDKAVVDKSIALVG--IPHLAHRMVH---TLSDGERQKV 154
Cdd:PRK11614 77 IMReAVAIVPEGRRVFSRMTVEENLAMG-----GFFA-----ERDQFQERIKWVYelFPRLHERRIQragTMSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLS 234
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
....*....
gi 2525300912 235 LNGSLSNFF 243
Cdd:PRK11614 226 ANEAVRSAY 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-236 |
4.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 2 NKETIHIENLSIGYPGK--GDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTD- 78
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqeNELVAL-NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 79 ---------------KQLSRVISVVL----------TEKCDIrnmsVVELIGLGRSPYtgfwgtlskEDKAVVDKSIALV 133
Cdd:PRK13631 97 helitnpyskkiknfKELRRRVSMVFqfpeyqlfkdTIEKDI----MFGPVALGVKKS---------EAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 134 GI--PHLaHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQlSRQTDKTIFLSTHDLELALQ 211
Cdd:PRK13631 164 GLddSYL-ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLE 241
|
250 260
....*....|....*....|....*
gi 2525300912 212 IADKIWLMDKANGVTVGTPEDLSLN 236
Cdd:PRK13631 242 VADEVIVMDKGKILKTGTPYEIFTD 266
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
5.13e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.19 E-value: 5.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKetIHIENLSIGYpgkGDVKaVADGICAGINSGELTCLLGANGVGKSTLLRTLSAF-----QPKLGGNIFIEGKEIGE 75
Cdd:PRK14247 1 MNK--IEIRDLKVSF---GQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 76 YTDKQLSRVISVVLTEKCDIRNMSVVELIGLGrsPYTGFWGTLSKEDKAVVDKSIALVGI-PHLAHRM---VHTLSDGER 151
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPE 231
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
....*
gi 2525300912 232 DLSLN 236
Cdd:PRK14247 231 EVFTN 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-218 |
5.64e-17 |
|
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: 78.30 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 20 DVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSrvisvvltekcdirnms 99
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR----------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 100 vvELIGLGRSPytGFWGTLSKE----------DKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYL 169
Cdd:cd03231 74 --GLLYLGHAP--GIKTTLSVLenlrfwhadhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525300912 170 DEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWL 218
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-245 |
6.49e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.31 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGkgdVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ-LSRVIS 86
Cdd:PRK10982 1 MSNISKSFPG---VKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 87 VVLTEKCDIRNMSVVELIGLGRSPYTGFW---GTLSKEDKAVVDKsialVGIPHLAHRMVHTLSDGERQKVMIAKALAQE 163
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLGRYPTKGMFvdqDKMYRDTKAIFDE----LDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 164 TPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLStHDLELALQIADKIWLMDKANGVTVGTPEDLSLNGSLSNFF 243
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMV 231
|
..
gi 2525300912 244 AR 245
Cdd:PRK10982 232 GR 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-233 |
6.56e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 24 VADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIG---------EYTDKQLSRVISVVLTEKCD 94
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 95 IRN----MSVVELIGLGRSPYTGFWGTLSKEdKAVvdKSIALVGIPHLAHRM--VHtLSDGERQKVMIAKALAQETPVIY 168
Cdd:PRK10619 100 HFNlwshMTVLENVMEAPIQVLGLSKQEARE-RAV--KYLAKVGIDERAQGKypVH-LSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 169 LDEPTAFLDfPSKV-EMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK10619 176 FDEPTSALD-PELVgEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-233 |
7.15e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 78.68 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03252 1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCdIRNMSVVELIGLGRspyTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMV----HTLSDGERQKVMIAKALA 161
Cdd:cd03252 79 GVVLQENV-LFNRSIRDNIALAD---PGMSMERVIEAAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSrqTDKTIFLSTHDLElALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-229 |
8.60e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 19 GDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQP--KLGGNIFIEGKEIGEYTDKQLSRV-ISVVLTEKCDI 95
Cdd:PRK13549 16 GGVKAL-DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAgIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 96 RNMSVVELIGLGRSPYTGfwGTLskEDKAVV---DKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEP 172
Cdd:PRK13549 95 KELSVLENIFLGNEITPG--GIM--DYDAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 173 TAFLDFPSKVEMMQLLHQLSRQTDKTIFLStHDLELALQIADKIWLMdkANGVTVGT 229
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACIYIS-HKLNEVKAISDTICVI--RDGRHIGT 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-266 |
9.66e-17 |
|
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: 78.60 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIG----EYTDKQLSRViSVVLTEKCDirnmsvveliGLG 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTV-RDLLSSITK----------DFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 108 RSPYtgfWGTlskedkavvdKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQL 187
Cdd:cd03237 91 THPY---FKT----------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 188 LHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGV--TVGTPEdlSLNGSLSNFFARKGIAF--DLETGLFRVaNEY 263
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVngVANPPQ--SLRSGMNRFLKNLDITFrrDPETGRPRI-NKL 234
|
...
gi 2525300912 264 TSR 266
Cdd:cd03237 235 GSV 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-221 |
9.77e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.95 E-value: 9.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSafqpklggnifieGKEIgeytdkqlsrvi 85
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------------GELE------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 svvltekcdirnmsvveliglgrsPYTGFWgtlskedkavvdKSIALVGIPHLAHrmvhtLSDGERQKVMIAKALAQETP 165
Cdd:cd03221 52 ------------------------PDEGIV------------TWGSTVKIGYFEQ-----LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 166 VIYLDEPTAFLDfpskVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03221 91 LLLLDEPTNHLD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELED 142
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-245 |
1.02e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.84 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYP-GKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLS-- 82
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHAL-NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 -RVISVV------LTEKCDIRNMSV-VELIGLGRspytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKV 154
Cdd:PRK11153 81 rRQIGMIfqhfnlLSSRTVFDNVALpLELAGTPK-----------AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDkaNGVTVGTpedls 234
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVID--AGRLVEQ----- 222
|
250
....*....|.
gi 2525300912 235 lnGSLSNFFAR 245
Cdd:PRK11153 223 --GTVSEVFSH 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-209 |
1.21e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYPgKGDVKA-VADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEI------ 73
Cdd:PRK11629 1 MNKILLQCDNLCKRYQ-EGSVQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 74 --GEYTDKQLSRVISV--VLTEKCDIRNMSVVELIGlGRSPytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDG 149
Cdd:PRK11629 80 akAELRNQKLGFIYQFhhLLPDFTALENVAMPLLIG-KKKP---------AEINSRALEMLAAVGLEHRANHRPSELSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 150 ERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELA 209
Cdd:PRK11629 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-238 |
1.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.62 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:PRK13650 5 IEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVE---LIGLGRSpytgfwGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQ 162
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEddvAFGLENK------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 163 ETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDL-ELALqiADKIWLMDKANGVTVGTPEDLSLNGS 238
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLdEVAL--SDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-214 |
1.41e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.15 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQpKLGGNIFIEGKEigEYTDK------ 79
Cdd:PRK14258 8 IKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRV--EFFNQniyerr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 ----QLSRVISVVLTeKCDIRNMSVVELIGLGrSPYTGFWGTLSKEDkaVVDKSIALVG----IPHLAHRMVHTLSDGER 151
Cdd:PRK14258 81 vnlnRLRRQVSMVHP-KPNLFPMSVYDNVAYG-VKIVGWRPKLEIDD--IVESALKDADlwdeIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIAD 214
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-233 |
4.91e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKaVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCdIRNMSVVELIGLGRSPYTgfwgtlSKEDKAVVDKSIA---LVGIPHLAHRMV----HTLSDGERQKVMIAK 158
Cdd:TIGR00958 558 ALVGQEPV-LFSGSVRENIAYGLTDTP------DEEIMAAAKAANAhdfIMEFPNGYDTEVgekgSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 159 ALAQETPVIYLDEPTAFLDfpskVEMMQLLHQLSRQTDKTIFLSTHDLELAlQIADKIWLMDKANGVTVGTPEDL 233
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQL 700
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-233 |
9.05e-16 |
|
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: 75.39 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:TIGR04406 1 TLVAENLIKSYKKR----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 -ISVVLTEKCDIRNMSVVE--LIGLGRSPytgfwgTLSK-EDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKAL 160
Cdd:TIGR04406 77 gIGYLPQEASIFRKLTVEEniMAVLEIRK------DLDRaEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-211 |
1.05e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLsafqpklggnifiegkeIGEYTDKQLSRVIsVVLTEKCDiRNMSVVELIGlgrspy 111
Cdd:COG2401 53 IEPGEIVLIVGASGSGKSTLLRLL-----------------AGALKGTPVAGCV-DVPDNQFG-REASLIDAIG------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 112 tgfwgtlSKEDKAVVDKSIALVGI--PHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLH 189
Cdd:COG2401 108 -------RKGDFKDAVELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180
....*....|....*....|....
gi 2525300912 190 QLSRQTDKTIFLSTH--DLELALQ 211
Cdd:COG2401 181 KLARRAGITLVVATHhyDVIDDLQ 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-233 |
1.24e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGY----PGKGdvKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTD--- 78
Cdd:PRK13649 3 INLQNVSYTYqagtPFEG--RALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 79 -KQLSRVISVVLT-EKCDIRNMSVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPH-LAHRMVHTLSDGERQKVM 155
Cdd:PRK13649 80 iKQIRKKVGLVFQfPESQLFEETVLKDVAFGPQNF----GVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-233 |
1.27e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 2 NKETIHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGK---------- 71
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 72 EIGEYTDKQLSRV----ISVVLTEKCDIRN--MSVVELIGLGRSPYTGfwgtLSKEDK-AVVDKSIALVGIPH---LAHR 141
Cdd:PRK10261 89 ELSEQSAAQMRHVrgadMAMIFQEPMTSLNpvFTVGEQIAESIRLHQG----ASREEAmVEAKRMLDQVRIPEaqtILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 142 MVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
250
....*....|..
