|
Name |
Accession |
Description |
Interval |
E-value |
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-341 |
1.18e-180 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 505.41 E-value: 1.18e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 1 MARVIIDHVSVVFGNRRKQALDLADQGASRAEIKDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPV 80
Cdd:COG4175 1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 81 EGNIYVGNagkeINVTTASSDELRYVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEW 160
Cdd:COG4175 81 AGEVLIDG----EDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 161 ANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:COG4175 157 EDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 241 MEDGRILQCGTAQEIVLTPANEHVANFVRHINPLSFLTARQVMRP---YNFQNGDISVA--------------------- 296
Cdd:COG4175 237 MKDGRIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPpeaVVSEKDGPRVAlrrmreegisslyvvdrdrrl 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 297 ---------------------------AMAKPDTSLPDLISVCDRKNGAIGV-AEDGRVIGVITEEDIIHHLA 341
Cdd:COG4175 317 lgvvtaddaleavkgekdleeilltdvPTVSPDTPLRDLLPLVAESPYPLAVvDEDGRLLGVISRGSLLAALA 389
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
4-343 |
2.97e-173 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 486.21 E-value: 2.97e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRKQALDLADQGASRAEIKDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:TIGR03415 1 IRFKNVDIVFGDQPDEALALLDQGKTREEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IYVGNAGKEINVTTASSDELRYVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANR 163
Cdd:TIGR03415 81 VLVKDGDGSVDVANCDAATLRRLRTHRVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMED 243
Cdd:TIGR03415 161 KPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 244 GRILQCGTAQEIVLTPANEHVANFVRHINPLSFLTARQVMRPYNF---------------------------QNGDISVA 296
Cdd:TIGR03415 241 GRIIQHGTPEEIVLNPANDYVADFVAHTNPLNVLTARDLMRPLTTlekvdgewcvskrydtwlktadkqvrrAAAGLPVA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 297 AMA---------------KPDTSLPDLISVCDRKNGAIGVAEDGRVIGVITEEDIIHHLAEH 343
Cdd:TIGR03415 321 AWAaeqevesleklptviNPDTPMRDVLAARHRTGGAILLVENGRIVGVIGDQNIYHALLGH 382
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-274 |
4.02e-131 |
|
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: 375.06 E-value: 4.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 6 IDHVSVVFGNRRKQALDLADQGASRAEIKDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIY 85
Cdd:cd03294 3 IKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 86 VGNAgkeiNVTTASSDELRYVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMV 165
Cdd:cd03294 83 IDGQ----DIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 166 TELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
250 260
....*....|....*....|....*....
gi 1946638175 246 ILQCGTAQEIVLTPANEHVANFVRHINPL 274
Cdd:cd03294 239 LVQVGTPEEILTNPANDYVREFFRGVDRA 267
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
43-341 |
2.02e-109 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 321.27 E-value: 2.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKeiNVTTASSDELR----YVrtrlvsmvFQQF 118
Cdd:COG1125 18 VDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILID--GE--DIRDLDPVELRrrigYV--------IQQI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 GLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLN--EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:COG1125 86 GLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 197 ALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV---RHINP 273
Cdd:COG1125 166 ALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVgadRGLRR 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 274 LSFLTARQVMRPynfqngdisVAAMAKPDTSLPDLISVCDRKN--GAIGVAEDGRVIGVITEEDIIHHLA 341
Cdd:COG1125 246 LSLLRVEDLMLP---------EPPTVSPDASLREALSLMLERGvdWLLVVDEDGRPLGWLTLEDLLRALA 306
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
37-321 |
2.78e-97 |
|
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: 292.53 E-value: 2.78e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 37 TNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRYVRTRLVSMVFQ 116
Cdd:TIGR01186 3 TGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDG----ENIMKQSPVELREVRRKKIGMVFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 QFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:TIGR01186 79 QFALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 197 ALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVRHINPLSF 276
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 277 LTARQVMRPYNfqNGDISVAAMAKPDTSLP-------DLISVCDRKNGAIGV 321
Cdd:TIGR01186 239 FDAERIAQRMN--TGPITKTADKGPRSALQlmrdervDSLYVVDRQNKLVGV 288
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
32-280 |
2.69e-89 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 271.59 E-value: 2.69e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTAssdELRYVrt 108
Cdd:COG3842 7 ELENVSkryGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD--GRDVTGLPP---EKRNV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 rlvSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:COG3842 80 ---GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
250
....*....|..
gi 1946638175 269 RHINplsFLTAR 280
Cdd:COG3842 237 GEAN---LLPGT 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
43-268 |
9.71e-88 |
|
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: 263.78 E-value: 9.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASsdELRyvrtRLVSMVFQQFGLFP 122
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID--GEDIREQDPV--ELR----RKIGYVIQQIGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGL--NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:cd03295 89 HMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 201 LIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:cd03295 169 ITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-246 |
1.54e-87 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 263.87 E-value: 1.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 1 MARVIIDHVSVVFGNRRKqaldladqgasraeikdlTNTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPV 80
Cdd:COG1116 5 APALELRGVSKRFPTGGG------------------GVTAL--DDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 81 EGNIYVGnaGKEinVTTASSDelryvrtrlVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEW 160
Cdd:COG1116 65 SGEVLVD--GKP--VTGPGPD---------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 161 ANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:COG1116 132 EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
....*...
gi 1946638175 241 MED--GRI 246
Cdd:COG1116 212 LSArpGRI 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
32-250 |
1.67e-83 |
|
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: 252.06 E-value: 1.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGVH---ECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTassdelRYVRT 108
Cdd:cd03259 2 ELKGLSKTYGSVRaldDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR----DVTG------VPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-268 |
4.48e-83 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 255.77 E-value: 4.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 1 MARVIIDHVSVVFGNrrkqaldladqgasraeikdltntVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPV 80
Cdd:COG3839 1 MASLELENVSKSYGG------------------------VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 81 EGNIYVGnaGKEINvttassdELRyVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEW 160
Cdd:COG3839 57 SGEILIG--GRDVT-------DLP-PKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 161 ANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:COG3839 127 LDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAV 206
|
250 260
....*....|....*....|....*...
gi 1946638175 241 MEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:COG3839 207 MNDGRIQQVGTPEELYDRPANLFVAGFI 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-248 |
1.99e-82 |
|
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: 249.31 E-value: 1.99e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRkqaldladqgasraeikdltNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:cd03293 1 LEVRNVSKTYGGGG--------------------GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IYVGNAGkeinVTTASSDelryvrtrlVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANR 163
Cdd:cd03293 61 VLVDGEP----VTGPGPD---------RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIME- 242
Cdd:cd03293 128 YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSa 207
|
....*..
gi 1946638175 243 -DGRILQ 248
Cdd:cd03293 208 rPGRIVA 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-344 |
5.64e-81 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 252.26 E-value: 5.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 12 VFGNRRKQALDLADQGASRAEIKDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagk 91
Cdd:PRK10070 13 IFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 92 eINVTTASSDELRYVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGG 171
Cdd:PRK10070 90 -VDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 172 MQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGT 251
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 252 AQEIVLTPANEHVANFVRHINPLSFLTARQVMRpyNFQNGDISVAAMAKPDTSLpDLISVCDRKNGAIgVAEDGRVIGVI 331
Cdd:PRK10070 249 PDEILNNPANDYVRTFFRGVDISQVFSAKDIAR--RTPNGLIRKTPGFGPRSAL-KLLQDEDREYGYV-IERGNKFVGAV 324
|
330
....*....|...
gi 1946638175 332 TEEDIIHHLAEHQ 344
Cdd:PRK10070 325 SIDSLKTALTQQQ 337
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
47-268 |
2.58e-75 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 235.81 E-value: 2.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTAssdelryVRTRLVSMVFQQFGLFPWRTV 126
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN--GRDLFTNLP-------PRERRVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:COG1118 93 AENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 207 QDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:COG1118 173 RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
41-268 |
2.22e-73 |
|
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: 226.73 E-value: 2.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 41 LGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASSdelryvrtRLVSMVFQQFGL 120
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--GKDITNLPPHK--------RPVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 121 FPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:cd03300 84 FPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 201 LIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:cd03300 164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
32-268 |
6.77e-71 |
|
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: 220.62 E-value: 6.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVL-GVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDELRY 105
Cdd:COG1127 7 EVRNLTksfgdRVVLdGV---SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD--GQDI--TGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 106 VRTRlVSMVFQQFGLFPWRTVADNIGFGL-EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFAT 184
Cdd:COG1127 80 LRRR-IGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 185 GAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPaNEHV 264
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWV 237
|
....
gi 1946638175 265 ANFV 268
Cdd:COG1127 238 RQFL 241
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
47-276 |
1.95e-69 |
|
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: 220.68 E-value: 1.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvtTASSDELR-YvrtrlvSMVFQQFGLFPWRT 125
Cdd:TIGR03265 24 SLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQG--GRDI---TRLPPQKRdY------GIVFQSYALFPNLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNH 205
Cdd:TIGR03265 93 VADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREH 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 206 LQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVRHINPLSF 276
Cdd:TIGR03265 173 LRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPG 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-255 |
7.54e-67 |
|
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: 218.62 E-value: 7.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT--------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDEL 103
Cdd:COG1123 262 EVRNLSkrypvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD--GKDL--TKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 104 RYVRTRlVSMVFQQ-FG-LFPWRTVADNIGFGLEVAGV-PKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGLA 179
Cdd:COG1123 338 RELRRR-VQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 180 RAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-260 |
1.64e-65 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 207.79 E-value: 1.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 1 MARVIIDHVSVVFGNRRKQALDLADqgasraeikdltntvlgvheCSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPV 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQD--------------------VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 81 EGNIYVGnaGKEinVTTASSDelRYVrtrlvsmVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEW 160
Cdd:COG4525 61 SGEITLD--GVP--VTGPGAD--RGV-------VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 161 ANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:COG4525 128 ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVV 207
|
250 260 270
....*....|....*....|....*....|....
gi 1946638175 241 MED--GRI------------LQCGTAQEIVLTPA 260
Cdd:COG4525 208 MSPgpGRIverleldfsrrfLAGEDARAIKSDPA 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
47-272 |
2.32e-65 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 210.96 E-value: 2.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTAssdELRYVRTrlvsmVFQQFGLFPWRTV 126
Cdd:PRK09452 34 DLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML--DGQDITHVPA---ENRHVNT-----VFQSYALFPHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:PRK09452 104 FENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 207 QDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVRHIN 272
Cdd:PRK09452 184 QNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEIN 249
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
32-271 |
3.82e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 206.00 E-value: 3.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvtTASSDELRYV 106
Cdd:COG1126 3 EIENLHksfgdLEVL--KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD--GEDL---TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRlVSMVFQQFGLFPWRTVADNIGFGL-EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATG 185
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 186 APVLLMDEPFSALDP-LIRnhlqdELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPAN 261
Cdd:COG1126 155 PKVMLFDEPTSALDPeLVG-----EVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
250
....*....|
gi 1946638175 262 EHVANFVRHI 271
Cdd:COG1126 230 ERTRAFLSKV 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
32-267 |
4.72e-65 |
|
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: 205.43 E-value: 4.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDELRYV 106
Cdd:cd03261 2 ELRGLTksfggRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID--GEDI--SGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRlVSMVFQQFGLFPWRTVADNIGFGL-EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATG 185
Cdd:cd03261 76 RRR-MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 186 APVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIvLTPANEHVA 265
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVR 233
|
..
gi 1946638175 266 NF 267
Cdd:cd03261 234 QF 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
32-271 |
9.53e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 208.39 E-value: 9.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDELR 104
Cdd:COG1135 3 ELENLSktfptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD--GVDL--TALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 YVRTRlVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFAT 184
Cdd:COG1135 79 AARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 185 GAPVLLMDEPFSALDPlirnhlQ--DELLELQKRLNK----TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLT 258
Cdd:COG1135 158 NPKVLLCDEATSALDP------EttRSILDLLKDINRelglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
250
....*....|...
gi 1946638175 259 PANEHVANFVRHI 271
Cdd:COG1135 232 PQSELTRRFLPTV 244
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
32-255 |
2.77e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 198.36 E-value: 2.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvtTASSDELRyvrt 108
Cdd:COG1131 2 EVRGLTkryGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV--LGEDV---ARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-250 |
6.45e-62 |
|
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: 196.71 E-value: 6.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnagkEINVTTASSDElryvrtRLVSMVFQQFGLFP 122
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG----GRDVTDLPPKD------RDIAMVFQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:cd03301 86 HMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1946638175 203 RNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03301 166 RVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
32-245 |
8.55e-62 |
|
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: 195.10 E-value: 8.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASSDELRyvrt 108
Cdd:cd03229 2 ELKNVSkryGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID--GEDLTDLEDELPPLR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNIGFGLevagvpkkqrqaiiaeqldlvglnewanrmvtelSGGMQQRIGLARAFATGAPV 188
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
58-278 |
8.96e-62 |
|
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: 200.41 E-value: 8.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 58 LMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvtTASSDELRYVrtrlvSMVFQQFGLFPWRTVADNIGFGLEVA 137
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD--GEDV---TNVPPHLRHI-----NMVFQSYALFPHMTVEENVAFGLKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 138 GVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRL 217
Cdd:TIGR01187 71 KVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 218 NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVRHINPLSFLT 278
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATV 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
43-268 |
4.88e-61 |
|
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: 195.64 E-value: 4.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEinvttASSdelRYVRTRLVSMVFQQFGLFP 122
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG--GED-----ATD---VPVQERNVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEV----AGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL 198
Cdd:cd03296 88 HMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 199 DPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-259 |
1.55e-60 |
|
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: 193.95 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRKQALDLADqgasraeikdltntvlgvheCSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKD--------------------VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IYVgnAGKEInvTTASSDELRYVRTRlVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANR 163
Cdd:cd03258 62 VLV--DGTDL--TLLSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMED 243
Cdd:cd03258 137 YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK 216
|
250
....*....|....*.
gi 1946638175 244 GRILQCGTAQEIVLTP 259
Cdd:cd03258 217 GEVVEEGTVEEVFANP 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
32-246 |
3.14e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 192.95 E-value: 3.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELR 104
Cdd:COG1136 6 ELRNLTksygtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG----QDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 YVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFAT 184
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 185 GAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGRI 246
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
32-255 |
5.32e-60 |
|
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: 192.55 E-value: 5.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT----NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINvttasSDELRYVR 107
Cdd:COG1122 2 ELENLSfsypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD--GKDIT-----KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 tRLVSMVFQ----QFgLFPwrTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFA 183
Cdd:COG1122 75 -RKVGLVFQnpddQL-FAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 184 TGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
32-250 |
1.10e-59 |
|
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: 191.57 E-value: 1.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvtTASSDELR 104
Cdd:cd03257 3 EVKNLSvsfptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF--DGKDL---LKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 YVRTRLVSMVFQ--QFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLN---EWANRMVTELSGGMQQRIGLA 179
Cdd:cd03257 78 KIRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 180 RAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
32-246 |
1.40e-58 |
|
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: 188.47 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELR 104
Cdd:cd03255 2 ELKNLSktyggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG----TDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 YVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFAT 184
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 185 GAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAiKMGNRIAIMEDGRI 246
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
32-246 |
1.09e-57 |
|
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: 185.81 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASSDELRyv 106
Cdd:cd03262 2 EIKNLHksfgdFHVL--KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID--GLKLTDDKKNINELR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 rtRLVSMVFQQFGLFPWRTVADNIGFGL-EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATG 185
Cdd:cd03262 76 --QKVGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 186 APVLLMDEPFSALDPlirnHLQDELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03262 154 PKVMLFDEPTSALDP----ELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-267 |
3.69e-57 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 189.16 E-value: 3.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLGvhECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASsdelryV 106
Cdd:PRK11432 8 VLKNITkrfgsNTVID--NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE----DVTHRS------I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGA 186
Cdd:PRK11432 76 QQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 187 PVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVAN 266
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMAS 235
|
.
gi 1946638175 267 F 267
Cdd:PRK11432 236 F 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
47-268 |
5.21e-57 |
|
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: 184.85 E-value: 5.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDElryvrtRLVSMVFQQFGLFPWRTV 126
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN--GKDI--TNLPPEK------RDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 207 QDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
47-267 |
1.16e-55 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 181.49 E-value: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDElryvrtRLVSMVFQQFGLFPWRTV 126
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ----DLTALPPAE------RPVSMLFQENNLFPHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEvagvPK-----KQRQAI--IAEQldlVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:COG3840 89 AQNIGLGLR----PGlkltaEQRAQVeqALER---VGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 200 PLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANF 267
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
44-275 |
2.50e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 181.82 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGniYVGNAGKEINVTTAssdelryvRTRLVSMVFQQFGLFPW 123
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG--HIRFHGTDVSRLHA--------RDRKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 RTVADNIGFGLEVagVPKKQR--QAIIAEQ----LDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:PRK10851 89 MTVFDNIAFGLTV--LPRRERpnAAAIKAKvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 198 LDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVRHINPLS 275
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQ 244
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
44-245 |
2.77e-54 |
|
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: 176.89 E-value: 2.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagKEINVTTASSDELRyvrtRLVSMVFQ----QFg 119
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----DGKDLTKLSLKELR----RKVGLVFQnpddQF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPwrTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:cd03225 89 FGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1946638175 200 PLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:cd03225 167 PAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
37-269 |
4.13e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.77 E-value: 4.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 37 TNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRYVRtRLVSMVFQ 116
Cdd:PRK11153 15 GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG----QDLTALSEKELRKAR-RQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 QFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:PRK11153 90 HFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 197 ALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVR 269
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
32-261 |
5.31e-54 |
|
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: 177.93 E-value: 5.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDELRyv 106
Cdd:COG1120 3 EAENLSvgyggRPVL--DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD--GRDL--ASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 rtRLVSMVFQQ----FGLfpwrTVADNIGFG----LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGL 178
Cdd:COG1120 75 --RRIAYVPQEppapFGL----TVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 179 ARAFATGAPVLLMDEPFSALDPlirNHlQDELLELQKRLN----KTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQE 254
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDL---AH-QLEVLELLRRLArergRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
....*..
gi 1946638175 255 iVLTPAN 261
Cdd:COG1120 225 -VLTPEL 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
45-250 |
3.21e-53 |
|
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: 174.41 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 45 ECSLDIaEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVG-----NAGKEINVTTassdelryvRTRLVSMVFQQFG 119
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfDSRKKINLPP---------QQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADNIGFGLEVAGvPKKQRQAIiAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:cd03297 86 LFPHLNVRENLAFGLKRKR-NREDRISV-DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 200 PLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-260 |
5.62e-53 |
|
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: 182.41 E-value: 5.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKP---VEGNIYVGNagkeINVTTASSDel 103
Cdd:COG1123 6 EVRDLSvrypgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDG----RDLLELSEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 104 ryVRTRLVSMVFQQFG--LFPWrTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARA 181
Cdd:COG1123 80 --LRGRRIGMVFQDPMtqLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 182 FATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPA 260
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-263 |
6.08e-53 |
|
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: 174.99 E-value: 6.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFG--NRRKQALdladqgasraeikdltntvlgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVE 81
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVL----------------------KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 82 GNIYVGnaGKEinVTTASSDELRyvrtRLVSMVFQQ-FG-LFPWRTVADNIGFGLEVAGVPkkQRQAIIAEQLDLVGLN- 158
Cdd:COG1124 60 GEVTFD--GRP--VTRRRRKAFR----RRVQMVFQDpYAsLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPp 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 159 EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRI 238
Cdd:COG1124 130 SFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRV 209
|
250 260
....*....|....*....|....*
gi 1946638175 239 AIMEDGRILQCGTAQEIVLTPANEH 263
Cdd:COG1124 210 AVMQNGRIVEELTVADLLAGPKHPY 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
37-271 |
1.29e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 173.74 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 37 TNTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDElRYVRtRLVSMVFQ 116
Cdd:PRK09493 13 PTQVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG----LKVNDPKVDE-RLIR-QEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 QFGLFPWRTVADNIGFG-LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:PRK09493 85 QFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 196 SALDPLIRNhlqdELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVRHI 271
Cdd:PRK09493 165 SALDPELRH----EVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-260 |
1.35e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.09 E-value: 1.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 6 IDHVSVVFGNRRKqALDladqgasraeikdltntvlGVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIY 85
Cdd:COG3638 5 LRNLSKRYPGGTP-ALD-------------------DV---SLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEIL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 86 VGNagkeINVTTASSDELRYVRTRlVSMVFQQFGLFPWRTVADNI-------------GFGLevagVPKKQRQAIIaEQL 152
Cdd:COG3638 62 VDG----QDVTALRGRALRRLRRR-IGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsLLGL----FPPEDRERAL-EAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 153 DLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAI 232
Cdd:COG3638 132 ERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLAR 211
|
250 260
....*....|....*....|....*...
gi 1946638175 233 KMGNRIAIMEDGRILQCGTAQEivLTPA 260
Cdd:COG3638 212 RYADRIIGLRDGRVVFDGPPAE--LTDA 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
38-246 |
1.63e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 172.93 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 38 NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRYVRtRLVSMVFQQ 117
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG----QDLSRLKRREIPYLR-RRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:COG2884 88 FRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 198 LDPlirnHLQDELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:COG2884 168 LDP----ETSWEIMELLEEINRrgtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
47-260 |
4.63e-51 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 172.61 E-value: 4.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDELRYVRtRLVSMVFQQ-FG-LFPWR 124
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF--DGQDI--TGLSGRELRPLR-RRMQMVFQDpYAsLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAGV-PKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:COG4608 113 TVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 203 R----NHLQDelleLQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPA 260
Cdd:COG4608 193 QaqvlNLLED----LQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
32-260 |
9.89e-51 |
|
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: 171.39 E-value: 9.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKP---VEGNIYVGnaGKEInvTTASSD 101
Cdd:COG0444 3 EVRNLKvyfptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFD--GEDL--LKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 102 ELRYVRTRLVSMVFQQ-FG-LFPWRTVADNIGFGLEV-AGVPKKQRQAIIAEQLDLVGLNEWANRMVT---ELSGGMQQR 175
Cdd:COG0444 79 ELRKIRGREIQMIFQDpMTsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 176 IGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 1946638175 256 VLTPA 260
Cdd:COG0444 239 FENPR 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
32-272 |
1.15e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 172.71 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGVH---ECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvttasSDELRYVRT 108
Cdd:PRK11607 21 EIRNLTKSFDGQHavdDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--GVDL------SHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 rlVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:PRK11607 93 --INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
....
gi 1946638175 269 RHIN 272
Cdd:PRK11607 251 GSVN 254
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
43-255 |
1.39e-50 |
|
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: 168.13 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIK-----PVEGNIYVGnaGKEINVTTASSDELRyvrtRLVSMVFQQ 117
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLD--GKDIYDLDVDVLELR----RRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLFPwRTVADNIGFGLEVAGV-PKKQRQAIIAEQLDLVGLNEWANR--MVTELSGGMQQRIGLARAFATGAPVLLMDEP 194
Cdd:cd03260 90 PNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 195 FSALDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-255 |
1.59e-49 |
|
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: 165.82 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 6 IDHVSVVFGNRrKQALdladqgasraeikdltntvlgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIY 85
Cdd:cd03256 3 VENLSKTYPNG-KKAL----------------------KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 86 VgnagKEINVTTASSDELRYVRTRlVSMVFQQFGLFPWRTVADNIGFGL--------EVAGVPKKQRQAIIAEQLDLVGL 157
Cdd:cd03256 60 I----DGTDINKLKGKALRQLRRQ-IGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 158 NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNR 237
Cdd:cd03256 135 LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADR 214
|
250
....*....|....*...
gi 1946638175 238 IAIMEDGRILQCGTAQEI 255
Cdd:cd03256 215 IVGLKDGRIVFDGPPAEL 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
47-255 |
3.85e-49 |
|
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: 164.56 E-value: 3.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDelryvrtRLVsmVFQQFGLFPWRTV 126
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL--EGKQI--TEPGPD-------RMV--VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLE--VAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRN 204
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 205 HLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
32-255 |
1.77e-48 |
|
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: 163.10 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNT---VLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINvttasSDELRyvrt 108
Cdd:COG4555 3 EVENLSKKygkVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-----PREAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELqKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
47-248 |
3.67e-48 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 162.95 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDElryvrtrlvSMVFQQFGLFPWRTV 126
Cdd:PRK11248 21 NLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGPGAER---------GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1946638175 207 QDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIME--DGRILQ 248
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-255 |
2.48e-47 |
|
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: 159.59 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRKQALDladqgasraeikDLtntvlgvhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVD------------DL----------SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IYVGnaGKEINvttassDELRYVRtRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANR 163
Cdd:cd03263 59 AYIN--GYSIR------TDRKAAR-QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLDEAIKMGNRIAIMED 243
Cdd:cd03263 130 RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSD 207
|
250
....*....|..
gi 1946638175 244 GRILQCGTAQEI 255
Cdd:cd03263 208 GKLRCIGSPQEL 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
44-270 |
1.53e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 158.25 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTT-ASSDELRYVRtRLVSMVFQQFGLFP 122
Cdd:COG4161 19 FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNI--AGHQFDFSQkPSEKAIRLLR-QKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADN-IGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:COG4161 96 HLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 202 IRNHLQDELLELQKrLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAqEIVLTPANEHVANFVRH 270
Cdd:COG4161 176 ITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAHYLSH 242
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
32-268 |
1.61e-46 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 158.23 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNA---GKEINVTTASSDEL 103
Cdd:TIGR00972 3 EIENLNlfygeKEAL--KNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVlfdGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 104 RyvrtRLVSMVFQQFGLFPwRTVADNIGFGLEVAGV-PKKQRQAIIAEQLDLVGL-NEWANRM---VTELSGGMQQRIGL 178
Cdd:TIGR00972 81 R----RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwDEVKDRLhdsALGLSGGQQQRLCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 179 ARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLT 258
Cdd:TIGR00972 156 ARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTN 233
|
250
....*....|
gi 1946638175 259 PANEHVANFV 268
Cdd:TIGR00972 234 PKEKRTEDYI 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
44-270 |
2.71e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.48 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTASSD-ELRYVRtRLVSMVFQQFGLFP 122
Cdd:PRK11124 19 FDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI--AGNHFDFSKTPSDkAIRELR-RNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADN-IGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK11124 96 HLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 202 IRNHLQDELLELQKrLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVlTPANEHVANFVRH 270
Cdd:PRK11124 176 ITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFT-QPQTEAFKNYLSH 242
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
32-246 |
9.55e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.97 E-value: 9.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLG---VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrt 108
Cdd:COG4619 2 ELEGLSFRVGGkpiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG----KPLSAMPPPEWR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPwRTVADNIGFGLEVAGvpKKQRQAIIAEQLDLVGLNEWA-NRMVTELSGGMQQRIGLARAFATGAP 187
Cdd:COG4619 74 RQVAYVPQEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 188 VLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-255 |
1.72e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 156.05 E-value: 1.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnagkeiNVTTASSDELRYV 106
Cdd:TIGR04520 2 EVENVSfsypeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD------GLDTLDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RtRLVSMVFQ----QF-GlfpwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARA 181
Cdd:TIGR04520 76 R-KKVGMVFQnpdnQFvG----ATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 182 FATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIkMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREI 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
48-268 |
1.91e-45 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 159.04 E-value: 1.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 48 LDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagKEINVTTASSdelryvrtRLVSMVFQQFGLFPWRTVA 127
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE--KRMNDVPPAE--------RGVGMVFQSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 128 DNIGFGLEVAGVPK---KQRQAIIAEQLDLVGLNEwanRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRN 204
Cdd:PRK11000 94 ENMSFGLKLAGAKKeeiNQRVNQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 205 HLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
32-271 |
3.44e-45 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 154.76 E-value: 3.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT----NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDELRYVR 107
Cdd:TIGR02315 3 EVENLSkvypNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILL--EGTDI--TKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 TRlVSMVFQQFGLFPWRTVADNI--------GFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLA 179
Cdd:TIGR02315 79 RR-IGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 180 RAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIvltp 259
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL---- 233
|
250
....*....|..
gi 1946638175 260 aNEHVanfVRHI 271
Cdd:TIGR02315 234 -DDEV---LRHI 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-268 |
3.55e-45 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 155.19 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 24 ADQGASRAEIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIK--P---VEGNIYVGnaGKEINV 95
Cdd:COG1117 5 ASTLEPKIEVRNLNvyyGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLD--GEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 96 TTASSDELRyvrtRLVSMVFQQFGLFPWrTVADNIGFGLEVAGVPKKQRQAIIAEQ-LDLVGL-NEWANRM---VTELSG 170
Cdd:COG1117 83 PDVDVVELR----RRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEEsLRKAALwDEVKDRLkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 171 GMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
250
....*....|....*...
gi 1946638175 251 TAQEIVLTPANEHVANFV 268
Cdd:COG1117 236 PTEQIFTNPKDKRTEDYI 253
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-268 |
8.74e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 156.93 E-value: 8.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLG----VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDElryvr 107
Cdd:PRK11650 5 KLQAVRKSYDGktqvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR----VVNELEPAD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 tRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAP 187
Cdd:PRK11650 76 -RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 188 VLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANF 267
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
|
.
gi 1946638175 268 V 268
Cdd:PRK11650 235 I 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
32-246 |
6.17e-44 |
|
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: 149.08 E-value: 6.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINvttassDELRYVRt 108
Cdd:cd03230 2 EVRNLSkryGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--LGKDIK------KEPEEVK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNIgfglevagvpkkqrqaiiaeqldlvglnewanrmvtELSGGMQQRIGLARAFATGAPV 188
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
32-261 |
3.56e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 3.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvtTASSDELRYV 106
Cdd:COG1121 8 ELENLTvsyggRPVL--EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL--FGKPP---RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 rtrlvsmvfQQFGLFPWR---TVADNIGFGL----EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLA 179
Cdd:COG1121 81 ---------PQRAEVDWDfpiTVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 180 RAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMeDGRILQCGTAQEiVLTP 259
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEE-VLTP 228
|
..
gi 1946638175 260 AN 261
Cdd:COG1121 229 EN 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-245 |
1.76e-42 |
|
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: 145.22 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRKQALdladqgasraeiKDLtntvlgvhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVL------------KDV----------SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFPwRTVADNIgfglevagvpkkqrqaiiaeqldlvglnewanr 163
Cdd:cd03228 59 ILIDG----VDLRDLDLESLR----KNIAYVPQDPFLFS-GTIRENI--------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 mvteLSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMED 243
Cdd:cd03228 97 ----LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDD 169
|
..