gi 2525300912 222 ANGVTVGTPEDL 233
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-236 |
2.08e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgkGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTL---SAFQPK--LGGNIFIEGKEI-G 74
Cdd:PRK14239 1 MTEPILQVSDLSVYY---NKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEvtITGSIVYNGHNIyS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 75 EYTDK-QLSRVISVVLtEKCDIRNMSVVELIGLGRSpYTGFwgtlskEDKAVVDKSI--ALVG------IPHLAHRMVHT 145
Cdd:PRK14239 77 PRTDTvDLRKEIGMVF-QQPNPFPMSIYENVVYGLR-LKGI------KDKQVLDEAVekSLKGasiwdeVKDRLHDSALG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsrQTDKTIFLSTHDLELALQIADKIWLMDKANGV 225
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
250
....*....|.
gi 2525300912 226 TVGTPEDLSLN 236
Cdd:PRK14239 227 EYNDTKQMFMN 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-233 |
2.18e-15 |
|
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: 76.76 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 3 KETIHIENLSIGYPG--KGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIE-GKEIGEYTDK 79
Cdd:TIGR03269 277 EPIIKVRNVSKRYISvdRGVVKAV-DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 ------QLSRVISVVLTEKCDIRNMSVV----ELIGLG--------RSPYT----GFwgtlsKEDKAVvdksialvgipH 137
Cdd:TIGR03269 356 gpdgrgRAKRYIGILHQEYDLYPHRTVLdnltEAIGLElpdelarmKAVITlkmvGF-----DEEKAE-----------E 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 138 LAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIW 217
Cdd:TIGR03269 420 ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAA 499
|
250
....*....|....*.
gi 2525300912 218 LMDKANGVTVGTPEDL 233
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEI 515
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-233 |
2.20e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIE--NLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTD 78
Cdd:PRK13536 35 GSMSTVAIDlaGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 79 KQLSRVISVVLTEKCDiRNMSVVE-LIGLGRspytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIA 157
Cdd:PRK13536 111 LARARIGVVPQFDNLD-LEFTVREnLLVFGR-----YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 158 KALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-233 |
2.68e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.40 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAF-QPKLG----GNIFIEG-KEIGEYTD 78
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeQPEAGtirvGDITIDTaRSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 79 --KQLSRVISVVLTEKCDIRNMSVVELIGLGrsPYTgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:PRK11264 79 liRQLRQHVGFVFQNFNLFPHRTVLENIIEG--PVI-VKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDfPSKV-EMMQLLHQLSrQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALD-PELVgEVLNTIRQLA-QEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-233 |
3.54e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.84 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 22 KAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVVLTEKCDiRNMSVV 101
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLD-PDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 102 E-LIGLGRspytgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPS 180
Cdd:PRK13537 99 EnLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 181 KVEMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13537 174 RHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-211 |
4.30e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 26 DGICAGINSGELTCLLGANGVGKSTLLRTLSAFQ-PKLGG-NIFIEGKEIGEYTDKQLSRVISVVLTEKC--------DI 95
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlPDTGTiEWIFKDEKNKKKTKEKEKVLEKLVIQKTRfkkikkikEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 96 RN-MSVV--------------ELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIP-HLAHRMVHTLSDGERQKVMIAKA 159
Cdd:PRK13651 104 RRrVGVVfqfaeyqlfeqtieKDIIFGPVSM----GVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 160 LAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQ 211
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLE 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-216 |
4.32e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.02 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 19 GDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQP--KLGGNIFIEGKEIGEYTDKQLSRV-ISVVLTEKCDI 95
Cdd:TIGR02633 12 GGVKAL-DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 96 RNMSVVELIGLGRSpyTGFWGTLSKEDKAV--VDKSIALVGIPHL-AHRMVHTLSDGERQKVMIAKALAQETPVIYLDEP 172
Cdd:TIGR02633 91 PELSVAENIFLGNE--ITLPGGRMAYNAMYlrAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525300912 173 TAFLDFPSKVEMMQLLHQLSRQTDKTIFLStHDLELALQIADKI 216
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAVCDTI 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-216 |
4.34e-15 |
|
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: 73.94 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 34 SGELTCLLGANGVGKSTLLRTLSA-FQPKLGGNI----------FIEGKEIGEYTDKQLSRVISVvltekcdIRNMSVVE 102
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDdppdwdeildEFRGSELQNYFTKLLEGDVKV-------IVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 103 LIglgrsP--YTGFWGTL--SKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDF 178
Cdd:cd03236 98 LI-----PkaVKGKVGELlkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 2525300912 179 PSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKI 216
Cdd:cd03236 173 KQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-234 |
6.52e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeytdkQLSRVISVV------LTEkcD------IRNMSVVE 102
Cdd:COG1129 278 GEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV------RIRSPRDAIragiayVPE--DrkgeglVLDLSIRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 103 LIGLGRSPYTGFWGTLS-KEDKAVVDKSIALVGI-PHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPS 180
Cdd:COG1129 350 NITLASLDRLSRGGLLDrRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 181 KVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMdkANGVTVG--TPEDLS 234
Cdd:COG1129 430 KAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVM--REGRIVGelDREEAT 482
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-256 |
7.10e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.35 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 21 VKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSafqpklG------GNIFIEG----KEigeytDKQLSRVISVVLT 90
Cdd:COG4586 35 VEAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLT------GilvptsGEVRVLGyvpfKR-----RKEFARRIGVVFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 91 EKC----DIrnmSVVELIGLGRSPYTgfwgtLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETP 165
Cdd:COG4586 103 QRSqlwwDL---PAIDSFRLLKAIYR-----IPDAEyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKanGVTVgtpEDLSLNGSLSNFFAR 245
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH--GRII---YDGSLEELKERFGPY 249
|
250
....*....|.
gi 2525300912 246 KGIAFDLETGL 256
Cdd:COG4586 250 KTIVLELAEPV 260
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-233 |
7.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGY-PGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTD----K 79
Cdd:PRK13641 2 SIKFENVDYIYsPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 QLSRVISVVLT-EKCDIRNMSVVELIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGIPH-LAHRMVHTLSDGERQKVMIA 157
Cdd:PRK13641 82 KLRKKVSLVFQfPEAQLFENTVLKDVEFGPKNF----GFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 158 KALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-259 |
8.34e-15 |
|
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: 75.21 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSafqpklgGNIFIEGKEIgeytDKQLSrvISV---VLTEKCDirnMSVVELIglgR 108
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEV----DEDLK--ISYkpqYISPDYD---GTVEEFL---R 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 109 SPYTGFWGTlSKEDKAVVDKsialVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLL 188
Cdd:COG1245 424 SANTDDFGS-SYYKTEIIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 189 HQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGV--TVGTPEDLS--LNGSLSNFfarkGIAF--DLETGLFRV 259
Cdd:COG1245 499 RRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVhgHASGPMDMRegMNRFLKEL----GITFrrDEETGRPRI 571
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-248 |
9.55e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.08 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 27 GICAGINSGELTCLLGANGVGKSTLLRTLSAFQPK---LGGNIFIEGKEIGEytdKQLSRVISVVLTEKCDIRNMSVVE- 102
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTLTVREh 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 103 -----LIGLGRSPYTgfwgtlsKEDKAVVDKSIALVGIPHLAH------RMVHTLSDGERQKVMIAKALAQETPVIYLDE 171
Cdd:TIGR00955 120 lmfqaHLRMPRRVTK-------KEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 172 PTAFLDFPSKVEMMQLLHQLSrQTDKTIFLSTHDLELAL-QIADKIWLMDKANGVTVGTPEDlslngsLSNFFARKGI 248
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQ------AVPFFSDLGH 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-219 |
1.03e-14 |
|
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: 74.72 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 9 ENLSIGYPGK--------GDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKlGGNIFIEGKEIGEYTDKQ 80
Cdd:COG4172 279 RDLKVWFPIKrglfrrtvGHVKAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 ---LSRVISVV-------LtekcDIRnMSVVELIGLG-RSPYTGfwgtLSKEDK-AVVDKSIALVGI-PHLAHRMVHTLS 147
Cdd:COG4172 357 lrpLRRRMQVVfqdpfgsL----SPR-MTVGQIIAEGlRVHGPG----LSAAERrARVAEALEEVGLdPAARHRYPHEFS 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 148 DGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKT-IFLStHDLELALQIADKIWLM 219
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAyLFIS-HDLAVVRALAHRVMVM 499
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
146-233 |
1.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.28 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGV 225
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
....*...