gi 1946638175 244 GR 245
Cdd:cd03228 170 GR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
47-196 |
2.91e-42 |
|
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: 143.94 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINvttasSDELRYVRTRlVSMVFQQFGLFPWRTV 126
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD--GQDLT-----DDERKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMV----TELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
47-254 |
7.28e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 145.50 E-value: 7.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTASSdelryvrtRLVSMVFQQFGLFPWRTV 126
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL--NGQDHTTTPPSR--------RPVSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFG----LEVAGVPKKQRQAIiAEQldlVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:PRK10771 89 AQNIGLGlnpgLKLNAAQREKLHAI-ARQ---MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 203 RNhlqdELLEL------QKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRI--------LQCGTAQE 254
Cdd:PRK10771 165 RQ----EMLTLvsqvcqERQL--TLLMVSHSLEDAARIAPRSLVVADGRIawdgptdeLLSGKASA 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
32-250 |
8.87e-42 |
|
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: 143.73 E-value: 8.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTAssdelryv 106
Cdd:cd03214 1 EVENLSvgyggRTVL--DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD--GKDLASLSP-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 rtrlvsmvfqqfglfpwRTVADNIGFglevagVPkkqrQAiiaeqLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGA 186
Cdd:cd03214 69 -----------------KELARKIAY------VP----QA-----LELLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 187 PVLLMDEPFSALDPlirNHlQDELLELQKRL----NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03214 117 PILLLDEPTSHLDI---AH-QIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
47-255 |
1.01e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 146.44 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRYVRTRlVSMVFQ----QfgLFP 122
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDG----RDITAKKKKKLKDLRKK-VGLVFQfpehQ--LFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNE-WANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:TIGR04521 98 -ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 202 IRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
43-262 |
1.27e-41 |
|
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: 152.15 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIkPVEGNIYVgnAGKEInvTTASSDELRYVRTRLvSMVFQQ-FG-L 120
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRF--DGQDL--DGLSRRALRPLRRRM-QVVFQDpFGsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 121 FPWRTVADNIGFGLEV--AGVPKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:COG4172 376 SPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 198 LDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANE 262
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
29-269 |
1.65e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 145.28 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 29 SRAEIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkEINVTTASSDEL 103
Cdd:PRK11264 2 SAIEVKNLVkkfhgQTVL--HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDI--TIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 104 RYVRT--RLVSMVFQQFGLFPWRTVADNIGFG-LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLAR 180
Cdd:PRK11264 78 GLIRQlrQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 181 AFATGAPVLLMDEPFSALDPlirnHLQDELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVL 257
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDP----ELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
250
....*....|..
gi 1946638175 258 TPANEHVANFVR 269
Cdd:PRK11264 234 DPQQPRTRQFLE 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
45-255 |
1.71e-41 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 148.33 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 45 ECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVG-----NAGKEINVTTassdelryvRTRLVSMVFQQFG 119
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSARGIFLPP---------HRRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADNIGFGLEVAgvPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:COG4148 88 LFPHLSVRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 200 PLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
47-250 |
2.97e-41 |
|
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: 143.40 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnagkEINVTTASSDElryvrtRLVSMVFQQFGLFPWRTV 126
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN----GVDVTAAPPAD------RPVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:cd03298 88 EQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1946638175 207 QDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
47-256 |
2.75e-40 |
|
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: 150.37 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFPwRTV 126
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG----IDLRQIDPASLR----RQIGVVLQDVFLFS-GTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEvaGVPKKQrqaiIAEQLDLVGLNEWANRM-------VTE----LSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:COG2274 566 RENITLGDP--DATDEE----IIEAARLAGLHDFIEALpmgydtvVGEggsnLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 196 SALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:COG2274 640 SALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
47-256 |
3.28e-40 |
|
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: 148.76 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFPwRTV 126
Cdd:COG4987 355 SLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG----VDLRDLDEDDLR----RRIAVVPQRPHLFD-TTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGvpkkqrQAIIAEQLDLVGLNEWANR-------MVTE----LSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:COG4987 426 RENLRLARPDAT------DEELWAALERVGLGDWLAAlpdgldtWLGEggrrLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 196 SALDPLIRNHLQDELLELQKrlNKTLIFVSHDLDEAIKMgNRIAIMEDGRILQCGTAQEIV 256
Cdd:COG4987 500 EGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELL 557
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-270 |
9.35e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 141.09 E-value: 9.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDL-----TNTVL-GVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTT-------- 97
Cdd:COG4598 10 EVRDLhksfgDLEVLkGV---SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVG--GEEIRLKPdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 98 ASSDELRYVRTRLvSMVFQQFGLFPWRTVADNIGFG-LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRI 176
Cdd:COG4598 85 ADRRQLQRIRTRL-GMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 177 GLARAFATGAPVLLMDEPFSALDPlirnHLQDELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQ 253
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|....*..
gi 1946638175 254 EIVLTPANEHVANFVRH 270
Cdd:COG4598 240 EVFGNPKSERLRQFLSS 256
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
40-245 |
1.70e-39 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 138.92 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 40 VLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDELRYVRtRLVSMVFQQFG 119
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGE----DVNRLRGRQLPLLR-RRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:TIGR02673 90 LLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1946638175 200 PlirnHLQDELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:TIGR02673 170 P----DLSERILDLLKRLNKrgtTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
43-254 |
1.76e-39 |
|
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: 146.44 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING----VDLSDLDPASWR----RQIAWVPQNPYLFA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WrTVADNIGFGLEVAGvpkkqrQAIIAEQLDLVGLNEWANR-------MVTE----LSGGMQQRIGLARAFATGAPVLLM 191
Cdd:COG4988 425 G-TIRENLRLGRPDAS------DEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 192 DEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQE 254
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
43-254 |
2.26e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.46 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG----VDIRDLTLESLR----RQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGFGLEVAGvpkkqRQAIIaEQLDLVGLNEWANRM-------VTE----LSGGMQQRIGLARAFATGAPVLLM 191
Cdd:COG1132 428 -GTIRENIRYGRPDAT-----DEEVE-EAAKAAQAHEFIEALpdgydtvVGErgvnLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 192 DEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQE 254
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
43-255 |
2.44e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.54 E-value: 2.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASsdELRyvrtRLVSMVFQ----QF 118
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG--GMVLSEETVW--DVR----RQVGMVFQnpdnQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 -GlfpwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:PRK13635 95 vG----ATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 198 LDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKmGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-255 |
4.69e-39 |
|
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: 137.89 E-value: 4.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvttasSDELRYVRt 108
Cdd:cd03265 2 EVENLVkkyGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDV------VREPREVR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
39-254 |
7.75e-39 |
|
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: 137.57 E-value: 7.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 39 TVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDELRYVRTRLVSMVFQQF 118
Cdd:COG4181 26 TIL--KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL--AGQDL--FALDEDARARLRARHVGFVFQSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 GLFPWRTVADNIGFGLEVAGVPKKQRQAiiAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL 198
Cdd:COG4181 100 QLLPTLTALENVMLPLELAGRRDARARA--RALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 199 DPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAiKMGNRIAIMEDGRILQCGTAQE 254
Cdd:COG4181 178 DAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
47-271 |
3.45e-38 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 136.50 E-value: 3.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGN------AGKEINVTTASSDELRYVRTRlVSMVFQQFGL 120
Cdd:TIGR03005 20 NFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGeqlyhmPGRNGPLVPADEKHLRQMRNK-IGMVFQSFNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 121 FPWRTVADNIGFG-LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:TIGR03005 99 FPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 200 PlirnHLQDELLELQKRL----NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFVRHI 271
Cdd:TIGR03005 179 P----ELVGEVLNVIRRLasehDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSKV 250
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
44-238 |
3.76e-38 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 135.05 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYV-GNAGKEINvttaSSDELRYVRTRLvSMVFQQFGLFP 122
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLnGQETPPLN----SKKASKFRREKL-GYLFQNFALIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:TIGR03608 90 NETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKN 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1946638175 203 RNHLQDELLELQKRlNKTLIFVSHDLdEAIKMGNRI 238
Cdd:TIGR03608 170 RDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-246 |
4.11e-38 |
|
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: 135.23 E-value: 4.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 34 KDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTASSdeLRYVRtRLVSM 113
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV--NGQDVSDLRGRA--IPYLR-RKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 114 VFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDE 193
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 194 PFSALDPLIRNhlqdELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03292 163 PTGNLDPDTTW----EIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
32-245 |
4.55e-38 |
|
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: 133.14 E-value: 4.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrt 108
Cdd:cd00267 1 EIENLSfryGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG----KDIAKLPLEELR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQqfglfpwrtvadnigfglevagvpkkqrqaiiaeqldlvglnewanrmvteLSGGMQQRIGLARAFATGAPV 188
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-260 |
6.16e-38 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 138.71 E-value: 6.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 34 KDLTNTVLGVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVG-----NAGKEINVTTassdelryvRT 108
Cdd:TIGR02142 7 KRLGDFSLDA---DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfDSRKGIFLPP---------EK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPkkQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:TIGR02142 75 RRIGYVFQEARLFPHLSVRGNLRYGMKRARPS--ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPA 260
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
32-268 |
7.65e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 135.67 E-value: 7.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINR---LIKPVEGNIYVGNAGKEINVTTASSDELRy 105
Cdd:PRK14239 7 QVSDLSvyyNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPEVTITGSIVYNGHNIYSPRTDTVDLR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 106 vrtRLVSMVFQQFGLFPWrTVADNIGFGLEVAGVPKKQRQAIIAEQlDLVGLNEW---ANRM---VTELSGGMQQRIGLA 179
Cdd:PRK14239 86 ---KEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWdevKDRLhdsALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 180 RAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
....*....
gi 1946638175 260 ANEHVANFV 268
Cdd:PRK14239 239 KHKETEDYI 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
32-246 |
1.84e-37 |
|
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: 133.56 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTN---TVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGkeinVTTASSDELRYVRt 108
Cdd:cd03269 2 EVENVTKrfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP----LDIAARNRIGYLP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 rlvsmvfQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:cd03269 77 -------EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELqKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
47-264 |
1.97e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.86 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINvtTASSDELryVRTRLVsmVFQQFGL-FPWrT 125
Cdd:COG4559 21 SLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLN--GRPLA--AWSPWEL--ARRRAV--LPQHSSLaFPF-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFA-------TGAPVLLMDEPFSAL 198
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 199 DPlirnHLQDELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEiVLTPAN-EHV 264
Cdd:COG4559 172 DL----AHQHAVLRLARQLARrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE-VLTDELlERV 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-241 |
3.81e-37 |
|
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: 132.66 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvtTASSDELRYV 106
Cdd:cd03235 1 EVEDLTvsyggHPVL--EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV--FGKPL---EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 rtrlvsmvfQQFGLFPWR---TVADNIGFGL----EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLA 179
Cdd:cd03235 74 ---------PQRRSIDRDfpiSVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 180 RAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQkRLNKTLIFVSHDLDEAIKMGNRIAIM 241
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
47-256 |
9.50e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.19 E-value: 9.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINvttasSDELRYVRTRlVSMVFQ----QF-GLf 121
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI--DGITIS-----KENLKEIRKK-IGIIFQnpdnQFiGA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 pwrTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK13632 100 ---TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 202 IRNHLQDELLELQKRLNKTLIFVSHDLDEAIKmGNRIAIMEDGRILQCGTAQEIV 256
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
42-269 |
3.61e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.63 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 42 GVHEC----SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNA------GKEINVTTASSDELRYVRTRLv 111
Cdd:PRK10619 16 GEHEVlkgvSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrDKDGQLKVADKNQLRLLRTRL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 112 SMVFQQFGLFPWRTVADNIGFG-LEVAGVPKKQRQAIIAEQLDLVGLNEWAN-RMVTELSGGMQQRIGLARAFATGAPVL 189
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 190 LMDEPFSALDPlirnHLQDELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVAN 266
Cdd:PRK10619 175 LFDEPTSALDP----ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
...
gi 1946638175 267 FVR 269
Cdd:PRK10619 251 FLK 253
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
43-262 |
4.93e-36 |
|
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: 130.18 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKP----VEGNIYVgnAGKEINvttassdELRYvRTRLVSMVFQQ- 117
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILL--DGRPLL-------PLSI-RGRHIATIMQNp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLF-PWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVT---ELSGGMQQRIGLARAFATGAPVLLMDE 193
Cdd:TIGR02770 72 RTAFnPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKypfQLSGGMLQRVMIALALLLEPPFLIADE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 194 PFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANE 262
Cdd:TIGR02770 152 PTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
47-261 |
1.78e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.51 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDELryVRTRlvSMVFQQFGL-FPWrT 125
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR----PLADWSPAEL--ARRR--AVLPQHSSLsFPF-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFA------TGAPVLLMDEPFSALD 199
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 200 PLirnHlQDELLELQKRL----NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEiVLTPAN 261
Cdd:PRK13548 173 LA---H-QHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE-VLTPET 233
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
47-255 |
2.73e-35 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 130.20 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvtTASSDELRyvrtRLVSMVFQQFGLFPWRTV 126
Cdd:TIGR01188 13 NFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARV--AGYDV---VREPRKVR----RSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1946638175 207 QDELLELqKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR01188 164 WDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-260 |
2.98e-35 |
|
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: 134.43 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKP----VEGNIYVgnAGKEInvTTASS 100
Cdd:COG4172 8 SVEDLSvafgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILF--DGQDL--LGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 101 DELRYVRTRLVSMVFQQ--FGLFPWRTVADNIGFGLEV-AGVPKKQRQAIIAEQLDLVGLNEWANRMVT---ELSGGMQQ 174
Cdd:COG4172 84 RELRRIRGNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 175 RIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQE 254
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
....*.
gi 1946638175 255 IVLTPA 260
Cdd:COG4172 244 LFAAPQ 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
47-255 |
3.58e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.78 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSdELRYVRTRlVSMVFQ--QFGLFPwR 124
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG----VDITDKKV-KLSDIRKK-VGLVFQypEYQLFE-E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGL--NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 203 RNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
41-260 |
3.71e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 129.75 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 41 LGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeiNVTTASSDE--LRYVRTRlVSMVFQqf 118
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE-----RVITAGKKNkkLKPLRKK-VGIVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 glFPW-----RTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNE-WANRMVTELSGGMQQRIGLARAFATGAPVLLMD 192
Cdd:PRK13634 93 --FPEhqlfeETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 193 EPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPA 260
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
38-246 |
4.99e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 128.64 E-value: 4.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 38 NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDelryvrTRlvsMVFQQ 117
Cdd:PRK11247 25 RTVL--NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA----PLAEARED------TR---LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLFPWRTVADNIGFGLEVAGVPKKqRQAiiaeqLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQWRDAA-LQA-----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1946638175 198 LDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-255 |
1.30e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.30 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTAssdelryvrt 108
Cdd:COG4152 3 ELKGLTkrfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD--GEPLDPEDR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 rlvsmvfQQFG-------LFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARA 181
Cdd:COG4152 71 -------RRIGylpeergLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 182 FAtGAPVLL-MDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG4152 144 LL-HDPELLiLDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
43-240 |
2.53e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 125.29 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKP---VEGNIYVGnaGKEInvttassDELRyVRTRLVSMVFQQFG 119
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLN--GRRL-------TALP-AEQRRIGILFQDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADNIGFGLeVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:COG4136 87 LFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1946638175 200 PLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
38-250 |
3.65e-34 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 126.08 E-value: 3.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 38 NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNI-YVGNAGKEINVTTASSDELRYVRTRLVSMVFQ 116
Cdd:COG4107 23 GTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVyYRDRDGGPRDLFALSEAERRRLRRTDWGMVYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 Q--FGLFPWRTVADNIGFGLEVAGVpkKQRQAIIAEQLDLVGLNEW-ANRMV---TELSGGMQQRIGLARAFATGAPVLL 190
Cdd:COG4107 103 NprDGLRMDVSAGGNIAERLMAAGE--RHYGDIRARALEWLERVEIpLERIDdlpRTFSGGMQQRVQIARALVTNPRLLF 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 191 MDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:COG4107 181 LDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESG 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
47-231 |
4.50e-34 |
|
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: 124.51 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEInvttaSSDELRyvrtRLVSMVFQQFGLFPWRTV 126
Cdd:COG4133 22 SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-----AREDYR----RRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQaiIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP------ 200
Cdd:COG4133 93 RENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAagvall 170
|
170 180 190
....*....|....*....|....*....|...