gi 2525300912 226 TVGTPEDL 233
Cdd:PRK13646 226 SQTSPKEL 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-219 |
1.23e-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: 70.92 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKG---DVKAvadgicaginsGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKeigeytdkqlsrv 84
Cdd:cd03215 7 VRGLSVKGAVRDvsfEVRA-----------GEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 isvvltekcDIRNMSVVELI--GLGRSPytgfwgtlskEDK----AVVDKSIAL-VGIPHLahrmvhtLSDGERQKVMIA 157
Cdd:cd03215 63 ---------PVTRRSPRDAIraGIAYVP----------EDRkregLVLDLSVAEnIALSSL-------LSGGNQQKVVLA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 158 KALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLM 219
Cdd:cd03215 117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVM 177
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-237 |
1.50e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 3 KETIHIENLSIGYPGKGdvKAVADgICAGINSGELTCLLGANGVGKSTLLRTLS-AFQPKlGGNIFIEGKEIGEYTDKQL 81
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSR--QGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQ-SGRILIDGTDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 82 SRVISVVLTEKCdIRNMSVVELIGLGRSPYTgfwgtlSKEDKAVVDKSIALVGIPHLAHR---MV----HTLSDGERQKV 154
Cdd:PRK13657 408 RRNIAVVFQDAG-LFNRSIEDNIRVGRPDAT------DEEMRAAAERAQAHDFIERKPDGydtVVgergRQLSGGERQRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqtDKTIFLSTHDLElALQIADKIWLMDKANGVTVGTPEDLS 234
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDELV 557
|
...
gi 2525300912 235 LNG 237
Cdd:PRK13657 558 ARG 560
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
8-233 |
1.56e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.40 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPG-KGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKlggN-------IFIEGKEIGEYTDK 79
Cdd:COG4170 6 IRNLTIEIDTpQGRVKAV-DRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD---NwhvtadrFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 QLSRVISvvltekcdiRNMSVV-----------ELIG------LGRSPYTGFWGTLSKEDKAvvdKSIAL---VGIPHla 139
Cdd:COG4170 82 ERRKIIG---------REIAMIfqepsscldpsAKIGdqlieaIPSWTFKGKWWQRFKWRKK---RAIELlhrVGIKD-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 140 HRMV-----HTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIAD 214
Cdd:COG4170 148 HKDImnsypHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWAD 227
|
250
....*....|....*....
gi 2525300912 215 KIWLMDKANGVTVGTPEDL 233
Cdd:COG4170 228 TITVLYCGQTVESGPTEQI 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-227 |
2.25e-14 |
|
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: 70.66 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGK--GDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLS--AFQPKLGGNIFIEGKEIGEytdKQ 80
Cdd:cd03213 3 TLSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVVLTEKCDIRNMSVVEliglgrspytgfwgTLskedkavvDKSIALVGIphlahrmvhtlSDGERQKVMIAKAL 160
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRE--------------TL--------MFAAKLRGL-----------SGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSrQTDKTIFLSTHDL-ELALQIADKIWLMdkANGVTV 227
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPsSEIFELFDKLLLL--SQGRVI 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-239 |
2.62e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKG--DVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEG-------KEIGEY 76
Cdd:PRK13645 7 IILDNVSYTYAKKTpfEFKAL-NNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 77 tdKQLSRVISVVLT-EKCDIRNMSVVELIGLGrsPYTgfWGTLSKEDKAVVDKSIALVGIPH-LAHRMVHTLSDGERQKV 154
Cdd:PRK13645 86 --KRLRKEIGLVFQfPEYQLFQETIEKDIAFG--PVN--LGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLS 234
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
....*
gi 2525300912 235 LNGSL 239
Cdd:PRK13645 240 SNQEL 244
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-223 |
3.77e-14 |
|
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: 69.55 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03246 1 LEVENVSFRYPGAE--PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEkcdirnmsvVELiglgrspytgFWGTLSKedkavvdksialvgiphlahrmvHTLSDGERQKVMIAKALAQETP 165
Cdd:cd03246 79 GYLPQD---------DEL----------FSGSIAE-----------------------NILSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDLELaLQIADKIWLMDKAN 223
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPET-LASADRILVLEDGR 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-233 |
3.94e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 10 NLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKL-----GGNIFIEGKEIGEYTDKQLSRV 84
Cdd:PRK14271 26 NLTLGFAGK----TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrySGDVLLGGRSIFNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKCDIRNMSVVELIGLGRSPYTgfwGTLSKEDKAVVDKSIALVGI-PHLAHRMVHT---LSDGERQKVMIAKAL 160
Cdd:PRK14271 102 RVGMLFQRPNPFPMSIMDNVLAGVRAHK---LVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 161 AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTdkTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-234 |
4.98e-14 |
|
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: 72.53 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKavadGICAGINSGELTCLLGANGVGKSTL---LRTLSAFQPKLGGNIFIEGK-------EIGE 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLK----NISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIIYHVALcekcgyvERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 76 YTDKQLSRVISVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTLS-KEDKAV------------------VDKSIALVGIP 136
Cdd:TIGR03269 77 KVGEPCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlYGDDTVldnvlealeeigyegkeaVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 137 HLAHRMVHT---LSDGERQKVMIAKALAQETPVIYLDEPTAFLDfPSKVEMM-QLLHQLSRQTDKTIFLSTHDLELALQI 212
Cdd:TIGR03269 157 QLSHRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|..
gi 2525300912 213 ADKIWLMDKANGVTVGTPEDLS 234
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-233 |
8.39e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 20 DVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAF------QPKLGGNIFIEGKEIGEYTDKQLSRVISVVLTEKC 93
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 94 DIRNMSVVELIGLgrsPYTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHT----LSDGERQKVMIAKALAQETPVIYL 169
Cdd:PRK14246 101 PFPHLSIYDNIAY---PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 170 DEPTAFLDFPSKVEMMQLLHQLSRQTdkTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-230 |
1.01e-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: 72.35 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 36 ELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKqLSRVISVVLTEKCDIRNMSVVELIGLgrspYTGFW 115
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLGMCPQHNILFHHLTVAEHILF----YAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 116 GTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLhqLSRQT 195
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
170 180 190
....*....|....*....|....*....|....*
gi 2525300912 196 DKTIFLSTHDLELALQIADKIWLMDKANGVTVGTP 230
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-233 |
1.22e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.59 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:PRK11176 342 IEFRNVTFTYPGK-EVPALRN-INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVlTEKCDIRNMSVVELIGLGRSpytgfwGTLSKED--KAVvdksialvgipHLAHRM---------VHT--------L 146
Cdd:PRK11176 420 ALV-SQNVHLFNDTIANNIAYART------EQYSREQieEAA-----------RMAYAMdfinkmdngLDTvigengvlL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 147 SDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsrQTDKTIFLSTHDLElALQIADKIWLMDKANGVT 226
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVE 558
|
....*..
gi 2525300912 227 VGTPEDL 233
Cdd:PRK11176 559 RGTHAEL 565
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-233 |
1.51e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 2 NKETIHIENLSIGYPGkgdvkAVADGICAGINSGELTCLLGANGVGKS----TLLRTLSAFQPKLGGNIFIEGKEIGEYT 77
Cdd:PRK10418 1 MPQQIELRNIALQAAQ-----PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 78 DKqlSRVISVVLTEKCD----IRNMS--VVE-LIGLGRSPytgfwgtlskeDKAVVDKSIALVGIPHlAHRMVHT----L 146
Cdd:PRK10418 76 LR--GRKIATIMQNPRSafnpLHTMHthAREtCLALGKPA-----------DDATLTAALEAVGLEN-AARVLKLypfeM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 147 SDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVT 226
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
....*..
gi 2525300912 227 VGTPEDL 233
Cdd:PRK10418 222 QGDVETL 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-220 |
1.52e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 3 KETIHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFI-EGKEIGeYTDKQL 81
Cdd:COG0488 313 KKVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIG-YFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 82 S------RVISVVLTEKCDIRNMSVVELigLGRSpytGFwgtlSKEDkavvdksialvgiphlAHRMVHTLSDGERQKVM 155
Cdd:COG0488 388 EeldpdkTVLDELRDGAPGGTEQEVRGY--LGRF---LF----SGDD----------------AFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDfpskVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFE 503
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-206 |
1.63e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLS-AFQPKLGG--------NIfIE---GKEIGEYTDKQLSRVISVVltekcdiRNMSVVE 102
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSgELIPNLGDyeeepswdEV-LKrfrGTELQNYFKKLYNGEIKVV-------HKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 103 LIglgrsPYTgFWGT----LSKEDKA-VVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLD 177
Cdd:PRK13409 171 LI-----PKV-FKGKvrelLKKVDERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*....
gi 2525300912 178 FPSKVEMMQLLHQLSRqtDKTIFLSTHDL 206
Cdd:PRK13409 245 IRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-220 |
2.06e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIE-GKEIG-------EYTDK 79
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGylpqeppLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 qlsRVISVVLTEKCDIRNMsVVELIGLGRSPYTGF-----WGTLSKEDKAV--------VDKSIALVGIPHLAH-RMVHT 145
Cdd:COG0488 77 ---TVLDTVLDGDAELRAL-EAELEELEAKLAEPDedlerLAELQEEFEALggweaearAEEILSGLGFPEEDLdRPVSE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDfpskVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-233 |
2.22e-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: 71.20 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 2 NKETI-HIENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeytdkq 80
Cdd:TIGR01257 1933 NKTDIlRLNELTKVYSGTS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------- 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 lsrvisvvLTEKCDI-RNM------SVVELIGLGRSP---YTGFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGE 150
Cdd:TIGR01257 2004 --------LTNISDVhQNMgycpqfDAIDDLLTGREHlylYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGN 2075
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 151 RQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTP 230
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
...
gi 2525300912 231 EDL 233
Cdd:TIGR01257 2155 QHL 2157
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
132-233 |
2.50e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 132 LVGIPHLAHRM---VHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLEL 208
Cdd:PRK11022 137 QVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAL 216
|
90 100
....*....|....*....|....*
gi 2525300912 209 ALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:PRK11022 217 VAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-206 |
3.35e-13 |
|
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: 70.20 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 34 SGELTCLLGANGVGKSTLLRTLS-AFQPKLGgNI-----------FIEGKEIGEYTDKQLSRVISVVLTEKcdirnmsVV 101
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSgELKPNLG-DYdeepswdevlkRFRGTELQDYFKKLANGEIKVAHKPQ-------YV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 102 ELIGlgRSpytgFWGT----LSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFL 176
Cdd:COG1245 170 DLIP--KV----FKGTvrelLEKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|
gi 2525300912 177 DFPSKVEMMQLLHQLSRQtDKTIFLSTHDL 206
Cdd:COG1245 244 DIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-230 |
3.96e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 67.52 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03244 3 IEFKNVSLRY--RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVV-----------------LTEKCDIRNMSVVELIGLgrspyTGFWGTLSKEDKAVVDKSIAlvgiphlahrmvhTLSD 148
Cdd:cd03244 81 SIIpqdpvlfsgtirsnldpFGEYSDEELWQALERVGL-----KEFVESLPGGLDTVVEEGGE-------------NLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 149 GERQKVMIAKALAQETPVIYLDEPTAFLDfpskVEMMQLLHQLSRQ--TDKTIFLSTHDLELALQiADKIWLMDKANGVT 226
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVD----PETDALIQKTIREafKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
....
gi 2525300912 227 VGTP 230
Cdd:cd03244 218 FDSP 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-219 |
4.03e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.22 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 17 GKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEY---TDKQLSRVISVV----- 88
Cdd:PRK11308 24 PERLVKAL-DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVfqnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 89 ------------LTEKCDIrNMSvveligLGRspytgfwgtlsKEDKAVVDKSIALVGI-PHLAHRMVHTLSDGERQKVM 155
Cdd:PRK11308 103 gslnprkkvgqiLEEPLLI-NTS------LSA-----------AERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKT-IFLStHDLELALQIADKIWLM 219
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSyVFIS-HDLSVVEHIADEVMVM 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-233 |
4.24e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.75 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKgdvkAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:COG1137 3 TLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 -ISVVLTEKCDIRNMSV-------VELIGLGRspytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMI 156
Cdd:COG1137 79 gIGYLPQEASIFRKLTVednilavLELRKLSK-----------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 157 AKALAQETPVIYLDEPTAFLDfPSKV-EMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVD-PIAVaDIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
8-233 |
4.93e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.06 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGY-PGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKlggNIFIEGKEIgEYTDKQLSRvIS 86
Cdd:PRK15093 6 IRNLTIEFkTSDGWVKAV-DRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD---NWRVTADRM-RFDDIDLLR-LS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 87 VVLTEKCDIRNMSVV-----------ELIG------LGRSPYTGFWGTLSKEDKAVVDKSIALVGIP---HLAHRMVHTL 146
Cdd:PRK15093 80 PRERRKLVGHNVSMIfqepqscldpsERVGrqlmqnIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKdhkDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 147 SDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVT 226
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
....*..
gi 2525300912 227 VGTPEDL 233
Cdd:PRK15093 240 TAPSKEL 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-221 |
7.99e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.42 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLS-IGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:COG1101 2 LELKNLSkTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVV----LTEKCdiRNMSVVE--LIGLGRSPYTGFWGTLSKEDKAVVDKSIALVGIpHLAHRM---VHTLSDGERQKVM 155
Cdd:COG1101 82 IGRVfqdpMMGTA--PSMTIEEnlALAYRRGKRRGLRRGLTKKRRELFRELLATLGL-GLENRLdtkVGLLSGGQRQALS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDfPSKVEM-MQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALD-PKTAALvLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHE 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-215 |
8.79e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 9 ENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQP-----KLGGNIFIEGKEI--GEYTDKQL 81
Cdd:PRK14243 14 ENLNVYY---GSFLAVKN-VWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 82 SRVISVVLtEKCDIRNMSVVELIGLGrSPYTGFWGTLSKedkaVVDKSIALVGIPHLAHRMVHT----LSDGERQKVMIA 157
Cdd:PRK14243 90 RRRIGMVF-QKPNPFPKSIYDNIAYG-ARINGYKGDMDE----LVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 158 KALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTdkTIFLSTHDLELALQIADK 215
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDM 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-207 |
1.08e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKG-------DVKAVADGICAGINSGELTCLLGANGVGKST----LLRTLSAfqpklGGNIFIEGKEIGEY 76
Cdd:PRK15134 278 VEQLQVAFPIRKgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 77 TDKQL---SRVISVVLTEKCDIRN--MSVVELIGLGRSPYTGfwgTLSKEDK-AVVDKSIALVGI-PHLAHRMVHTLSDG 149
Cdd:PRK15134 353 NRRQLlpvRHRIQVVFQDPNSSLNprLNVLQIIEEGLRVHQP---TLSAAQReQQVIAVMEEVGLdPETRHRYPAEFSGG 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 150 ERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLL------HQLSrqtdkTIFLStHDLE 207
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLkslqqkHQLA-----YLFIS-HDLH 487
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-227 |
1.08e-12 |
|
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: 65.73 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSA--FQPKLGGNIFIEGKEIgeytDKQLSR 83
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPL----DKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 VISVVltEKCDIR--NMSVVELIGLgrspytgfwgtlskedkavvdkSIALVGiphlahrmvhtLSDGERQKVMIAKALA 161
Cdd:cd03232 80 STGYV--EQQDVHspNLTVREALRF----------------------SALLRG-----------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqTDKTIFLSTHD-LELALQIADKIWLMDKaNGVTV 227
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQpSASIFEKFDRLLLLKR-GGKTV 189
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-224 |
1.22e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 66.20 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGK---EIGEYTDKQLSRVISVVLTEKCDIRNMSVVELIGLGr 108
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFG- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 109 SPYTgfwgtlSKEDKAVVDK-----SIALvgIPH-----LAHRMVHtLSDGERQKVMIAKALAQETPVIYLDEPTAFLDF 178
Cdd:cd03290 103 SPFN------KQRYKAVTDAcslqpDIDL--LPFgdqteIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525300912 179 PSKVEMMQL-LHQLSRQTDKTIFLSTHDLELaLQIADkiWLMDKANG 224
Cdd:cd03290 174 HLSDHLMQEgILKFLQDDKRTLVLVTHKLQY-LPHAD--WIIAMKDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-247 |
1.51e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLR-TLSAFQPKLGGNIFIEGKEIGeYTDKQLSRV 84
Cdd:PRK09544 5 VSLENVSVSF---GQRRVLSD-VSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAPDEGVIKRNGKLRIG-YVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKcdiRNMSVveliglgrSPYTgfwgtlskeDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:PRK09544 80 TTLPLTVN---RFLRL--------RPGT---------KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 165 PVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKaNGVTVGTPEDLSLNGSLSNFFA 244
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPEFISMFG 218
|
...
gi 2525300912 245 RKG 247
Cdd:PRK09544 219 PRG 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-219 |
1.93e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 20 DVKAVADgICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIgeytdKQLSRVISV-----VLTE--- 91
Cdd:PRK09700 275 DRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI-----SPRSPLDAVkkgmaYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 92 ------KCDI-RNMSVVELIGLGRspYTGFWGTL-SKEDKAVVDKSIALVGIP-HLAHRMVHTLSDGERQKVMIAKALAQ 162
Cdd:PRK09700 349 dngffpNFSIaQNMAISRSLKDGG--YKGAMGLFhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 163 ETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQIADKIWLM 219
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF 482
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-215 |
2.06e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 66.21 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDVKAVADgICAGINSGELTCLLGANGVGKSTLLRTL---SAFQP--KLGGNIFIEGKEIgeytdkq 80
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKD-INLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPgaRVEGEILLDGEDI------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVVltekcDIR----------N---MSVVELIGLG---RspytgfwGTLSKED-KAVVDKSIALVGIP-----HL 138
Cdd:COG1117 81 YDPDVDVV-----ELRrrvgmvfqkpNpfpKSIYDNVAYGlrlH-------GIKSKSElDEIVEESLRKAALWdevkdRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 139 aHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDfP---SKVEmmQLLHQLSRQTdkTIFLSTHDLELALQIADK 215
Cdd:COG1117 149 -KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD-PistAKIE--ELILELKKDY--TIVIVTHNMQQAARVSDY 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-220 |
5.25e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 64.38 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 24 VADGICAGINSGELTCLLGANGVGKSTLLRTLSA-FQPKlGGNIFIEG--------------------KEIGeYTdKQLS 82
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPD-SGSILVRHdggwvdlaqaspreilalrrRTIG-YV-SQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTEkcDIrnmsVVE-LIGLGRSPYTGfwgtlskEDKAvvdKSI-ALVGIP-HLAHRMVHTLSDGERQKVMIAKA 159
Cdd:COG4778 103 RVIPRVSAL--DV----VAEpLLERGVDREEA-------RARA---RELlARLNLPeRLWDLPPATFSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 160 LAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQ--TDKTIFlstHDLELALQIADKIWLMD 220
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgtAIIGIF---HDEEVREAVADRVVDVT 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-208 |
8.75e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ---LS 82
Cdd:PRK10908 2 IRFEHVSKAYLGG---RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTEKCDIRNMSVVELIGLgrsPYTgFWGTLSKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQ 162
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAI---PLI-IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2525300912 163 ETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRqTDKTIFLSTHDLEL 208
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGL 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-207 |
1.72e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.88 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 7 HIENLSIGYPGKGDVKAVadgiCAGINSGELTCLLGANGVGKSTLLRTLSAFQP---KLGGNIFIEGKEIgeyTDKQ-LS 82
Cdd:COG4136 3 SLENLTITLGGRPLLAPL----SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRL---TALPaEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTEKCDIRNMSVVELIGLGRSPytgfwgTLSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALA 161
Cdd:COG4136 76 RRIGILFQDDLLFPHLSVGENLAFALPP------TIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLE 207
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-266 |
1.72e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLS-AFQPKlGGNIFIEGKeigeytdkqlsrvISV----VLTEKcdirNMSVVELIG- 105
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAgVLKPD-EGEVDPELK-------------ISYkpqyIKPDY----DGTVEDLLRs 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 106 ----LGRSPYtgfWGTLSKEdkavvdksialVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSK 181
Cdd:PRK13409 424 itddLGSSYY---KSEIIKP-----------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 182 VEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGV--TVGTPEDLS--LNGSLSNFfarkGIAF--DLETG 255
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKhgHASGPMDMRegMNRFLKEL----GITFrrDEETG 565
|
250
....*....|.