gi 1946638175 201 --LIRNHLQDellelqkrlNKTLIFVSHDLDEA 231
Cdd:COG4133 171 aeLIAAHLAR---------GGAVLLTTHQPLEL 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
43-260 |
6.00e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 125.51 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDELryvrTRLVSMVFQQFgLFP 122
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG--DKPI--SMLSSRQL----ARRLALLPQHH-LTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WR-TVADNIGFG----LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:PRK11231 89 EGiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 198 LDpliRNHlQDELLELQKRLN---KTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEiVLTPA 260
Cdd:PRK11231 169 LD---INH-QVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE-VMTPG 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
40-256 |
1.02e-33 |
|
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: 130.31 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 40 VLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINVTTASSDElRYVRTRLVSMVFQQFG 119
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDG-RGRAKRYIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADNI--GFGLEVagvPKK--QRQAIIAeqLDLVGLNEWA-----NRMVTELSGGMQQRIGLARAFATGAPVLL 190
Cdd:TIGR03269 376 LYPHRTVLDNLteAIGLEL---PDElaRMKAVIT--LKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 191 MDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
43-264 |
1.14e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 124.77 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDElryvRTRL-VSMVFQQFGLF 121
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF--DGRDI--TGLPPHR----IARLgIARTFQNPRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVADNI----------GFGLEVAGVPKKQRQ-----AIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGA 186
Cdd:COG0411 92 PELTVLENVlvaaharlgrGLLAALLRLPRARREerearERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 187 PVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpANEHV 264
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR---ADPRV 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-268 |
1.74e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 124.39 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNA----GKEINVTTASsdELRyvrtRLVSMVFQQFGLFP 122
Cdd:PRK14246 30 TIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfGKDIFQIDAI--KLR----KEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQR-QAIIAEQLDLVGL----NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREiKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 198 LDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
47-255 |
2.05e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.98 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTASSDElryvrtRL-VSMVFQQFGLFPWRT 125
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL--DGEPVRFRSPRDAQ------AAgIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAG---VPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:COG1129 96 VAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTERE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 203 RNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG1129 176 VERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
45-305 |
2.56e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 124.85 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 45 ECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeINVTTASSDELRYVRTRlVSMVFQ--QFGLFP 122
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDI---VVSSTSKQKEIKPVRKK-VGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK13643 100 -ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 202 IRNHLQdELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTA----QEIVLTPANEHVANFVRHinplsFL 277
Cdd:PRK13643 179 ARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPsdvfQEVDFLKAHELGVPKATH-----FA 252
|
250 260
....*....|....*....|....*...
gi 1946638175 278 TARQVMRPYNFQNGDISVAAMAKPDTSL 305
Cdd:PRK13643 253 DQLQKTGAVTFEKLPITRAELVTLLTSL 280
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
47-255 |
9.33e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.95 E-value: 9.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDELRYVRTRLvSMVFQQFGLFPWRTV 126
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE----NIPAMSRSRLYTVRKRM-SMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGL-EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNH 205
Cdd:PRK11831 102 FDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1946638175 206 LQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
47-255 |
1.24e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.53 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYV-GNAGKEINVTtassdELRyvrtRLVSMVFQQ-FGLFPWR 124
Cdd:PRK13650 27 SFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVW-----DIR----HKIGMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRN 204
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 205 HLQDELLELQKRLNKTLIFVSHDLDEaIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
47-264 |
2.00e-32 |
|
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: 121.00 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDElryvRTRL-VSMVFQQFGLFPWRT 125
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD--GEDI--TGLPPHE----IARLgIGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNI--------GFGLEVAGVPKKQRQAI--IAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:cd03219 92 VLENVmvaaqartGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 196 SALDPLIRNHLQDELLELqKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpANEHV 264
Cdd:cd03219 172 AGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR---NNPRV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
43-255 |
4.70e-32 |
|
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: 119.46 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDElryvRTRL-VSMVFQQFGLF 121
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD--GRDI--TGLPPHE----RARAgIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVADNigfgLEVAG--VPKKQRQAIIAEQLDLV-GLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL 198
Cdd:cd03224 88 PELTVEEN----LLLGAyaRRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 199 DPLIRnhlqDELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:cd03224 164 APKIV----EEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
43-255 |
4.87e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEgniyvgNAGKEINV--TTASSDELRYVRTRlVSMVFQQ-FG 119
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD------NPNSKITVdgITLTAKTVWDIREK-VGIVFQNpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:PRK13640 96 QFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 200 PLIRNHLQDELLELQKRLNKTLIFVSHDLDEAiKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
43-253 |
1.10e-31 |
|
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: 119.91 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEinVTTASSDELRYVRtRLVSMVFQQ-FGLF 121
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF--RGQD--LYQLDRKQRRAFR-RDVQLVFQDsPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 -PWRTVADNIGFGLE-VAGVPKKQRQAIIAEQLDLVGL-NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL 198
Cdd:TIGR02769 102 nPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 199 DPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRIL-QCGTAQ 253
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVeECDVAQ 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-250 |
1.78e-31 |
|
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: 117.68 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRkqALDladqgasraeikdltntvlgvhECSLDIAEGeTLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:cd03264 1 LQLENLTKRYGKKR--ALD----------------------GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IYVGnaGKEInvtTASSDELRyvrtRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANR 163
Cdd:cd03264 56 IRID--GQDV---LKQPQKLR----RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLDEAIKMGNRIAIMED 243
Cdd:cd03264 127 KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNK 204
|
....*..
gi 1946638175 244 GRILQCG 250
Cdd:cd03264 205 GKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-268 |
3.10e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.09 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 29 SRAEIKDL------TNTVLGVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIK-----PVEGNIYVGnaGKEINVTT 97
Cdd:PRK14247 2 NKIEIRDLkvsfgqVEVLDGV---NLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLD--GQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 98 ASsdELRyvrtRLVSMVFQQFGLFPWRTVADNIGFGLEVAGV--PKKQRQAIIAEQLDLVGL-NEWANRM---VTELSGG 171
Cdd:PRK14247 77 VI--ELR----RRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 172 MQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGT 251
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
250
....*....|....*..
gi 1946638175 252 AQEIVLTPANEHVANFV 268
Cdd:PRK14247 229 TREVFTNPRHELTEKYV 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
47-261 |
9.93e-31 |
|
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: 116.72 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN-IYV-GNA-GKEinvttassdELRYVRTR--LVSMVFQQFglF 121
Cdd:COG1119 23 SWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfGERrGGE---------DVWELRKRigLVSPALQLR--F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVADNI----GFGleVAGVPKK--QRQAIIAEQ-LDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEP 194
Cdd:COG1119 92 PRDETVLDVvlsgFFD--SIGLYREptDEQRERARElLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 195 FSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEiVLTPAN 261
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE-VLTSEN 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-256 |
1.30e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 116.33 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 1 MARVI-IDHVSVVFGNRRKQALDLADQGASRAEIKDLTNTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKP 79
Cdd:COG1134 1 MSSMIeVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWAL--KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 80 VEGNIYVgnagkeinvttassdelryvRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNE 159
Cdd:COG1134 79 TSGRVEV--------------------NGRVSALLELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 160 WANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIA 239
Cdd:COG1134 139 FIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAI 217
|
250
....*....|....*..
gi 1946638175 240 IMEDGRILQCGTAQEIV 256
Cdd:COG1134 218 WLEKGRLVMDGDPEEVI 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
34-250 |
1.49e-30 |
|
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: 115.54 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 34 KDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGkeinvtTASSDELRYVRTRLvSM 113
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DG------FDVVKEPAEARRRL-GF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 114 VFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDE 193
Cdd:cd03266 83 VSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 194 PFSALDPLIRNHLQdELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03266 163 PTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-259 |
2.17e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 119.18 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 21 LDLADQGASRAEikdlTNTVLGVHecsLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASS 100
Cdd:PRK09536 4 IDVSDLSVEFGD----TTVLDGVD---LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG----DDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 101 DELryvrTRLVSMVFQQFGL---FPWRTVadnigfgLEVAGVPKKQR--------QAIIAEQLDLVGLNEWANRMVTELS 169
Cdd:PRK09536 73 RAA----SRRVASVPQDTSLsfeFDVRQV-------VEMGRTPHRSRfdtwtetdRAAVERAMERTGVAQFADRPVTSLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 170 GGMQQRIGLARAFATGAPVLLMDEPFSALDPlirNHlQDELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDI---NH-QVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
250
....*....|...
gi 1946638175 247 LQCGtAQEIVLTP 259
Cdd:PRK09536 218 RAAG-PPADVLTA 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
32-247 |
3.00e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 114.24 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLG---VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGniyvgnagkEINVTTASSDELRYVRT 108
Cdd:cd03268 2 KTNDLTKTYGKkrvLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG---------EITFDGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQfGLFPWRTVADNIGFGLEVAGVPKKqrqaIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPV 188
Cdd:cd03268 73 RIGALIEAP-GFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRIL 247
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-250 |
8.17e-30 |
|
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: 113.78 E-value: 8.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRKQALDLADQGASRAEIKDLTNTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRKGEVGEFWAL--KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IyvgnagkeinvttassdelrYVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANR 163
Cdd:cd03220 79 V--------------------TVRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMED 243
Cdd:cd03220 139 PVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEK 217
|
....*..
gi 1946638175 244 GRILQCG 250
Cdd:cd03220 218 GKIRFDG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
41-268 |
8.99e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 114.49 E-value: 8.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 41 LGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINR---LIKP--VEGNIYVGnaGKEINVTTASSDELRyvrtRLVSMVF 115
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFH--GKNLYAPDVDPVEVR----RRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 116 QQFGLFPwRTVADNIGFGLEVAG--------VPKKQRQAI----IAEQLDLVGLNewanrmvteLSGGMQQRIGLARAFA 183
Cdd:PRK14243 98 QKPNPFP-KSIYDNIAYGARINGykgdmdelVERSLRQAAlwdeVKDKLKQSGLS---------LSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 184 TGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIM---------EDGRILQCGTAQE 254
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEK 245
|
250
....*....|....
gi 1946638175 255 IVLTPANEHVANFV 268
Cdd:PRK14243 246 IFNSPQQQATRDYV 259
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
40-259 |
1.02e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.96 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 40 VLGVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNI-YVGNagkeiNVTTASSDELRYVRTRlVSMVFQQ- 117
Cdd:PRK15079 37 VDGV---TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGK-----DLLGMKDDEWRAVRSD-IQMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 -FGLFPWRTVADNIGFGLEVAgVPKKQRQAI---IAEQLDLVGL-NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMD 192
Cdd:PRK15079 108 lASLNPRMTIGEIIAEPLRTY-HPKLSRQEVkdrVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 193 EPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
43-262 |
1.28e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 114.16 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeinvttassDELRY----VRTRLVSMVFQQF 118
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING------------HKLEYgdykYRCKHIRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 G--LFPwRTvadNIGFGLEVagvPKK--------QRQAIIAEQLDLVGL-NEWANRMVTELSGGMQQRIGLARAFATGAP 187
Cdd:COG4167 97 NtsLNP-RL---NIGQILEE---PLRlntdltaeEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 188 VLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANE 262
Cdd:COG4167 170 IIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHE 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
58-268 |
1.43e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.42 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 58 LMGLSGSGKSTLLRTINRLIKPVEGNIYVGN---AGKEInvtTASSDELRYvrTRLVSMVFQQFGLFPwRTVADNIGFGL 134
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllGGRSI---FNYRDVLEF--RRRVGMLFQRPNPFP-MSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 135 EVAG-VPKKQRQAIIAEQLDLVGLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDE 209
Cdd:PRK14271 126 RAHKlVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 210 LLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:PRK14271 206 IRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
43-264 |
1.67e-29 |
|
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: 113.02 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDElryvRTRL-VSMVFQQFGLF 121
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ----DITKLPMHK----RARLgIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 202 IRNHLQDELLELQKRLNKTLIfVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpANEHV 264
Cdd:cd03218 168 AVQDIQKIIKILKDRGIGVLI-TDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA---ANELV 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
48-268 |
2.46e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 113.40 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 48 LDIAEGETLVLMGLSGSGKSTLLRTINRLIK-----PVEGNIYVgnAGKEINVTTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRL--FGRNIYSPDVDPIEVR----REVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGV--PKKQRQAIIAEQLDLVGL-NEWANRM---VTELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 197 ALDPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEHVANFV 268
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
37-255 |
3.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.64 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 37 TNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeinVTTASSDELRYVRTRlVSMVFQ 116
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------LDTSDEENLWDIRNK-AGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 QfglfP-----WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLM 191
Cdd:PRK13633 93 N----PdnqivATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 192 DEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKmGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
39-248 |
4.41e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.86 E-value: 4.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 39 TVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvgnAGKEINVTTASSDELRYVRtRLVSMVFQQ- 117
Cdd:PRK10419 26 TVL--NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV----SWRGEPLAKLNRAQRKAFR-RDIQMVFQDs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLF-PWRTVADNIGFGLE-VAGVPKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEP 194
Cdd:PRK10419 99 ISAVnPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 195 FSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQ 248
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
47-246 |
4.80e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 111.19 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINvttassdelRYVRTRLVSMVFQ--QFGLFPwR 124
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN--GKPIK---------AKERRKSIGYVMQdvDYQLFT-D 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAGvpkkQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRN 204
Cdd:cd03226 88 SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1946638175 205 HLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03226 164 RVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
42-255 |
7.86e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.62 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 42 GVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTaSSDELRYVRTRlVSMVFQ--QFG 119
Cdd:PRK13641 22 GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI--AGYHITPET-GNKNLKKLRKK-VSLVFQfpEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNE-WANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL 198
Cdd:PRK13641 98 LFE-NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 199 DPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
47-247 |
1.99e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.98 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKeiNVTTASSDELRYVRTRLVSMVFQQFGLFPWRTV 126
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRV--AGQ--DVATLDADALAQLRREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDplirNHL 206
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD----SHS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1946638175 207 QDELLELQKRLNK---TLIFVSHDLDEAIKmGNRIAIMEDGRIL 247
Cdd:PRK10535 180 GEEVMAILHQLRDrghTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-259 |
2.03e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 115.72 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 6 IDHVSVVFGNRRKQALDLADQGASRAEIKD-LTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNI 84
Cdd:PRK10261 302 IEQDTVVDGEPILQVRNLVTRFPLRSGLLNrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 85 YVGnaGKEINvtTASSDELRYVRtRLVSMVFQQ--FGLFPWRTVADNIGFGLEVAGV-PKKQRQAIIAEQLDLVGLN-EW 160
Cdd:PRK10261 382 IFN--GQRID--TLSPGKLQALR-RDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEH 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 161 ANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:PRK10261 457 AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
250
....*....|....*....
gi 1946638175 241 MEDGRILQCGTAQEIVLTP 259
Cdd:PRK10261 537 MYLGQIVEIGPRRAVFENP 555
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-268 |
2.81e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.51 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 35 DLTNTVLGVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLiKPVEGNIYVGNA----GKEINVTTASSDELRyvrtRL 110
Cdd:PRK14258 18 DTQKILEGV---SMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRveffNQNIYERRVNLNRLR----RQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 111 VSMVFQQFGLFPwRTVADNIGFGLEVAG-VPKKQRQAIIAEQLDLVGL-NEWANRM---VTELSGGMQQRIGLARAFATG 185
Cdd:PRK14258 90 VSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwDEIKHKIhksALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 186 APVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMED-----GRILQCGTAQEIVLTPA 260
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
....*...