gi 2525300912 256 LFRVaNEYTSR 266
Cdd:PRK13409 566 RPRV-NKPGSY 575
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-219 |
2.94e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 24 VADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV-ISVVLTEKCDIRNMSVVE 102
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 103 --LIGLGRSPytgfwgtlskEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLdfpS 180
Cdd:PRK15439 106 niLFGLPKRQ----------ASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL---T 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2525300912 181 KVEMMQLLHQLS--RQTDKTIFLSTHDLELALQIADKIWLM 219
Cdd:PRK15439 173 PAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVM 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-221 |
4.04e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 4 ETIHIENLSIGYPGKG-DVKAVAdgicAGINSGELTCLLGANGVGKSTLLRTLSA-FQPKlGGNIFIEGKEIGEYTDKQL 81
Cdd:PRK10522 321 QTLELRNVTFAYQDNGfSVGPIN----LTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQ-SGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 82 SRVISVVLTEkcdirnmsvVELiglgrspytgFWGTLSKE----DKAVVDKSIALVGIPH----LAHRMVHT-LSDGERQ 152
Cdd:PRK10522 396 RKLFSAVFTD---------FHL----------FDQLLGPEgkpaNPALVEKWLERLKMAHklelEDGRISNLkLSKGQKK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 153 KVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDlELALQIADKIWLMDK 221
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRN 524
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-219 |
4.81e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 19 GDVKAVADGICAG---------INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVVL 89
Cdd:PRK11288 254 GEVRLRLDGLKGPglrepisfsVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 90 TE--KCD--IRNMSVVELIGLGRSPYTGFWGTL--SKEDKAVVDKSIALVGI--PHlAHRMVHTLSDGERQKVMIAKALA 161
Cdd:PRK11288 334 PEdrKAEgiIPVHSVADNINISARRHHLRAGCLinNRWEAENADRFIRSLNIktPS-REQLIMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 162 QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSThDLELALQIADKIWLM 219
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSS-DLPEVLGVADRIVVM 469
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-219 |
4.89e-11 |
|
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: 63.69 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 4 ETIHIENLSIGYPGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTL-SAFQPKLGGNIFIEGKEIGEYTDKQLS 82
Cdd:TIGR02633 256 VILEARNLTCWDVINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 RVISVVLTEkcDIRNMSVVELIGLGR----SPYTGFwGTLSKEDKAVVDKSIaLVGIPHLAHRMVH------TLSDGERQ 152
Cdd:TIGR02633 335 RAGIAMVPE--DRKRHGIVPILGVGKnitlSVLKSF-CFKMRIDAAAELQII-GSAIQRLKVKTASpflpigRLSGGNQQ 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 153 KVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSThDLELALQIADKIWLM 219
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSS-ELAEVLGLSDRVLVI 476
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-220 |
5.09e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.72 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV----ISVVLTEKCDIRNMSV---VELI 104
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIPTLNAlenVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 105 GLGRspytgfwGTLSKEDKavvDKSIALVGIPHLAHRMVH---TLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSK 181
Cdd:PRK10584 113 ALLR-------GESSRQSR---NGAKALLEQLGLGKRLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2525300912 182 VEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMD 220
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-217 |
6.66e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 4 ETIHIENLSIGYPgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFI-EGKEIgeytdkqls 82
Cdd:COG4178 361 GALALEDLTLRTP---DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV--------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 83 rvisVVLTEKcdirnmsvveliglgrsPYTGfWGTL----------SKEDKAVVDKSIALVGIPHLAHRM------VHTL 146
Cdd:COG4178 429 ----LFLPQR-----------------PYLP-LGTLreallypataEAFSDAELREALEAVGLGHLAERLdeeadwDQVL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 147 SDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQlsrQTDKTIFLST---------HDLELALQiADKIW 217
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELPGTTVISVghrstlaafHDRVLELT-GDGSW 562
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-230 |
7.32e-11 |
|
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: 60.89 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKcdirnmsvVELIGLGRSpytgfwgTLSKEDKAVVDKSIALVGIPHLAHrmvhTLSDGERQKVMIAKALAQETP 165
Cdd:cd03369 85 TIIPQDP--------TLFSGTIRS-------NLDPFDEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 166 VIYLDEPTAFLDFPSKVEMMQLLHQLSrqTDKTIFLSTHDLElalQIA--DKIWLMDKANGVTVGTP 230
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLR---TIIdyDKILVMDAGEVKEYDHP 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-233 |
9.92e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYPGKgdvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQlsRV 84
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLtekcdiRN------MSVVELIGLG---RspytgfwgtlsKEDKAVVDKSIA----LVGIPHLAHRMVHTLSDGER 151
Cdd:PRK11650 78 IAMVF------QNyalyphMSVRENMAYGlkiR-----------GMPKAEIEERVAeaarILELEPLLDRKPRELSGGQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 152 QKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHD-LElALQIADKIWLMDKANGVTVGTP 230
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqVE-AMTLADRVVVMNGGVAEQIGTP 219
|
...
gi 2525300912 231 EDL 233
Cdd:PRK11650 220 VEV 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-194 |
3.70e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISV--------VLTEKCDIRNMSVVEL 103
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDewqrnntdMLSPGEDDTGRTTAEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 104 IGLGrspytgfwgtlsKEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVE 183
Cdd:PRK10938 106 IQDE------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|.
gi 2525300912 184 MMQLLHQLSRQ 194
Cdd:PRK10938 174 LAELLASLHQS 184
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-204 |
3.77e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 4 ETIHIENLSIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSafQPKLGGniFIEGKEI---GEYTDKQ 80
Cdd:TIGR00956 758 DIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG--VITGGDRlvnGRPLDSS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISVVLTEKCDIRNMSVVEliGLGRSPYTGFWGTLSKEDK-AVVDKSIALVGIPHLAHRMVHTLSDG----ERQKVM 155
Cdd:TIGR00956 834 FQRSIGYVQQQDLHLPTSTVRE--SLRFSAYLRQPKSVSKSEKmEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLT 911
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525300912 156 IAKAL-AQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSrQTDKTIFLSTH 204
Cdd:TIGR00956 912 IGVELvAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-214 |
4.30e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.47 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAF-----QPKLGGNIFIEGKEIgeYTDK- 79
Cdd:PRK14267 5 IETVNLRVYY---GS-NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 80 ---QLSRVISVVLTEKCDIRNMSVVELIGLGRSpYTGFWGTLSKEDKAV---VDKSIALVGIPHLAHRMVHTLSDGERQK 153
Cdd:PRK14267 79 dpiEVRREVGMVFQYPNPFPHLTIYDNVAIGVK-LNGLVKSKKELDERVewaLKKAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 154 VMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLsrQTDKTIFLSTHDLELALQIAD 214
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSD 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-236 |
5.20e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 18 KGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV---ISVVLTEKCD 94
Cdd:PRK11831 17 RGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 95 IRNMSVVELIGLGRSPYTGFWGTLSkedKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTA 174
Cdd:PRK11831 96 FTDMNVFDNVAYPLREHTQLPAPLL---HSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 175 FLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDLSLN 236
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-204 |
8.06e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 22 KAVADGICAGINSGELTCLLGANGVGKSTLLRTLSA--FQPKLGGNIFIEGKEIGeytdKQLSRVISVVLTEKCDIRNMS 99
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPT----KQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 100 VVE---LIGLGRSPytgfwGTLSKEDKAVVDKS-IALVGIPH-----LAHRMVHTLSDGERQKVMIAKALAQETPVIYLD 170
Cdd:PLN03211 157 VREtlvFCSLLRLP-----KSLTKQEKILVAESvISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|....