gi 1946638175 261 NEHVANFV 268
Cdd:PRK14258 249 DSRTREYV 256
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-255 |
2.86e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 111.25 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRrkqaldladqgaSRAEIKDLTNTvlgvhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:PRK13645 7 IILDNVSYTYAKK------------TPFEFKALNNT-------SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IYVGNAGKEINVTTASsdELRYVRtRLVSMVFQ--QFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGL-NEW 160
Cdd:PRK13645 68 TIVGDYAIPANLKKIK--EVKRLR-KEIGLVFQfpEYQLFQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 161 ANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:PRK13645 144 VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
250
....*....|....*
gi 1946638175 241 MEDGRILQCGTAQEI 255
Cdd:PRK13645 224 MHEGKVISIGSPFEI 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
43-264 |
4.12e-28 |
|
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: 109.30 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDElryvRTRL-VSMVFQQFGLF 121
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF--DGEDI--TGLPPHR----IARLgIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVADNigfgLEVAGVPKKQRQAIiAEQLDLVG-----LNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:COG0410 91 PSLTVEEN----LLLGAYARRDRAEV-RADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 197 ALDPLIRnhlqDELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpANEHV 264
Cdd:COG0410 166 GLAPLIV----EEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL---ADPEV 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
43-256 |
5.32e-28 |
|
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: 109.24 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG----HDVRDYTLASLR----RQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLV-GLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:cd03251 90 -DTVAENIAYGRPGATREEVEEAARAANAHEFImELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 198 LDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:cd03251 169 LDTESERLVQAALERLMK--NRTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
38-254 |
1.05e-27 |
|
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: 108.08 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 38 NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQ 117
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG----IDIRDISRKSLR----SMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLV-----GLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMD 192
Cdd:cd03254 86 TFLFS-GTIMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 193 EPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLDeAIKMGNRIAIMEDGRILQCGTAQE 254
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDE 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
47-255 |
1.32e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.06 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASSDeLRYVRTRlVSMVFQqfglFPW--- 123
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD--DTLITSTSKNKD-IKQIRKK-VGLVFQ----FPEsql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 --RTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNE-WANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:PRK13649 99 feETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 201 LIRNhlqdELLELQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13649 179 KGRK----ELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
43-255 |
1.99e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.41 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNI-YVGNAGK-------------EINVTTASSDELRYVRT 108
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKnkkktkekekvleKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 --RLVSMVFQ--QFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNE-WANRMVTELSGGMQQRIGLARAFA 183
Cdd:PRK13651 103 irRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 184 TGAPVLLMDEPFSALDPlirnHLQDELLELQKRLN---KTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDP----QGVKEILEIFDNLNkqgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
47-255 |
5.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.53 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeinvTTASSDELRYVRTRlVSMVFQQ-FGLFPWRT 125
Cdd:PRK13648 29 SFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN-------QAITDDNFEKLRKH-IGIVFQNpDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNH 205
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1946638175 206 LQDELLELQKRLNKTLIFVSHDLDEAIKmGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-260 |
9.73e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.63 E-value: 9.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 38 NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVG---NAGKEINVTTASSDELRYVRT-----R 109
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyIGDKKNNHELITNPYSKKIKNfkelrR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 110 LVSMVFQ--QFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNE-WANRMVTELSGGMQQRIGLARAFATGA 186
Cdd:PRK13631 117 RVSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 187 PVLLMDEPFSALDPLIRNHLQDELLElQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPA 260
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-269 |
9.96e-27 |
|
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: 105.70 E-value: 9.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 29 SRAEIKDLTNTvlgvhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYV-GNAGKEINvttassdeLRYVR 107
Cdd:cd03249 12 SRPDVPILKGL-------SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRDLN--------LRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 tRLVSMVFQQFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLV-GLNEWANRMV----TELSGGMQQRIGLARAF 182
Cdd:cd03249 77 -SQIGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDTLVgergSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 183 ATGAPVLLMDEPFSALDplirnhLQDElLELQKRLNK-----TLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEivL 257
Cdd:cd03249 155 LRNPKILLLDEATSALD------AESE-KLVQEALDRamkgrTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDE--L 224
|
250
....*....|..
gi 1946638175 258 TPANEHVANFVR 269
Cdd:cd03249 225 MAQKGVYAKLVK 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
43-256 |
1.11e-26 |
|
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: 105.65 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYV-GNagkeiNVTTASSDELRyvrtRLVSMVFQQFGLF 121
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGH-----DLALADPAWLR----RQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLV-GLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:cd03252 89 N-RSIRDNIALADPGMSMERVIEAAKLAGAHDFIsELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 197 ALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
47-246 |
1.17e-26 |
|
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: 104.98 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFpWRTV 126
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG----TDIRQLDPADLR----RNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAgvpKKQRqaiIAEQLDLVGLNEWANR-------MVTE----LSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:cd03245 95 RDNITLGAPLA---DDER---ILRAAELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 196 SALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRI 246
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
46-256 |
1.28e-26 |
|
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: 105.39 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 46 CSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEI-NVTTASsdeLRyvrtRLVSMVFQQFGLFPwR 124
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID--GQDIrEVTLDS---LR----RAIGVVPQDTVLFN-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAG---VPKKQRQAIIAEQLdlVGLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:cd03253 90 TIGYNIRYGRPDATdeeVIEAAKAAQIHDKI--MRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 198 LDPLIRNHLQDELLELQKrlNKTLIFVSHDLDEaIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:cd03253 168 LDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRIVERGTHEELL 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
47-228 |
1.29e-26 |
|
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: 110.07 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFPwRTV 126
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG----VPLADADADSWR----DQIAWVPQHPFLFA-GTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLV-GLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:TIGR02857 413 AENIRLARPDASDAEIREALERAGLDEFVaALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180
....*....|....*....|....*..
gi 1946638175 202 IRNHLQDELLELQKrlNKTLIFVSHDL 228
Cdd:TIGR02857 493 TEAEVLEALRALAQ--GRTVLLVTHRL 517
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
46-246 |
1.94e-26 |
|
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: 102.89 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 46 CSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTassdelryvrtrlvsmvfqqfglfpwrt 125
Cdd:cd03216 19 VSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--GKEVSFAS---------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 vadnigfglevagvPKKQRQAIIAeqldlvglnewanrMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPlirnH 205
Cdd:cd03216 69 --------------PRDARRAGIA--------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTP----A 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1946638175 206 LQDELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03216 117 EVERLFKVIRRLraqGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
43-272 |
2.27e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.48 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLI---KPVEGNIYVgnAGKEINVTTASSDELRYVRTRlVSMVFQQFG 119
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIEL--LGRTVQREGRLARDIRKSRAN-TGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADNIGFGlEVAGVP----------KKQRQAIIaEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVL 189
Cdd:PRK09984 97 LVNRLSVLENVLIG-ALGSTPfwrtcfswftREQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 190 LMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIvltpANEHVANFVR 269
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF----DNERFDHLYR 250
|
...
gi 1946638175 270 HIN 272
Cdd:PRK09984 251 SIN 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-256 |
3.45e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.78 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT----NTVLgVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKeiNVTTASSDELryvr 107
Cdd:COG4604 3 EIKNVSkrygGKVV-LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV--DGL--DVATTPSREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 TRLVSMVFQQFGLFPWRTVADNIGFGle--vaGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATG 185
Cdd:COG4604 74 AKRLAILRQENHINSRLTVRELVAFGrfpyskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 186 APVLLMDEPFSALDP--------LIRnHLQDEllelqkrLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:COG4604 154 TDYVLLDEPLNNLDMkhsvqmmkLLR-RLADE-------LGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
52-251 |
3.55e-26 |
|
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: 110.10 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 52 EGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTtassdeLRYVRTRLvSMVFQQFGLFPWRTVADNIG 131
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG--GKDIETN------LDAVRQSL-GMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 132 FGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELL 211
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1946638175 212 ELqkRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGT 251
Cdd:TIGR01257 1106 KY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
47-245 |
5.08e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEinVTTASSDELRyvrtRL-VSMVFQQFGLFPWRT 125
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID--GKP--VRIRSPRDAI----ALgIGMVHQHFMLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGVPKKQRQAIIAE----------QLDLvglnewaNRMVTELSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:COG3845 97 VAENIVLGLEPTKGGRLDRKAARARirelseryglDVDP-------DAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 196 SALDPlirnhlQ--DELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:COG3845 170 AVLTP------QeaDELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
43-255 |
7.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnagkEINVTTASSD-ELRYVRTRlVSMVFQ--QFG 119
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD----DITITHKTKDkYIRPVRKR-IGMVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPwRTVADNIGFGLEVAGVPKKQRQAIiAEQLdLVGLNEWANRMVT---ELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:PRK13646 98 LFE-DTVEREIIFGPKNFKMNLDEVKNY-AHRL-LMDLGFSRDVMSQspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 197 ALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
47-231 |
1.04e-25 |
|
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: 101.73 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVttaSSDELRYVRTRlVSMVFQ----QfgLFp 122
Cdd:TIGR01166 12 NFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLID--GEPLDY---SRKGLLERRQR-VGLVFQdpddQ--LF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:TIGR01166 83 AADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180 190
....*....|....*....|....*....|..
gi 1946638175 203 RNhlqdELLELQKRLN---KTLIFVSHDLDEA 231
Cdd:TIGR01166 163 RE----QMLAILRRLRaegMTVVISTHDVDLA 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
47-255 |
2.06e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 104.28 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagKEINVTTASSDELRYVRTRlVSMVFQQ-FG-LFPWR 124
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY----QGQDLLKADPEAQKLLRQK-IQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEV-AGVPKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:PRK11308 110 KVGQILEEPLLInTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 203 RNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-246 |
2.14e-25 |
|
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: 100.58 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 27 GASRAEIKDLTNTvLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDELRYV 106
Cdd:cd03215 1 GEPVLEVRGLSVK-GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL--DGKPV--TRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRLVSMVFQQFGLFPWRTVADNIGFGLEvagvpkkqrqaiiaeqldlvglnewanrmvteLSGGMQQRIGLARAFATGA 186
Cdd:cd03215 76 GIAYVPEDRKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 187 PVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
42-245 |
2.14e-25 |
|
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: 101.74 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 42 GVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINVTTASSDELRYVRTRLVSMVFQQFGLF 121
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILALRRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PwRTVAdnigfgLEV-------AGVPKKQRQAIIAEQLDLVGLNE--WANRMVTeLSGGMQQRIGLARAFATGAPVLLMD 192
Cdd:COG4778 106 P-RVSA------LDVvaeplleRGVDREEARARARELLARLNLPErlWDLPPAT-FSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 193 EPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLD--EAIkmGNRIAIMEDGR 245
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEvrEAV--ADRVVDVTPFS 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
45-246 |
2.45e-25 |
|
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: 100.37 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 45 ECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDELRyvrtRLVSMVFQQFGLFPwR 124
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA----DISQWDPNELG----DHVGYLPQDDELFS-G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIgfglevagvpkkqrqaiiaeqldlvglnewanrmvteLSGGMQQRIGLARAFaTGAP-VLLMDEPFSALDPLIR 203
Cdd:cd03246 91 SIAENI-------------------------------------LSGGQRQRLGLARAL-YGNPrILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1946638175 204 NHLQDELLELQKRlNKTLIFVSHDLdEAIKMGNRIAIMEDGRI 246
Cdd:cd03246 133 RALNQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
53-246 |
3.06e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.49 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 53 GETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTASSDELRYVRtRLVSMVFQQFGLFPWRTVADNIGF 132
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS--GHDI--TRLKNREVPFLR-RQIGMIFQDHHLLMDRTVYDNVAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 133 GLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDplirNHLQDELLE 212
Cdd:PRK10908 103 PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEGILR 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1946638175 213 LQKRLNK---TLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:PRK10908 179 LFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-259 |
5.57e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 102.90 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 1 MARVIIDHVSVVFGnrrkqaldlaDQGAS-RAeikdltntvlgVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKp 79
Cdd:PRK11022 1 MALLNVDKLSVHFG----------DESAPfRA-----------VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 80 vegniYVGNAGKE------INVTTASSDELRYVRTRLVSMVFQQ--FGLFPWRTVADNIGFGLEV-AGVPKKQRQAIIAE 150
Cdd:PRK11022 59 -----YPGRVMAEklefngQDLQRISEKERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAID 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 151 QLDLVGLNEWANRMVT---ELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHD 227
Cdd:PRK11022 134 LLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD 213
|
250 260 270
....*....|....*....|....*....|..
gi 1946638175 228 LDEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PRK11022 214 LALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-260 |
5.96e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLI--KPVE---GNIYVgnAGKeiNVTTASSDELRYVRTRLVSMVFQQ 117
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsPPVVypsGDIRF--HGE--SLLHASEQTLRGVRGNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 --FGLFPWRTVADNIgfgLEV----AGVPKKQRQAIIAEQLDLVGLNEWANRMVT---ELSGGMQQRIGLARAFATGAPV 188
Cdd:PRK15134 101 pmVSLNPLHTLEKQL---YEVlslhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPA 260
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
34-250 |
8.25e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 34 KDLTNTVLGVhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTAssdelRYVRTRlVSM 113
Cdd:PRK13647 15 KDGTKALKGL---SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV--MGREVNAENE-----KWVRSK-VGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 114 VFQ----QfgLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVL 189
Cdd:PRK13647 84 VFQdpddQ--VFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 190 LMDEPFSALDPlirnHLQDELLELQKRLN---KTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:PRK13647 161 VLDEPMAYLDP----RGQETLMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-256 |
9.02e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.04 E-value: 9.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 3 RVIIDHVSVVFGNRRKqaldladqgasraeikdltntvlGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEG 82
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQ-----------------------GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 83 NIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWA- 161
Cdd:PRK13657 391 RILIDG----TDIRTVTRASLR----RNIAVVFQDAGLFN-RSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGy 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 162 NRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNR 237
Cdd:PRK13657 462 DTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRL-STVRNADR 538
|
250
....*....|....*....