gi 2525300912 171 EPTAFLDFPSKVEMMQLLHQLSrQTDKTIFLSTH 204
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMH 264
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-228 |
8.98e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLS---RVISVVLTE---KCDIRN------MSVVE 102
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDpyaSLDPRQtvgdsiMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 103 LIGLGRSpytgfwgtlsKEDKAVVDKSIALVGI-PHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSK 181
Cdd:PRK10261 430 VHGLLPG----------KAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525300912 182 VEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVG 228
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-219 |
1.16e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ-LSRVIsVVLTE--KCD--IRNMSVVELIGL 106
Cdd:PRK10762 275 LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGI-VYISEdrKRDglVLGMSVKENMSL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 107 GRSPY-TGFWGTLS-KEDKAVVDKSIALVGI--PHLAHRmVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKV 182
Cdd:PRK10762 354 TALRYfSRAGGSLKhADEQQAVSDFIRLFNIktPSMEQA-IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKK 432
|
170 180 190
....*....|....*....|....*....|....*..
gi 2525300912 183 EMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLM 219
Cdd:PRK10762 433 EIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-216 |
1.29e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 15 YPGkgdVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPK--LGGNIFIEGkEIGEYTDKQLS--RVISVVLT 90
Cdd:NF040905 11 FPG---VKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDG-EVCRFKDIRDSeaLGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 91 EKCDIRNMSVVELIGLGRSPYT-GF--WGTLSKEDKAVVDKsialVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVI 167
Cdd:NF040905 86 ELALIPYLSIAENIFLGNERAKrGVidWNETNRRARELLAK----VGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525300912 168 YLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLStHDLELALQIADKI 216
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIIS-HKLNEIRRVADSI 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
64-233 |
1.57e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 64 GNIFIEGKEIGEYTDKQLSRVISVVLTEKCdIRNMSVVELIGLGRSPYTgfwgtlsKEDK------AVVDKSIAlvGIPH 137
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPM-LFNMSIYENIKFGKEDAT-------REDVkrackfAAIDEFIE--SLPN 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 138 LAHRMV----HTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLElALQIA 213
Cdd:PTZ00265 1347 KYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRS 1425
|
170 180
....*....|....*....|....*
gi 2525300912 214 DKIWLMDKA--NGVTV---GTPEDL 233
Cdd:PTZ00265 1426 DKIVVFNNPdrTGSFVqahGTHEEL 1450
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-220 |
1.66e-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: 56.71 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDVKAVA-DGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKeigeytdkqlsrv 84
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKCdIRNMSVVELIgLGRSPYtgfwgtlskeDKAVVDKSI---ALV-----------------GIphlahrmvh 144
Cdd:cd03250 68 IAYVSQEPW-IQNGTIRENI-LFGKPF----------DEERYEKVIkacALEpdleilpdgdlteigekGI--------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 145 TLSDGERQKVMIAKALAQETPVIYLDEPTAFLDfpSKVEmMQLLHQLSR---QTDKTIFLSTHDLELALQiADKIWLMD 220
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVD--AHVG-RHIFENCILgllLNNKTRILVTHQLQLLPH-ADQIVVLD 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-216 |
2.02e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLSIGYpgKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQ 80
Cdd:PRK10247 1 MQENSPLLQLQNVGY--LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 LSRVISvvltekcdirnMSVVELIGLGRSPYTGF---WGTLSK--EDKAVVDkSIALVGIP-HLAHRMVHTLSDGERQKV 154
Cdd:PRK10247 79 YRQQVS-----------YCAQTPTLFGDTVYDNLifpWQIRNQqpDPAIFLD-DLERFALPdTILTKNIAELSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLElALQIADKI 216
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKV 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
32-221 |
6.00e-09 |
|
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: 55.35 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAfqpKLGGNIFIEG---------KEIGEYTDKQlsrvISVVLTEKCDIRNMSVVE 102
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGdihyngipyKEFAEKYPGE----IIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 103 LIglgrspytgfwgtlskedkavvDKSIALVGiphlaHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKV 182
Cdd:cd03233 103 TL----------------------DFALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2525300912 183 EMMQLLHQLSRQTDKTIFLSThdlelaLQIADKIW-LMDK 221
Cdd:cd03233 156 EILKCIRTMADVLKTTTFVSL------YQASDEIYdLFDK 189
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
35-228 |
6.20e-09 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 55.99 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSrvisvvlteKCDIRNMSVVELIGLGRSPYTGF 114
Cdd:TIGR02323 29 GEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLS---------EAERRRLMRTEWGFVHQNPRDGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 115 WGTLSKedKAVVDKSIALVGIPHL------AHRMVH--------------TLSDGERQKVMIAKALAQETPVIYLDEPTA 174
Cdd:TIGR02323 100 RMRVSA--GANIGERLMAIGARHYgniratAQDWLEeveidptriddlprAFSGGMQQRLQIARNLVTRPRLVFMDEPTG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 175 FLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGVTVG 228
Cdd:TIGR02323 178 GLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-228 |
6.75e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVVLTE---------KCDIRNMSVVELIg 105
Cdd:PRK10982 274 GEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEerrstgiyaYLDIGFNSLISNI- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 106 lgrSPYTGFWGTLS----KEDKAVVDKSIALVGIPHlaHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSK 181
Cdd:PRK10982 353 ---RNYKNKVGLLDnsrmKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAK 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525300912 182 VEMMQLLHQLSRQTDKTIFLSTHDLELaLQIADKIWLMdkANGVTVG 228
Cdd:PRK10982 428 FEIYQLIAELAKKDKGIIIISSEMPEL-LGITDRILVM--SNGLVAG 471
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-233 |
8.39e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.65 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGYpgkGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV 84
Cdd:PRK10790 340 RIDIDNVSFAY---RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 IS------VVLTEkcdirnmSVVELIGLGRSpytgfwgtLSKEdkaVVDKSIALVGIPHLAHRM---VHT--------LS 147
Cdd:PRK10790 417 VAmvqqdpVVLAD-------TFLANVTLGRD--------ISEE---QVWQALETVQLAELARSLpdgLYTplgeqgnnLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 148 DGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTdkTIFLSTHDLELALQiADKIWLMDKANGVTV 227
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
....*.
gi 2525300912 228 GTPEDL 233
Cdd:PRK10790 556 GTHQQL 561
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-221 |
1.17e-08 |
|
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: 54.85 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 12 SIGYPGKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIfiegkeigeytdkqlsrvisvvlte 91
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 92 kcdIRNMSVVELIGLGrspyTGFWGTLS----------------KEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVM 155
Cdd:cd03220 80 ---TVRGRVSSLLGLG----GGFNPELTgreniylngrllglsrKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 156 IAKALAQEtPVIYL-DEPTAFLD--FPSKveMMQLLHQLsRQTDKTIFLSTHDLELALQIADKIWLMDK 221
Cdd:cd03220 153 FAIATALE-PDILLiDEVLAVGDaaFQEK--CQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
146-250 |
1.22e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.73 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLMDKANGV 225
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
90 100
....*....|....*....|....*.
gi 2525300912 226 -TVGTPEDLSLNGsLSNFFARKGIAF 250
Cdd:cd03222 152 yGIASQPKGTREG-INRFLRGYLITF 176
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-232 |
2.59e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYpgkgDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTL-SAFQPKLGGNIFIEGKEIGEY---------T 77
Cdd:PRK15064 322 VENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLvGELEPDSGTVKWSENANIGYYaqdhaydfeN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 78 DKQLSRVISVVLTEKCD---IRNMsvveligLGRSPYTGfwgtlskEDkavVDKSialvgiphlahrmVHTLSDGERQKV 154
Cdd:PRK15064 398 DLTLFDWMSQWRQEGDDeqaVRGT-------LGRLLFSQ-------DD---IKKS-------------VKVLSGGEKGRM 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDFPSkVEMMQLLHQLSRQTdkTIFLStHDLELALQIADKIWLMdKANGVT--VGTPED 232
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMES-IESLNMALEKYEGT--LIFVS-HDREFVSSLATRIIEI-TPDGVVdfSGTYEE 522
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-177 |
7.23e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLSAfqPKLGGniFIEGK-EIGEYTDKQ--LSRVISvvLTEKCDIRNMSVVELIGLGRSPY 111
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDiRISGFPKKQetFARISG--YCEQNDIHSPQVTVRESLIYSAF 979
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 112 TGFWGTLSKEDKAV-VDKSIALVGIPHLAHRMVHT-----LSDGERQKVMIAKALAQETPVIYLDEPTAFLD 177
Cdd:PLN03140 980 LRLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-232 |
1.13e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.01 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYP-------------------GKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLS-AFQPKLGgn 65
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWAL-KDVSFEVERGESVGIIGRNGAGKSTLLKLIAgILEPTSG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 66 ifiegkeigeytdkqlsRVisvvltekcdIRNMSVVELIGLGrspyTGFWGTLS----------------KEDKAVVDKS 129
Cdd:COG1134 82 -----------------RV----------EVNGRVSALLELG----AGFHPELTgreniylngrllglsrKEIDEKFDEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 130 IALVGIPHLAHRMVHTLSDGERQKVMIAKALAQEtPVIYL-DEPTAFLD--FPSKVemMQLLHQLSRQTdKTIFLSTHDL 206
Cdd:COG1134 131 VEFAELGDFIDQPVKTYSSGMRARLAFAVATAVD-PDILLvDEVLAVGDaaFQKKC--LARIRELRESG-RTVIFVSHSM 206
|
250 260
....*....|....*....|....*.
gi 2525300912 207 ELALQIADKIWLMDKANGVTVGTPED 232
Cdd:COG1134 207 GAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
40-191 |
3.80e-07 |
|
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: 49.46 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 40 LLGANGVGKSTLLRTLSAFQPKLGGNIfiegkeigeytdkqlsrvisvVLTEKCDIrnmsvvelIGLGRSPYTGFwGTLs 119
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRI---------------------GMPEGEDL--------LFLPQRPYLPL-GTL- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 120 kedkavvdKSIalvgiphLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQL 191
Cdd:cd03223 81 --------REQ-------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-219 |
4.15e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 3 KETIHIENLSIGYPGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTL-SAFQPKLGGNIFIEGKEIGEYTDKQL 81
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPHIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 82 SRVISVVLTE--KCD--IRNMSVVELIGLGRSPYTGFWGTLSKEDK-AVVDKSIALVGI----PHLAhrmVHTLSDGERQ 152
Cdd:PRK13549 336 IAQGIAMVPEdrKRDgiVPVMGVGKNITLAALDRFTGGSRIDDAAElKTILESIQRLKVktasPELA---IARLSGGNQQ 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525300912 153 KVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSThdlELA--LQIADKIWLM 219
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISS---ELPevLGLSDRVLVM 478
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-218 |
4.77e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 26 DGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV--------ISVVLT--Ekcdi 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpgIKTELTalE---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 96 rNMSvveliglgrspytgFWGTLSKE-DKAVVDKSIALVGiphLAHRM---VHTLSDGERQKVMIAKALAQETPVIYLDE 171
Cdd:PRK13538 94 -NLR--------------FYQRLHGPgDDEALWEALAQVG---LAGFEdvpVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 172 P-TAfLDfpsKVEMMQLLHQLSRQTDK--TIFLSTH-DLELALQIADKIWL 218
Cdd:PRK13538 156 PfTA-ID---KQGVARLEALLAQHAEQggMVILTTHqDLPVASDKVRKLRL 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-243 |
5.04e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 5 TIHIENLSIGY-PGkgdVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSR 83
Cdd:PLN03232 1234 SIKFEDVHLRYrPG---LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 VISVVltekcdirNMSVVELIGLGR---SPYT-----GFWGTLSKED-KAVVDKSIalVGIPHLAHRMVHTLSDGERQKV 154
Cdd:PLN03232 1311 VLSII--------PQSPVLFSGTVRfniDPFSehndaDLWEALERAHiKDVIDRNP--FGLDAEVSEGGENFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 155 MIAKALAQETPVIYLDEPTAFLDfpskVEMMQLLHQLSRQTDK--TIFLSTHDLELALQiADKIWLMDKANGVTVGTPED 232
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVD----VRTDSLIQRTIREEFKscTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
250
....*....|.
gi 2525300912 233 LsLNGSLSNFF 243
Cdd:PLN03232 1456 L-LSRDTSAFF 1465
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-211 |
9.50e-07 |
|
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: 50.68 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKGdvKAVADGICAGINSGELTCLLGANGVGKSTLLrtlSAFQPKLG--GNIFIEGKEIGEYTDKQLSRVI 85
Cdd:TIGR01271 1220 VQGLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLL---SALLRLLSteGEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVlTEKCDI------RNMS------------VVELIGLgRSPYTGFWGTLskeDKAVVDKSialvgiphlahrmvHTLS 147
Cdd:TIGR01271 1295 GVI-PQKVFIfsgtfrKNLDpyeqwsdeeiwkVAEEVGL-KSVIEQFPDKL---DFVLVDGG--------------YVLS 1355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525300912 148 DGERQKVMIAKALAQETPVIYLDEPTAFLDfPSkveMMQLLHQLSRQT--DKTIFLSTHDLELALQ 211
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLD-PV---TLQIIRKTLKQSfsNCTVILSEHRVEALLE 1417
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
35-219 |
1.13e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 35 GELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEiGEYTD---------KQLSRV-ISVVLTEKCDIRNMSVV--- 101
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDlyalseaerRRLLRTeWGFVHQHPRDGLRMQVSagg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 102 ----ELIGLGRSPY------TGFWgtLSKedkavvdksialVGIPhlAHRM---VHTLSDGERQKVMIAKALAQETPVIY 168
Cdd:PRK11701 111 nigeRLMAVGARHYgdiratAGDW--LER------------VEID--AARIddlPTTFSGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 169 LDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELALQIADKIWLM 219
Cdd:PRK11701 175 MDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-236 |
1.33e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 24 VADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVISVVLTEKcdirnmsvVEL 103
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP--------VLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 104 IGLGRSPYTGFWGTLSKEdkavVDKSIALVGI-PHLA-------HRMVH---TLSDGERQKVMIAKALAQE-TPVIYLDE 171
Cdd:PTZ00243 1397 DGTVRQNVDPFLEASSAE----VWAALELVGLrERVAsesegidSRVLEggsNYSVGQRQLMCMARALLKKgSGFILMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525300912 172 PTAFLDfpskvemmqllHQLSRQTDKTIFLS---------THDLELALQIaDKIWLMDKANGVTVGTPEDLSLN 236
Cdd:PTZ00243 1473 ATANID-----------PALDRQIQATVMSAfsaytvitiAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-177 |
2.66e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 32 INSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEG---------------------------KEIGEYTdKQLSRV 84
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdpprnvegtvydfvaegiEEQAEYL-KRYHDI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 ISVVLTEKCDiRNMSvvELIGL-GRSPYTGFWGTLSKedkavVDKSIALVGIPhlAHRMVHTLSDGERQKVMIAKALAQE 163
Cdd:PRK11147 105 SHLVETDPSE-KNLN--ELAKLqEQLDHHNLWQLENR-----INEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 2525300912 164 TPVIYLDEPTAFLD 177
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
118-233 |
2.77e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 118 LSKED-KAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtD 196
Cdd:NF000106 116 LSRKDaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-G 194
|
90 100 110
....*....|....*....|....*....|....*..
gi 2525300912 197 KTIFLSTHDLELALQIADKIWLMDKANGVTVGTPEDL 233
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-218 |
5.80e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 34 SGELTCLLGANGVGKSTLLRTLSAF-QPKLGGNIFIEGKEIGEYTDKQLSRVISvvltekcdirnmsvveliglgrspyt 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 113 gfwgtlskedkavvdksialvgiphlaHRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQL----- 187
Cdd:smart00382 55 ---------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190
....*....|....*....|....*....|.
gi 2525300912 188 LHQLSRQTDKTIFLSTHDLELALQIADKIWL 218
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-231 |
8.71e-06 |
|
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: 45.98 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIgypgKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFqPK---LGGNIFIEGKeigeytdkqlsrv 84
Cdd:cd03217 3 IKDLHV----SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKyevTEGEILFKGE------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 85 isvvltekcDIRNMSVVELIGLG-----RSPYTgfwgtlskedkavvdksIALVGIPHLAHRMVHTLSDGERQKVMIAKA 159
Cdd:cd03217 65 ---------DITDLPPEERARLGiflafQYPPE-----------------IPGVKNADFLRYVNEGFSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 160 LAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTHDLELALQI-ADKIWLMDKANGVTVGTPE 231
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-211 |
1.09e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.39 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYPGKGDvkAVADGICAGINSGELTCLLGANGVGKSTLlrtLSAFQPKLG--GNIFIEGKEIGEYTDKQLSR 83
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLLNteGDIQIDGVSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 84 VISVVlTEKCDIRNMSvvelIGLGRSPYtgfwGTLSKEDKAVVDKSIALVGI-----PHLAHRMV---HTLSDGERQKVM 155
Cdd:cd03289 78 AFGVI-PQKVFIFSGT----FRKNLDPY----GKWSDEEIWKVAEEVGLKSVieqfpGQLDFVLVdggCVLSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLD-FPSKVEMMQLLHQLSrqtDKTIFLSTHDLELALQ 211
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDpITYQVIRKTLKQAFA---DCTVILSEHRIEAMLE 202
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-204 |
2.20e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 1 MNKETIHIENLsigYPGKGDVKaVADGICAGINSGELTCLLGANGVGKSTLLRTLsAFQPK---LGGNIFIEGKEIGEYT 77
Cdd:CHL00131 3 KNKPILEIKNL---HASVNENE-ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-AGHPAykiLEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 78 DKQLSRvISVVLT-----EKCDIRNMSVVELIGLGRSPYTGfwgtLSKEDK----AVVDKSIALVGI-PHLAHRMVHT-L 146
Cdd:CHL00131 78 PEERAH-LGIFLAfqypiEIPGVSNADFLRLAYNSKRKFQG----LPELDPleflEIINEKLKLVGMdPSFLSRNVNEgF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525300912 147 SDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtDKTIFLSTH 204
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-252 |
4.08e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 133 VGIPHLA-HRMVHTLSDGERQKVMIAKALAQE-TPVIY-LDEPTAFLDFPSKVEMMQLLHQLSRQTDkTIFLSTHDlELA 209
Cdd:PRK00635 463 LGLPYLTpERALATLSGGEQERTALAKHLGAElIGITYiLDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQM 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2525300912 210 LQIADKIwlMDKANGVTV--------GTPED-LSLNGSLSNFFARKGIAFDL 252
Cdd:PRK00635 541 ISLADRI--IDIGPGAGIfggevlfnGSPREfLAKSDSLTAKYLRQELTIPI 590
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-205 |
5.76e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIGYPGKGDVKavadGICAGINSGELTCLLGANGVGKSTLLR-TLSAFQPKlGGNIFIEGK-EIGeYTDKQlsRVI 85
Cdd:PRK11147 322 MENVNYQIDGKQLVK----DFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQAD-SGRIHCGTKlEVA-YFDQH--RAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 svVLTEKcdirnmSVVELIGLGrspytgfwgtlsKEDKAVVDKSIALVGI-------PHLAHRMVHTLSDGERQKVMIAK 158
Cdd:PRK11147 394 --LDPEK------TVMDNLAEG------------KQEVMVNGRPRHVLGYlqdflfhPKRAMTPVKALSGGERNRLLLAR 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525300912 159 ALAQETPVIYLDEPTAFLDfpskVEMMQLLHQLSRQTDKTIFLSTHD 205
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-188 |
7.16e-05 |
|
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: 44.54 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgkGDvKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIfiegkEIGE-----YTDKq 80
Cdd:TIGR03719 323 IEAENLTKAF---GD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-----EIGEtvklaYVDQ- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 81 lSRvisvvltEKCDiRNMSVVELIGLGrspytgfwgtlskEDKAVVDKsialVGIPHLAH------------RMVHTLSD 148
Cdd:TIGR03719 393 -SR-------DALD-PNKTVWEEISGG-------------LDIIKLGK----REIPSRAYvgrfnfkgsdqqKKVGQLSG 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2525300912 149 GERQKVMIAKALAQETPVIYLDEPTAFLDfpskVEMMQLL 188
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRAL 482
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-216 |
7.88e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 8 IENLSIgyPGKGDVKAVaDGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRV-IS 86
Cdd:COG3845 260 VENLSV--RDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 87 VV----LTEKCdIRNMSVVELIGLGR---SPYTGfWGTLSKedKAVVDKSIALV---GI-PHLAHRMVHTLSDGERQKVM 155
Cdd:COG3845 337 YIpedrLGRGL-VPDMSVAENLILGRyrrPPFSR-GGFLDR--KAIRAFAEELIeefDVrTPGPDTPARSLSGGNQQKVI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 156 IAKALAQETPVIYLDEPTAFLDFPSkVEMM--QLLHQlsRQTDKTIFLSTHDLELALQIADKI 216
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGA-IEFIhqRLLEL--RDAGAAVLLISEDLDEILALSDRI 472
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-234 |
1.15e-04 |
|
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: 43.85 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 145 TLSDGERQKVMIAKAL-AQET-PVIY-LDEPTAFLDFPSKVEMMQLLHQLSRQTDkTIFLSTHDLELaLQIADkiWLMD- 220
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELsKRSTgRTLYiLDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDV-IKTAD--YIIDl 904
|
90 100
....*....|....*....|.