gi 1946638175 238 IAIMEDGRILQCGTAQEIV 256
Cdd:PRK13657 539 ILVFDNGRVVESGSFDELV 557
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
43-264 |
1.16e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvttasSDELRYVRTRL-VSMVFQQFGLF 121
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD--GEDI------THLPMHKRARLgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 pwR--TVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:COG1137 91 --RklTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 200 PLIRNHLQDELLELQKRLNKTLIfVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpANEHV 264
Cdd:COG1137 169 PIAVADIQKIIRHLKERGIGVLI-TDHNVRETLGICDRAYIISEGKVLAEGTPEEIL---NNPLV 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
47-255 |
1.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTASSDELRyvrtRLVSMVFQQFG--LFPwR 124
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI--KGEPIKYDKKSLLEVR----KTVGIVFQNPDdqLFA-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRN 204
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 205 HLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
47-255 |
1.84e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 104.06 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDELRyvrtRLVSMVFQQFGLFPwRTV 126
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA----DLSQWDREELG----RHIGYLPQDVELFD-GTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIgfglevAGVPKKQRQAII-AEQLdlVGLNEWANRM-------VTE----LSGGMQQRIGLARAFAtGAPVLL-MDE 193
Cdd:COG4618 423 AENI------ARFGDADPEKVVaAAKL--AGVHEMILRLpdgydtrIGEggarLSGGQRQRIGLARALY-GDPRLVvLDE 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 194 PFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
47-246 |
2.61e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSdelrYVRTRLVSMVFQ--QFGLFPWR 124
Cdd:COG1101 26 NLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KDVTKLPE----YKRAKYIGRVFQdpMMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNI----------GFGLevaGVPKKQRqAIIAEQLDLVGLN-EwaNRMVTE---LSGGmqQRIGLARAFATGAP--V 188
Cdd:COG1101 98 TIEENLalayrrgkrrGLRR---GLTKKRR-ELFRELLATLGLGlE--NRLDTKvglLSGG--QRQALSLLMATLTKpkL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 189 LLMDEPFSALDPlirnHLQDELLELQKRL----NKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:COG1101 170 LLLDEHTAALDP----KTAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
43-260 |
2.99e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.12 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN-IYVGNAgkeinVTTASSDELRYVRTRLVSMVFQQFGLF 121
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQP-----MSKLSSAAKAELRNQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK11629 100 PDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 202 IRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMgNRIAIMEDGRIlqcgtAQEIVLTPA 260
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL-----TAELSLMGA 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
56-259 |
3.24e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 56 LVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvttaSSDELRYVRtRLVSMVFQQFG--LFPwRTVADNIGFG 133
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLI--RGEPI-----TKENIREVR-KFVGLVFQNPDdqIFS-PTVEQDIAFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 134 LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLEL 213
Cdd:PRK13652 104 PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1946638175 214 QKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PRK13652 184 PETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
47-258 |
3.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDELRyvrtRLVSMVFQQ-FGLFPWRT 125
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE----LLTAENVWNLR----RKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNH 205
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 206 LQDELLELQKRLNKTLIFVSHDLDEAIKmGNRIAIMEDGRILQCGTAQEIVLT 258
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
51-255 |
4.48e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.10 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 51 AEGETLVLmGLSGSGKSTLLRTINRLIKPVEGNIYVGN-----AGKEINVTTassdelryvRTRLVSMVFQQFGLFPWRT 125
Cdd:PRK11144 23 AQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPP---------EKRRIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLevagvpKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDpLIRNH 205
Cdd:PRK11144 93 VRGNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 206 lqdELL----ELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK11144 166 ---ELLpyleRLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
47-255 |
5.47e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASSDELRyvrtRLVSMVFQQ--FGLFPwR 124
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD--GKPIDYSRKGLMKLR----ESVGMVFQDpdNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRN 204
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 205 HLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-264 |
7.41e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.29 E-value: 7.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagkeinVTTASSDELRYVRTRlVSMVFQQFGLFP 122
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--------LGVPVPARARLARAR-IGVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:PRK13536 128 EFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 203 RNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpaNEHV 264
Cdd:PRK13536 208 RHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI----DEHI 264
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
43-250 |
7.52e-24 |
|
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: 96.23 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvtTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD--GVPV---SDLEKALS----SLISVLNQRPYLFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGfglevagvpkkqrqaiiaeqldlvglnewanrmvTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:cd03247 89 -TTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1946638175 203 RNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03247 134 ERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
46-256 |
1.30e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.44 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 46 CSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFPwRT 125
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG----QPIADYSEAALR----QAISVVSQRVHLFS-AT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLevagvPKKQRQAIIA--EQLDL-------VGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:PRK11160 430 LRDNLLLAA-----PNASDEALIEvlQQVGLeklleddKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 197 ALDPLIRNHLQDELLELQKrlNKTLIFVSHDLDEAIKMgNRIAIMEDGRILQCGTAQEIV 256
Cdd:PRK11160 505 GLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELL 561
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
47-245 |
1.70e-23 |
|
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: 96.00 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeinvttassdelryvrtrlVSMVFQQfglfPW--- 123
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------------------IAYVSQE----PWiqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 RTVADNIGFGLEVAgvPKKQRQAIIAEQLDLvGLNEWANRMVTE-------LSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:cd03250 80 GTIRENILFGKPFD--EERYEKVIKACALEP-DLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1946638175 197 ALDPLIRNHLQDELLELQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGR 245
Cdd:cd03250 157 AVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-246 |
2.76e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.39 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTV-LGVHECS------LDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKeiNVTTASSDELR 104
Cdd:PRK10584 8 EVHHLKKSVgQGEHELSiltgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL--VGQ--PLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 YVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFAT 184
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 185 GAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMeDGRI 246
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLV-NGQL 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
43-231 |
8.32e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINVT--TASSDELRYVRTRLVSM-VFQQFG 119
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPqrSEVPDSLPLTVRDLVAMgRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 120 LFPWRTVADnigfglevagvpkkqrQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:NF040873 88 LWRRLTRDD----------------RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|..
gi 1946638175 200 PLIRNHLQDELLELQKRlNKTLIFVSHDLDEA 231
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
47-260 |
8.69e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.82 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeinVTTASSDELRYVRtRLVSMVFQQFGL-FPWRT 125
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG------IDTGDFSKLQGIR-KLVGIVFQNPETqFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPlirnH 205
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP----D 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 206 LQDELLELQKRLN---KTLIFVSHDLDEaIKMGNRIAIMEDGRILQCGTAQEIVLTPA 260
Cdd:PRK13644 171 SGIAVLERIKKLHekgKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
47-256 |
9.35e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.94 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASSdeLRyvrtRLVSMVFQQFGLFPwRTV 126
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD--GHDLRDYTLAS--LR----NQVALVSQNVHLFN-DTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFglevAGVPKKQRQAII-----AEQLDLV-GLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFS 196
Cdd:PRK11176 434 ANNIAY----ARTEQYSREQIEeaarmAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 197 ALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:PRK11176 510 ALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEKADEILVVEDGEIVERGTHAELL 566
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
32-260 |
9.47e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.10 E-value: 9.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNT-------VLGVHECSLDIAEGETLVLMGLSGSGKStllRTINRLIKPVEGNIYVGNA----GKEInvTTASS 100
Cdd:PRK09473 14 DVKDLRVTfstpdgdVTAVNDLNFSLRAGETLGIVGESGSGKS---QTAFALMGLLAANGRIGGSatfnGREI--LNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 101 DELRYVRTRLVSMVFQQ--FGLFPWRTVADNIgfgLEVAGVPKKQRQAIIAEQ----LDLVGLNEWANRMVT---ELSGG 171
Cdd:PRK09473 89 KELNKLRAEQISMIFQDpmTSLNPYMRVGEQL---MEVLMLHKGMSKAEAFEEsvrmLDAVKMPEARKRMKMyphEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 172 MQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGT 251
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
....*....
gi 1946638175 252 AQEIVLTPA 260
Cdd:PRK09473 246 ARDVFYQPS 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
47-207 |
1.16e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 93.58 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINvttassdELRYVRTRLVSMVFQQFGLFPWRTV 126
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN--GTPLA-------EQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGvpkkQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP------ 200
Cdd:TIGR01189 91 LENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKagvall 166
|
....*....
gi 1946638175 201 --LIRNHLQ 207
Cdd:TIGR01189 167 agLLRAHLA 175
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
47-206 |
1.20e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNI-YVGNAGKEINVTTASsdelRYVRTRlvsmvfqqFGLFPWRT 125
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIDDPDVAEAC----HYLGHR--------NAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEVAGvpkkQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP----- 200
Cdd:PRK13539 90 VAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAaaval 165
|
....*....
gi 1946638175 201 ---LIRNHL 206
Cdd:PRK13539 166 faeLIRAHL 174
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
39-261 |
4.49e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 39 TVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGN------AGKEINVTTASSDELRYVRTRLVS 112
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrSRQVIELSEQSAAQMRHVRGADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 113 MVFQQ--FGLFPWRTVADNIGFGLEV-AGVPKKQRQAIIAEQLDLVGLNEWA---NRMVTELSGGMQQRIGLARAFATGA 186
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 187 PVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPAN 261
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-256 |
5.26e-22 |
|
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: 96.80 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGV---HECSLDIAEGETLVLMGLSGSGKSTLLRTINRL--IKPVEGNI-----------YVGNAGK---- 91
Cdd:TIGR03269 2 EVKNLTKKFDGKevlKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVERPSKvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 92 -----------EINVTTASSDELRYVRTRLVSMVFQQFGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEW 160
Cdd:TIGR03269 82 cpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 161 ANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAI 240
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIW 241
|
250
....*....|....*.
gi 1946638175 241 MEDGRILQCGTAQEIV 256
Cdd:TIGR03269 242 LENGEIKEEGTPDEVV 257
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
47-228 |
6.74e-22 |
|
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: 96.28 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFPwRTV 126
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG----VPVSSLDQDEVR----RRVSVCAQDAHLFD-TTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGvpkkqrQAIIAEQLDLVGLNEWANRM-------VTE----LSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:TIGR02868 426 RENLRLARPDAT------DEELWAALERVGLADWLRALpdgldtvLGEggarLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|...
gi 1946638175 196 SALDPLIRNHLQDELLELQKRlnKTLIFVSHDL 228
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
44-256 |
1.49e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.36 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGN------AGKEI---------NVTTASSDELRYVRT 108
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyASKEVarrigllaqNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RlvsmvfqqfGLFP-------WRtvadnigfglevagvpkKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARA 181
Cdd:PRK10253 104 R---------GRYPhqplftrWR-----------------KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 182 FATGAPVLLMDEPFSALDPlirNHlQDELLELQKRLNK----TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDI---SH-QIDLLELLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
42-250 |
1.77e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.91 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 42 GVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNI-YVGNAGKEINVTTASSDELRYV-RTRLvSMVFQ--Q 117
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALSEAERRRLlRTEW-GFVHQhpR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLFPWRTVADNIGFGLEVAGVPKKQR-QAIIAEQLDLVGLNewANRM---VTELSGGMQQRIGLARAFATGAPVLLMDE 193
Cdd:PRK11701 100 DGLRMQVSAGGNIGERLMAVGARHYGDiRATAGDWLERVEID--AARIddlPTTFSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 194 PFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCG 250
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-264 |
1.89e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 33 IKDLTNTVLG---VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINVTTASSDELRYVRTR 109
Cdd:PRK10575 14 LRNVSFRVPGrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 110 LVS---MVFQQF---GLFPWRTvadnigfGLEVAGVPKKQRqaiIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFA 183
Cdd:PRK10575 94 LPAaegMTVRELvaiGRYPWHG-------ALGRFGAADREK---VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 184 TGAPVLLMDEPFSALDplIRNhlQDELLELQKRLNK----TLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PRK10575 164 QDSRCLLLDEPTSALD--IAH--QVDVLALVHRLSQerglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
....*
gi 1946638175 260 ANEHV 264
Cdd:PRK10575 240 TLEQI 244
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-256 |
2.83e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvttasSDELRYVRTRlVSMVFQQFGLFP 122
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL--CGEPV------PSRARHARQR-VGVVPQFDNLDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:PRK13537 94 DFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 203 RNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:PRK13537 174 RHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
43-262 |
4.59e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.91 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKS----TLLRTINRLIKPVEGNIYVGnaGKEInvttASSDelryVRTRLVSMVFQ-- 116
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLD--GKPV----APCA----LRGRKIATIMQnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 QFGLFPWRTVADNIGFGLEVAGVPKkqRQAIIAEQLDLVGLNEwANRMVT----ELSGGMQQRIGLARAFATGAPVLLMD 192
Cdd:PRK10418 89 RSAFNPLHTMHTHARETCLALGKPA--DDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 193 EPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANE 262
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
42-259 |
6.08e-21 |
|
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: 90.27 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 42 GVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNI-YVGNAGKEINVTTASSDELRYVRTRLVSMVFQQF-- 118
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELYQLSEAERRRLMRTEWGFVHQNPrd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 GLFPWRTVADNIGFGLEVAGVPKKQR-QAIIAEQLDLVGLNewANRM---VTELSGGMQQRIGLARAFATGAPVLLMDEP 194
Cdd:TIGR02323 98 GLRMRVSAGANIGERLMAIGARHYGNiRATAQDWLEEVEID--PTRIddlPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 195 FSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
43-257 |
2.59e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.11 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG----FSLKDIDRHTLR----QFINYLPQEPYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIgfgleVAGVPKKQRQAIIAEQLDLVGLNEWANRM-----------VTELSGGMQQRIGLARAFATGAPVLLM 191
Cdd:TIGR01193 562 -GSILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMplgyqtelseeGSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 192 DEPFSALDPLIRNHLQDELLELQkrlNKTLIFVSHDLDEAiKMGNRIAIMEDGRILQCGTAQEIVL 257
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-246 |
6.04e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTvLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASsDELR----YV- 106
Cdd:COG1129 258 EVEGLSVG-GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD--GKPVRIRSPR-DAIRagiaYVp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 --RTRLvsmvfqqfGLFPWRTVADNIGFG----LEVAGVPKKQRQAIIAEqldlvglnEWANRM----------VTELSG 170
Cdd:COG1129 334 edRKGE--------GLVLDLSIRENITLAsldrLSRGGLLDRRRERALAE--------EYIKRLriktpspeqpVGNLSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 171 GMQQRIGLARAFATGAPVLLMDEPFSALDP--------LIRnhlqdellELQKRlNKTLIFVSHDLDEAIKMGNRIAIME 242
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaeiyrLIR--------ELAAE-GKAVIVISSELPELLGLSDRILVMR 468
|
....
gi 1946638175 243 DGRI 246
Cdd:COG1129 469 EGRI 472
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
38-250 |
9.41e-20 |
|
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: 86.56 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 38 NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLI---KPVEGNIYVgnAGKEINvttassdelRYVRTRLVSMV 114
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILF--NGQPRK---------PDQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 115 FQQFGLFPWRTVADNIGFGLEVAGvPKKQRQAIIAEQLDLVGLNEWANRMV-----TELSGGMQQRIGLARAFATGAPVL 189
Cdd:cd03234 87 RQDDILLPGLTVRETLTYTAILRL-PRKSSDAIRKKRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 190 LMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHD-LDEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
43-230 |
2.38e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInvTTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF--EGEDI--STLKPEIYR----QQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGFGLEVAGvpKKQRQAIIAEQLDLVGL-NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK10247 95 -DTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180
....*....|....*....|....*....
gi 1946638175 202 IRNHLQDELLELQKRLNKTLIFVSHDLDE 230
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
47-246 |
1.02e-18 |
|
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: 83.67 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTtassdELRYVRtRLVSMVFQQFGLFPwRTV 126
Cdd:cd03248 34 SFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD--GKPISQY-----EHKYLH-SKVSLVGQEPVLFA-RSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLV-----GLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFIselasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1946638175 202 IRNHLQDELLELQKRlnKTLIFVSHDLdEAIKMGNRIAIMEDGRI 246
Cdd:cd03248 185 SEQQVQQALYDWPER--RTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
47-255 |
1.11e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 87.02 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINvttassdelRYVRTRL---VSMVFQQFGLFPw 123
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD--GADLK---------QWDRETFgkhIGYLPQDVELFP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 RTVADNIG-FGLEVagvpkkQRQAIIaEQLDLVGLNEWANRMV-----------TELSGGMQQRIGLARAFaTGAP-VLL 190
Cdd:TIGR01842 406 GTVAENIArFGENA------DPEKII-EAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARAL-YGDPkLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 191 MDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
32-255 |
1.39e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEI-NVTTASSDELRYVR 107
Cdd:PRK11300 7 SVSGLMmrfGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR--GQHIeGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 TrlvsmvFQQFGLFPWRTVADNI----------GF--GL-EVAGVPKKQRQAI--IAEQLDLVGLNEWANRMVTELSGGM 172
Cdd:PRK11300 85 T------FQHVRLFREMTVIENLlvaqhqqlktGLfsGLlKTPAFRRAESEALdrAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 173 QQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTA 252
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
...
gi 1946638175 253 QEI 255
Cdd:PRK11300 239 EEI 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
39-262 |
1.90e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 39 TVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYvgnagkeINVTTASSDELRYvRTRLVSMVFQ-- 116
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL-------IDDHPLHFGDYSY-RSQRIRMIFQdp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 QFGLFPWRTVADNIGFGLEV-AGVPKKQRQAIIAEQLDLVGL-NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEP 194
Cdd:PRK15112 97 STSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 195 FSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANE 262
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHE 244
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-251 |
1.90e-18 |
|
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: 82.54 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASsdeLRYV 106
Cdd:cd03244 4 EFKNVSlryrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG----VDISKIG---LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRLvSMVFQQFGLFPwRTVADNIGfglevagvPKKQRQ-AIIAEQLDLVGLNEWANRM-------VTE----LSGGMQQ 174
Cdd:cd03244 77 RSRI-SIIPQDPVLFS-GTIRSNLD--------PFGEYSdEELWQALERVGLKEFVESLpggldtvVEEggenLSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 175 RIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLElqKRLNKTLIFVSHDLDEAIKMgNRIAIMEDGRILQCGT 251
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDS 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-263 |
2.28e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKST----LLRTINRlikpvEGNIYVgnAGKEINvtTASSDELRYVRTRlVSMVFQ-- 116
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWF--DGQPLH--NLNRRQLLPVRHR-IQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 QFGLFPWRTVADNIGFGLEV--AGVPKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDE 193
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 194 PFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVLTPANEH 263
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-255 |
2.49e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGVH---ECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEIN-VTTASSDELRyvr 107
Cdd:PRK09700 7 SMAGIGKSFGPVHalkSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNINYNkLDHKLAAQLG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 trlVSMVFQQFGLFPWRTVADNIGFGL----EVAGVP----KKQRQaIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLA 179
Cdd:PRK09700 82 ---IGIIYQELSVIDELTVLENLYIGRhltkKVCGVNiidwREMRV-RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 180 RAFATGAPVLLMDEPFSALDplirNHLQDELLELQKRLN---KTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLT----NKEVDYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
47-246 |
9.19e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeiNVTTAssdelrYVRtrlvsmvfQQFGLFPWRTV 126
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----GLRIG------YLP--------QEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAE--------------QLDLVGLNEWA-------------------NRMVTELSGGMQ 173
Cdd:COG0488 79 LDTVLDGDAELRALEAELEELEAKlaepdedlerlaelQEEFEALGGWEaearaeeilsglgfpeedlDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 174 QRIGLARAFATGAPVLLMDEPfsaldpliRNHLqD----ELLE--LQKRlNKTLIFVSHD---LDEAIkmgNRIAIMEDG 244
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEP--------TNHL-DlesiEWLEefLKNY-PGTVLVVSHDryfLDRVA---TRILELDRG 225
|
..
gi 1946638175 245 RI 246
Cdd:COG0488 226 KL 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
32-226 |
1.30e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-----NTVLgVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvgnagkeinvttassdelryV 106
Cdd:COG4178 364 ALEDLTlrtpdGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI---------------------A 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRLVSMVFqqfglFPWR------TVADNIGFGLEVAGVPkkqrQAIIAEQLDLVGLNEWANRMVTE------LSGGMQQ 174
Cdd:COG4178 422 RPAGARVLF-----LPQRpylplgTLREALLYPATAEAFS----DAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 175 RIGLARAFATGAPVLLMDEPFSALDPlirnHLQDELLE-LQKRLNK-TLIFVSH 226
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDE----ENEAALYQlLREELPGtTVISVGH 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-246 |
1.37e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 14 GNRRKQAldladQGASRAEIKDLTNTvlGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEI 93
Cdd:PRK15439 257 GNRRQQA-----AGAPVLTVEDLTGE--GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLN--GKEI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 94 NVttassdelRYVRTRLVS-MVF-----QQFGLF-----PWRTVA---DNIGFGLEvagvPKKQRqAIIAEQLDLVGLN- 158
Cdd:PRK15439 328 NA--------LSTAQRLARgLVYlpedrQSSGLYldaplAWNVCAlthNRRGFWIK----PAREN-AVLERYRRALNIKf 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 159 EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRI 238
Cdd:PRK15439 395 NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRV 473
|
....*...
gi 1946638175 239 AIMEDGRI 246
Cdd:PRK15439 474 LVMHQGEI 481
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
44-254 |
2.34e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 82.95 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEI-NVTTASsdeLRyvrtRLVSMVFQQFGLFP 122
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID--GQDIrDVTQAS---LR----AAIGIVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGFGL------EVagvpkkqRQAIIAEQLD--LVGLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLL 190
Cdd:COG5265 446 -DTIAYNIAYGRpdaseeEV-------EAAARAAQIHdfIESLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 191 MDEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSH------DLDEaikmgnrIAIMEDGRILQCGTAQE 254
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivDADE-------ILVLEAGRIVERGTHAE 578
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-255 |
2.58e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 33 IKDLTNTvlgvhecsldIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvttaSSDELRYVRTRlVS 112
Cdd:TIGR00958 497 LKGLTFT----------LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD--GVPL-----VQYDHHYLHRQ-VA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 113 MVFQQFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGlnEWANRMVTE-------LSGGMQQRIGLARAFATG 185
Cdd:TIGR00958 559 LVGQEPVLFS-GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDTEvgekgsqLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 186 APVLLMDEPFSALDPLIRNHLQdellELQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQ----ESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
50-244 |
2.70e-17 |
|
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: 79.68 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 50 IAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINVTTASSDELRYVrtrlVSMVFQQfglfPW---RTV 126
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS----VAYAAQK----PWllnATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVagvpKKQRQAIIAE------QLDLVGL---NEWANRMVTeLSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:cd03290 96 EENITFGSPF----NKQRYKAVTDacslqpDIDLLPFgdqTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1946638175 198 LDPLIRNHL-QDELLELQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDG 244
Cdd:cd03290 171 LDIHLSDHLmQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-246 |
7.70e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 24 ADQGASRAEIKDLT----NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvTTAS 99
Cdd:COG3845 251 AEPGEVVLEVENLSvrddRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD--GEDI--TGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 100 SDELR-----YV---RTRlvsmvfqqFGLFPWRTVADNIgfGLEVAGVPKKQRQAIiaeqLDLVGLNEWANRMVTE---- 167
Cdd:COG3845 327 PRERRrlgvaYIpedRLG--------RGLVPDMSVAENL--ILGRYRRPPFSRGGF----LDRKAIRAFAEELIEEfdvr 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 168 ----------LSGGMQQRIGLARAFATGAPVLLMDEPFSALDP----LIRNhlqdELLELQKRlNKTLIFVSHDLDEAIK 233
Cdd:COG3845 393 tpgpdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQ----RLLELRDA-GAAVLLISEDLDEILA 467
|
250
....*....|...
gi 1946638175 234 MGNRIAIMEDGRI 246
Cdd:COG3845 468 LSDRIAVMYEGRI 480
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
38-256 |
8.08e-17 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 79.09 E-value: 8.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 38 NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvgnagkeinvttassdelryVRTRLVSMVFQQ 117
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---------------------DRNGEVSVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGLFPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 198 LDPLIRNHLQDELLELqKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIV 256
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
32-246 |
9.15e-17 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.21 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTV---LGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagkeinvttassDELRYVRT 108
Cdd:TIGR03740 2 ETKNLSKRFgkqTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF--------------DGHPWTRK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSM--VFQQFGLFPWRTVADNIGFGLEVAGVPKKQrqaiIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGA 186
Cdd:TIGR03740 68 DLHKIgsLIESPPLYENLTARENLKVHTTLLGLPDSR----IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 187 PVLLMDEPFSALDPLIRNHLQdELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELR-ELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
47-245 |
1.73e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTAssdelryvRTRL---VSMVFQQFGLFPW 123
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID--GQEMRFAST--------TAALaagVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 RTVADNIGFG-LEVAG--VPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL-- 198
Cdd:PRK11288 94 MTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsa 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 199 ---DPLIR--NHLQDEllelqkrlNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:PRK11288 174 reiEQLFRviRELRAE--------GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
47-199 |
1.92e-16 |
|
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: 76.76 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGkeinvttasSDELRYVRTRLVSMVFQQFGLFPWRTV 126
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP---------LDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 127 ADNIGFGLEVAGvpkkqrQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:cd03231 91 LENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
47-261 |
2.09e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIkPVEGNIYVgnAGKeiNVTTASSDELRYVRTRLV-------SM-VFQQF 118
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQF--AGQ--PLEAWSAAELARHRAYLSqqqtppfAMpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 GLFpwrtvadnigfglEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAP-------VLLM 191
Cdd:PRK03695 91 TLH-------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 192 DEPFSALDPLIRNHLqDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEiVLTPAN 261
Cdd:PRK03695 158 DEPMNSLDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE-VLTPEN 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-247 |
2.72e-16 |
|
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: 76.99 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 6 IDHVSVVFGNRRKQALDLadqGASRAEIKDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIY 85
Cdd:cd03267 3 VSNLSKSYRVYSKEPGLI---GSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 86 VGNagkeiNVTTASSDELRyvrtRLVSMVFQQFGLFPWR-TVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRM 164
Cdd:cd03267 80 VAG-----LVPWKRRKKFL----RRIGVVFGQKTQLWWDlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 165 VTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDG 244
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
...
gi 1946638175 245 RIL 247
Cdd:cd03267 231 RLL 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-268 |
3.35e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 14 GNRRKQALDLADQGASRAEIKDLTNTVLGVHEcsldiaEGETLVLMGLSGSGKSTLLRTI-NRLIKPVEGNIYVGNAGKE 92
Cdd:TIGR00955 18 GSWKQLVSRLRGCFCRERPRKHLLKNVSGVAK------PGELLAVMGSSGAGKTTLMNALaFRSPKGVKGSGSVLLNGMP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 93 INvttasSDELryvrtRLVSMVFQQFGLF-PWRTVADNIGFGLEV---AGVPKKQRQAIIAEQLDLVGLNEWAN------ 162
Cdd:TIGR00955 92 ID-----AKEM-----RAISAYVQQDDLFiPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANtrigvp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 163 RMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLEL-QKRlnKTLIFVSHD-LDEAIKMGNRIAI 240
Cdd:TIGR00955 162 GRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKG--KTIICTIHQpSSELFELFDKIIL 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1946638175 241 MEDGRILQCGTAQEIV--------LTPANEHVANFV 268
Cdd:TIGR00955 240 MAEGRVAYLGSPDQAVpffsdlghPCPENYNPADFY 275
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
43-266 |
3.67e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEI-NVTTAssdelRYVRtRLVSMVFQQFGLF 121
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD--GKDItDWQTA-----KIMR-EAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVADNIGFGLEVAgvPKKQRQAIIAEQLDLVG-LNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:PRK11614 93 SRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 201 LIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpANEHVAN 266
Cdd:PRK11614 171 IIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL---ANEAVRS 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
43-260 |
5.52e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.79 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTInrlikpvEGNIYVGNAGKEINVT---------TASSDELRYVRTRLVSM 113
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAL-------AGDLTGGGAPRGARVTgdvtlngepLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 114 VFQQFGlFPWrTVADNIGFG----LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFA------ 183
Cdd:PRK13547 90 QAAQPA-FAF-SAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 184 ---TGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEiVLTPA 260
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD-VLTPA 246
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
47-261 |
8.08e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 8.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIkPVEGNIYVgnAGKEINvtTASSDELRYVRTRLVSMVFQQFGLfpwrTV 126
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILL--NGRPLS--DWSAAELARHRAYLSQQQSPPFAM----PV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAI--IAEQLdlvGLNEWANRMVTELSGGMQQRIGLARAF--------ATGApVLLMDEPFS 196
Cdd:COG4138 87 FQYLALHQPAGASSEAVEQLLaqLAEAL---GLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinPEGQ-LLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 197 ALDplIRNHLQ-DELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEiVLTPAN 261
Cdd:COG4138 163 SLD--VAQQAAlDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE-VMTPEN 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
58-245 |
9.98e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.85 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 58 LMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTaSSDELRyvrtRLVSMVFQQFGLFPWRTVADNIGFGLeva 137
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILF--QGKEIDFKS-SKEALE----NGISMVHQELNLVLQRSVMDNMWLGR--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 138 gVPKK-----------QRQAIIAEqldlVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:PRK10982 99 -YPTKgmfvdqdkmyrDTKAIFDE----LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1946638175 207 QDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:PRK10982 174 FTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
47-255 |
1.16e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.81 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTASSDELRyvrtRLVSMVFQ--QFGLFpWR 124
Cdd:PRK13638 21 NLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW--QGKPLDYSKRGLLALR----QQVATVFQdpEQQIF-YT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRN 204
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 205 hlqdELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK13638 174 ----QMIAIIRRIvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
43-271 |
1.20e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINvttassdelRYVRTRLVSMVFQQFGL-- 120
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI--LGQPTR---------QALQKNLVAYVPQSEEVdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 121 -FPwRTVADNIGFG----LEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPF 195
Cdd:PRK15056 92 sFP-VLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 196 SALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNrIAIMEDGRILQCGTAqEIVLTPANEHVA--NFVRHI 271
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPT-ETTFTAENLELAfsGVLRHV 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
47-246 |
1.77e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.32 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeiNVTTASSDELRyvrtRLVSMVFQQFGLFpwRTV 126
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK----PVTAEQPEDYR----KLFSAVFTDFHLF--DQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGlNEWANrmvTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:PRK10522 413 LGPEGKPANPALVEKWLERLKMAHKLELED-GRISN---LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1946638175 207 QDELLELQKRLNKTLIFVSHDlDEAIKMGNRIAIMEDGRI 246
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
32-271 |
2.61e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.61 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPvegNIYVgNAGK----EINVTTASS 100
Cdd:PRK15093 5 DIRNLTiefktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD---NWRV-TADRmrfdDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 101 DELRYVRTRLVSMVFQ--QFGLFPwrtvADNIGFGLeVAGVPK-------------KQRQAIiaEQLDLVGLNEWANRMV 165
Cdd:PRK15093 81 RERRKLVGHNVSMIFQepQSCLDP----SERVGRQL-MQNIPGwtykgrwwqrfgwRKRRAI--ELLHRVGIKDHKDAMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 166 T---ELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIrnhlQDELLELQKRLNK----TLIFVSHDLDEAIKMGNRI 238
Cdd:PRK15093 154 SfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTT----QAQIFRLLTRLNQnnntTILLISHDLQMLSQWADKI 229
|
250 260 270
....*....|....*....|....*....|...
gi 1946638175 239 AIMEDGRILQCGTAQEIVLTPANEHVANFVRHI 271
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTTPHHPYTQALIRAI 262
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-255 |
2.88e-15 |
|
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: 77.36 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGVHECSLD-----IAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTtassdelryv 106
Cdd:TIGR01257 1939 RLNELTKVYSGTSSPAVDrlcvgVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV--AGKSILTN---------- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 rtrlVSMVFQQFGLFPWRTVADNIGFGLE-------VAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLA 179
Cdd:TIGR01257 2007 ----ISDVHQNMGYCPQFDAIDDLLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 180 RAFATGAPVLLMDEPFSALDPLIRNHLQDELLELqKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
50-200 |
3.37e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 50 IAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvgnagkEINVTTASSDElryvRTRLVSMVFQQFGLFPWRTVADN 129
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-------QIDGKTATRGD----RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 130 IGFgleVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:PRK13543 103 LHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
47-245 |
4.22e-15 |
|
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: 71.33 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvgnagkeinvTTASSDELRYvrtrlvsmvFQQfglfpwrtv 126
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVKIGY---------FEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 adnigfglevagvpkkqrqaiiaeqldlvglnewanrmvteLSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1946638175 207 QDELlelqKRLNKTLIFVSHD---LDEAIkmgNRIAIMEDGR 245
Cdd:cd03221 110 EEAL----KEYPGTVILVSHDryfLDQVA---TKIIELEDGK 144
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
47-259 |
5.55e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.65 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIkPVEGNIyvgnagkEINVTTASSDELRYVRtRLVSMVFQQFGLFPwRTV 126
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL-------KINGIELRELDPESWR-KHLSWVGQNPQLPH-GTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGlevagvpkkqRQAIIAEQLDLVGLNEWANRMVTE---------------LSGGMQQRIGLARAFATGAPVLLM 191
Cdd:PRK11174 440 RDNVLLG----------NPDASDEQLQQALENAWVSEFLPLlpqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 192 DEPFSALDPLIRNHLQDELLELQKRlnKTLIFVSHDLDEAIKMgNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
32-259 |
6.14e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.56 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPvegNIYVgNAG----KEINVTTASSDELRYVR 107
Cdd:COG4170 12 EIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD---NWHV-TADrfrwNGIDLLKLSPRERRKII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 108 TRLVSMVFQ--QFGLFPWRTVADNIgfgLEVagVP-----------KKQRQAIIAEQLDLVG-------LNEWANrmvtE 167
Cdd:COG4170 88 GREIAMIFQepSSCLDPSAKIGDQL---IEA--IPswtfkgkwwqrFKWRKKRAIELLHRVGikdhkdiMNSYPH----E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 168 LSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIrnhlQDELLELQKRLNK----TLIFVSHDLDEAIKMGNRIAIMED 243
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTT----QAQIFRLLARLNQlqgtSILLISHDLESISQWADTITVLYC 234
|
250
....*....|....*.