gi 2525300912 221 ----KANG---VTVGTPEDLS 234
Cdd:TIGR00630 905 gpegGDGGgtvVASGTPEEVA 925
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
145-229 |
1.23e-04 |
|
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: 42.31 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 145 TLSDGERQKVMIAKALAQETP--VIYLDEPTAFLDFPSKvemMQLLHQLSRQTDK--TIFLSTHDLELaLQIADKIWLMD 220
Cdd:cd03238 87 TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI---NQLLEVIKGLIDLgnTVILIEHNLDV-LSSADWIIDFG 162
|
....*....
gi 2525300912 221 KANGVTVGT 229
Cdd:cd03238 163 PGSGKSGGK 171
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-221 |
1.44e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 141 RMVHTLSDGERQKVMIAKALA------QETPVIYLDEPTAFLDfPSKVE--MMQLLHQLSRQTDKTIFLSTHDLELaLQI 212
Cdd:cd03240 111 DMRGRCSGGEKVLASLIIRLAlaetfgSNCGILALDEPTTNLD-EENIEesLAEIIEERKSQKNFQLIVITHDEEL-VDA 188
|
....*....
gi 2525300912 213 ADKIWLMDK 221
Cdd:cd03240 189 ADHIYRVEK 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-233 |
1.73e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 43.40 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 6 IHIENLSIGYpgKGDVKAVADGICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLSRVI 85
Cdd:TIGR00957 1285 VEFRNYCLRY--REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 86 SVVLTEKCDIRNMSVVELIGLGRSPYTGFWGTLSKED-KAVVDKSIAlvGIPHLAHRMVHTLSDGERQKVMIAKALAQET 164
Cdd:TIGR00957 1363 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHlKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525300912 165 PVIYLDEPTAFLDfpskVEMMQLLHQLSRQT--DKTIFLSTHDLELALQIAdKIWLMDKANGVTVGTPEDL 233
Cdd:TIGR00957 1441 KILVLDEATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
149-233 |
2.16e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 149 GERQKVMIAKALAQETPVIYLDEPTAFLDfPSKVEMM-QLLHQLSRQTDKTIFLSTHDLELALQiADKIWLMDKANGVTV 227
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD-PVARDMFwRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLAS 478
|
....*.
gi 2525300912 228 GTPEDL 233
Cdd:NF033858 479 DTPAAL 484
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
142-224 |
2.91e-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: 40.81 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 142 MVHTLSDGERQKVMIAKALA----QETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLsTHDLELALqIADKIW 217
Cdd:cd03227 74 TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVI-THLPELAE-LADKLI 151
|
....*..
gi 2525300912 218 LMDKANG 224
Cdd:cd03227 152 HIKKVIT 158
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
146-234 |
3.47e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 146 LSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQtdKTIFLSTHDLElALQIADKIWLMDKANGV 225
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
....*....
gi 2525300912 226 TVGTPEDLS 234
Cdd:PRK10789 529 QRGNHDQLA 537
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-90 |
3.60e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 42.09 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 4 ETIHIENLSIGYPGKGDVKAVADG-ICAGINSGELTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEYTDKQLS 82
Cdd:COG4615 326 QTLELRGVTYRYPGEDGDEGFTLGpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR 405
|
....*...
gi 2525300912 83 RVISVVLT 90
Cdd:COG4615 406 QLFSAVFS 413
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
143-219 |
9.54e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 9.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525300912 143 VHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSRQTDKTIFLSTHDLELaLQIADKIWLM 219
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPEL-LGMCDRIYVM 477
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
143-205 |
1.39e-03 |
|
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: 40.30 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525300912 143 VHTLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQLLHQLSrqtdKTIFLSTHD 205
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP----GTVVAVTHD 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
42-188 |
1.92e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 42 GANGVGKSTLLRTLSAFQPKLGGNIfiegkEIGE-----YTDKqlSR-----------VISVVLtekcdirnmsvvELIG 105
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTI-----KIGEtvklaYVDQ--SRdaldpnktvweEISGGL------------DIIK 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 106 LG------RSpYTG---FWGTlskedkavvDKSialvgiphlahRMVHTLSDGERQKVMIAKALAQETPVIYLDEPTAFL 176
Cdd:PRK11819 418 VGnreipsRA-YVGrfnFKGG---------DQQ-----------KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170
....*....|..
gi 2525300912 177 DfpskVEMMQLL 188
Cdd:PRK11819 477 D----VETLRAL 484
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
35-55 |
2.88e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.14 E-value: 2.88e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-233 |
3.40e-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: 39.23 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 133 VGIPHLA-HRMVHTLSDGERQKVMIAKAL-AQETPVIY-LDEPTAFLDFPSKVEMMQLLHQLsRQTDKTIFLSTHDlELA 209
Cdd:TIGR00630 475 VGLDYLSlSRAAGTLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDT 552
|
90 100 110
....*....|....*....|....*....|..
gi 2525300912 210 LQIADkiWLMDKANG--------VTVGTPEDL 233
Cdd:TIGR00630 553 IRAAD--YVIDIGPGagehggevVASGTPEEI 582
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
145-233 |
6.02e-03 |
|
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: 38.74 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 145 TLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQ-LLHQLsrQTDKTIFLSTHDLElALQIADKIWLMDKAN 223
Cdd:TIGR01271 548 TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEsCLCKL--MSNKTRILVTSKLE-HLKKADKILLLHEGV 624
|
90
....*....|
gi 2525300912 224 GVTVGTPEDL 233
Cdd:TIGR01271 625 CYFYGTFSEL 634
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-171 |
6.24e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.16 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 37 LTCLLGANGVGKSTLLRTLSAFQPKLGGNIFIEGKEIGEyTDKQLSRVISVVLTEKCDirnMSVVELIglgrspytGFWG 116
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-IAKPYCTYIGHNLGLKLE---MTVFENL--------KFWS 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2525300912 117 TLSkEDKAVVDKSIALVGIPHLAHRMVHTLSDGERQKVMIAKALAQETPVIYLDE 171
Cdd:PRK13541 96 EIY-NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
145-251 |
8.55e-03 |
|
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: 37.53 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525300912 145 TLSDGERQKVMIAKALAQETPVIYLDEPTAFLDFPSKVEMMQ-LLHQLsrQTDKTIFLSTHDLElALQIADKIWLMDKAN 223
Cdd:cd03291 159 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKL--MANKTRILVTSKME-HLKKADKILILHEGS 235
|
90 100
....*....|....*....|....*...
gi 2525300912 224 GVTVGTPEDLSlngSLSNFFARKGIAFD 251
Cdd:cd03291 236 SYFYGTFSELQ---SLRPDFSSKLMGYD 260
|
|
| |