gi 1946638175 244 GRILQCGTAQEIVLTP 259
Cdd:COG4170 235 GQTVESGPTEQILKSP 250
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-259 |
6.75e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.52 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 24 ADQGASRAEIKDLT---NTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASS 100
Cdd:PRK10789 309 EGRGELDVNIRQFTypqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD----IPLTKLQL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 101 DELRyvrTRLvSMVFQQFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAE-QLDLVGLNEWANRMVTE----LSGGMQQR 175
Cdd:PRK10789 385 DSWR---SRL-AVVSQTPFLFS-DTVANNIALGRPDATQQEIEHVARLASvHDDILRLPQGYDTEVGErgvmLSGGQKQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 176 IGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELleLQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQL 536
|
....
gi 1946638175 256 VLTP 259
Cdd:PRK10789 537 AQQS 540
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
53-246 |
7.75e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 53 GETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgKEINVTTASSDELRyvrtrlVSMVFQQFGLFPWRTVADNIGF 132
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-PCARLTPAKAHQLG------IYLVPQEPLLFPNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 133 GLEVAGVPKKQRQAIIAE---QLDL---VGLNEWANRMVTELsggMQqriGLARafatGAPVLLMDEPFSALDPLIRNHL 206
Cdd:PRK15439 110 GLPKRQASMQKMKQLLAAlgcQLDLdssAGSLEVADRQIVEI---LR---GLMR----DSRILILDEPTASLTPAETERL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1946638175 207 QDELLELQKrLNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:PRK15439 180 FSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
43-250 |
1.31e-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: 71.43 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTIN--RLIKPVEGNIYvgnagkeINVTTASSDELRyvrtRLVSMVFQQFGL 120
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVL-------INGRPLDKRSFR----KIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 121 FPWRTVADNIGFGLEVAGvpkkqrqaiiaeqldlvglnewanrmvteLSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:cd03213 94 HPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 201 liRNHLQdeLLELQKRL---NKTLIFVSHDL-DEAIKMGNRIAIMEDGRILQCG 250
Cdd:cd03213 145 --SSALQ--VMSLLRRLadtGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
44-199 |
5.39e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.83 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINvttASSDELRYvrtrlvSMVF--QQFGLF 121
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--GEPIR---RQRDEYHQ------DLLYlgHQPGIK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 122 PWRTVADNIGFGLEVAGVpkkQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:PRK13538 87 TELTALENLRFYQRLHGP---GDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
47-246 |
7.12e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeiNVTTA----SSDELRyvrtrlvsmvfqqfglfP 122
Cdd:COG0488 335 SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-----TVKIGyfdqHQEELD-----------------P 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIgfgleVAGVPKKQRQAIIA--EQLDLVGlnEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPfsaldp 200
Cdd:COG0488 393 DKTVLDEL-----RDGAPGGTEQEVRGylGRFLFSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP------ 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 201 liRNHLQDELLE-LQKRLNK---TLIFVSHD---LDeaiKMGNRIAIMEDGRI 246
Cdd:COG0488 460 --TNHLDIETLEaLEEALDDfpgTVLLVSHDryfLD---RVATRILEFEDGGV 507
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
39-247 |
1.11e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 39 TVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKeinvtTASSDELRYVRTrlVSMVFQQf 118
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV--LGY-----VPFKRRKEFARR--IGVVFGQ- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 glfpwRT-------VADNigFGL--EVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGmqQRI--GLARAFATGAP 187
Cdd:COG4586 104 -----RSqlwwdlpAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG--QRMrcELAAALLHRPK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 188 VLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRIL 247
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
47-229 |
1.57e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIK--PVEGNIyvgnagkEINVTTASSDelryvrtrlvsmvfqqfglfpwR 124
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV-------DVPDNQFGRE----------------------A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGLEVAgvpkkqrQAIiaEQLDLVGLNEWAN--RMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:COG2401 101 SLIDAIGRKGDFK-------DAV--ELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*..
gi 1946638175 203 RNHLQDELLELQKRLNKTLIFVSHDLD 229
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-273 |
1.69e-13 |
|
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: 71.90 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeinvttassdelryvrtrlVSMVFQQfglfP 122
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------------------VAYVPQQ----A 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 W---RTVADNIGFGLEVAgvPKKQRQAIIAEQL--DLVGLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDE 193
Cdd:TIGR00957 709 WiqnDSLRENILFGKALN--EKYYQQVLEACALlpDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 194 PFSALDPLIRNHLQDELLELQKRL-NKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEivLTPANEHVANFVRHIN 272
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQE--LLQRDGAFAEFLRTYA 863
|
.
gi 1946638175 273 P 273
Cdd:TIGR00957 864 P 864
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-254 |
1.78e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLG-VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVttasSDELRYVRT-- 108
Cdd:PRK09700 267 EVRNVTSRDRKkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN--GKDISP----RSPLDAVKKgm 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQFGLFPWRTVADNI---------GFGLEVAGVPKKQRQAIIAEQLDLVGLN-EWANRMVTELSGGMQQRIGL 178
Cdd:PRK09700 341 AYITESRRDNGFFPNFSIAQNMaisrslkdgGYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 179 ARAFATGAPVLLMDEPFSALDPLIRNhlqdELLELQKRL---NKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQE 254
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKA----EIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
47-255 |
1.87e-13 |
|
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: 71.48 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYvgNAGKeinvttassdelryvrtrlVSMVFQqfglFPW--- 123
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGR-------------------ISFSPQ----TSWimp 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 RTVADNIGFGLEVAGVpkKQRQAIIAEQL--DLVGLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:TIGR01271 501 GTIKDNIIFGLSYDEY--RYTSVIKACQLeeDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 198 LDPLIrnhlQDELLE--LQKRL-NKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:TIGR01271 579 LDVVT----EKEIFEscLCKLMsNKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-265 |
1.90e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 25 DQGASRAEIKDLTNTvlGVHE-CSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEINVTTASsDEL 103
Cdd:PRK11288 252 PLGEVRLRLDGLKGP--GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD--GKPIDIRSPR-DAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 104 RyvrtrlVSMVF-----QQFGLFPWRTVADNI-----GFGLEVAGVPKKQRQAIIAEQLdLVGLN---EWANRMVTELSG 170
Cdd:PRK11288 327 R------AGIMLcpedrKAEGIIPVHSVADNInisarRHHLRAGCLINNRWEAENADRF-IRSLNiktPSREQLIMNLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 171 GMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRIlqcg 250
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI---- 474
|
250
....*....|....*
gi 1946638175 251 tAQEIVLTPANEHVA 265
Cdd:PRK11288 475 -AGELAREQATERQA 488
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-245 |
2.37e-13 |
|
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: 70.62 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGV---HECSLDIAEGETLVLMGLSGSGKSTLLRTINRlIKP---VEGNIYVgnAGKEINVTTASSDElry 105
Cdd:TIGR02633 3 EMKGIVKTFGGVkalDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPhgtWDGEIYW--SGSPLKASNIRDTE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 106 vrTRLVSMVFQQFGLFPWRTVADNIGFGLEV-------AGVPKKQRQAIIAEQLDLVGLNEwaNRMVTELSGGMQQRIGL 178
Cdd:TIGR02633 77 --RAGIVIIHQELTLVPELSVAENIFLGNEItlpggrmAYNAMYLRAKNLLRELQLDADNV--TRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 179 ARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
43-264 |
3.04e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagKEINVTTassdeLRYVRTRLVSMVFQQFGLFP 122
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD--EDISLLP-----LHARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEV-AGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK10895 92 RLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 202 -------IRNHLQDELLelqkrlnkTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpANEHV 264
Cdd:PRK10895 172 svidikrIIEHLRDSGL--------GVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL---QDEHV 230
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
47-275 |
3.30e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.30 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINVTTASSDELryvrtrlvsmvfqqfglfpwrTV 126
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL---------------------TG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHL 206
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 207 QDELLELqKRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEIVltpanEHVANFVRHINPLS 275
Cdd:PRK13545 183 LDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV-----DHYDEFLKKYNQMS 245
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-255 |
4.83e-13 |
|
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: 68.34 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 25 DQGASRAEIKDLTNTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvGNAGKeinvttassdelr 104
Cdd:cd03291 37 DNNLFFSNLCLVGAPVL--KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGR------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 yvrtrlVSMVFQQFGLFPwRTVADNIGFGleVAGVPKKQRQAIIAEQL--DLVGLNEWANRMVTE----LSGGMQQRIGL 178
Cdd:cd03291 100 ------ISFSSQFSWIMP-GTIKENIIFG--VSYDEYRYKSVVKACQLeeDITKFPEKDNTVLGEggitLSGGQRARISL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 179 ARAFATGAPVLLMDEPFSALDPLIRNHLQDELLeLQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:cd03291 171 ARAVYKDADLYLLDSPFGYLDVFTEKEIFESCV-CKLMANKTRILVTSKM-EHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
43-246 |
8.50e-13 |
|
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: 66.52 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKP---VEGNI-YVGNAGKEINVTTassdelryvrTRLVSMVFQQF 118
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIhYNGIPYKEFAEKY----------PGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 GLFPWRTVADNIGFGLEVAGvpkkqrqaiiaeqldlvglnewaNRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL 198
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1946638175 199 DPLIRNHLQDELLELQKRLNKTLIF-VSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-245 |
9.95e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGVH---ECSLDIAEGETLVLMGLSGSGKSTLLRTINRlIKP---VEGNIYVgnAGKEINVTTASSDElry 105
Cdd:NF040905 3 EMRGITKTFPGVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPhgsYEGEILF--DGEVCRFKDIRDSE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 106 vrTRLVSMVFQQFGLFPWRTVADNIGFGLEVA--GV---PKKQRQAiiAEQLDLVGLNEWANRMVTELSGGMQQRIGLAR 180
Cdd:NF040905 77 --ALGIVIIHQELALIPYLSIAENIFLGNERAkrGVidwNETNRRA--RELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 181 AFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-245 |
9.98e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLGV---HECSLDIAEGETLVLMGLSGSGKSTLLRTINRlIKPV---EGNIYVgnAGKEINVTTASSDElry 105
Cdd:PRK13549 7 EMKNITKTFGGVkalDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIF--EGEELQASNIRDTE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 106 vrTRLVSMVFQQFGLFPWRTVADNIGFGLEV--AGV---PKKQRQAiiAEQLDLVGLNEWANRMVTELSGGMQQRIGLAR 180
Cdd:PRK13549 81 --RAGIAIIHQELALVKELSVLENIFLGNEItpGGImdyDAMYLRA--QKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 181 AFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGR 245
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
47-246 |
1.33e-12 |
|
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: 68.67 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEinVTTASSDELRyvrtRLVSMVFQQFGLFPwrtv 126
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD--GQP--VTADNREAYR----QLFSAVFSDFHLFD---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 adnigfglEVAGVPKKQRQAIIAEQLDLVGLNE---WANRMV--TELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:COG4615 420 --------RLLGLDGEADPARARELLERLELDHkvsVEDGRFstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPE 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1946638175 202 IRNHLQDELL-ELqKRLNKTLIFVSHDlDEAIKMGNRIAIMEDGRI 246
Cdd:COG4615 492 FRRVFYTELLpEL-KARGKTVIAISHD-DRYFDLADRVLKMDYGKL 535
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
47-259 |
1.67e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.65 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvttaSSDELRYVRtRLVSMVFQQFGLFPwRTV 126
Cdd:PTZ00243 1330 SFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVN--GREI-----GAYGLRELR-RQFSMIPQDPVLFD-GTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAgvpkkqrQAIIAEQLDLVGLNEwanRMVTELSG--------------GMQQRIGLARA-FATGAPVLLM 191
Cdd:PTZ00243 1401 RQNVDPFLEAS-------SAEVWAALELVGLRE---RVASESEGidsrvleggsnysvGQRQLMCMARAlLKKGSGFILM 1470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 192 DEPFSALDPLIRNHLQDELLELQKrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFS--AYTVITIAHRL-HTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
47-256 |
2.55e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNiyvgnA---GKEINvttASSDELRyvrtRLVSMVFQQFGLFPW 123
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-----AwlfGQPVD---AGDIATR----RRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 RTVADNigfgLEV-A---GVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:NF033858 354 LTVRQN----LELhArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 200 PLIRNHLQDELLELQKRLNKTlIFVS-HDLDEAIKMgNRIAIMEDGRILQCGTAQEIV 256
Cdd:NF033858 430 PVARDMFWRLLIELSREDGVT-IFIStHFMNEAERC-DRISLMHAGRVLASDTPAALV 485
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
37-226 |
3.31e-12 |
|
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: 63.71 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 37 TNTVLgVHECSLDIAEGETLVLMGLSGSGKSTLLRTINrlikpvegniyvgnagkeinvttassdelryvrtrlvsmvfq 116
Cdd:cd03223 12 DGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALA------------------------------------------ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 117 qfGLFPWRTVADNIGFGLEVAGVPkkQR----QAIIAEQLdlvgLNEWANrmvtELSGGMQQRIGLARAFATGAPVLLMD 192
Cdd:cd03223 49 --GLWPWGSGRIGMPEGEDLLFLP--QRpylpLGTLREQL----IYPWDD----VLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 1946638175 193 EPFSALDPlirnHLQDELLELQKRLNKTLIFVSH 226
Cdd:cd03223 117 EATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
130-255 |
7.60e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 130 IGFGLEVAgvpKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDE 209
Cdd:NF000106 110 IGR*LDLS---RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1946638175 210 LLELQkRLNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:NF000106 187 VRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-255 |
7.43e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 29 SRAEIKDLTNTvlgvhecSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagkeINVTTAssdelrYVRT 108
Cdd:PLN03130 626 SKAERPTLSNI-------NLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------IRGTVA------YVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 rlVSMVFQQfglfpwrTVADNIGFGLEVAgvPKKQRQAI----IAEQLDLV---GLNEWANRMVTeLSGGMQQRIGLARA 181
Cdd:PLN03130 687 --VSWIFNA-------TVRDNILFGSPFD--PERYERAIdvtaLQHDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 182 FATGAPVLLMDEPFSALDPLIRNHLQDELL--ELQkrlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDKCIkdELR---GKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
48-238 |
1.03e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 48 LDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvgNAGKEINVTTASSDELRYVRTrlvsmvfqqfglfpwrTVA 127
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI---IYEQDLIVARLQQDPPRNVEG----------------TVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 128 DNIGFGL-EVAGVPKK---------------------QRQAI------------IAEQLDLVGLNewANRMVTELSGGMQ 173
Cdd:PRK11147 85 DFVAEGIeEQAEYLKRyhdishlvetdpseknlnelaKLQEQldhhnlwqlenrINEVLAQLGLD--PDAALSSLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 174 QRIGLARAFATGAPVLLMDEPfsaldpliRNHLQ----DELLELQKRLNKTLIFVSHDLDEAIKMGNRI 238
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEP--------TNHLDietiEWLEGFLKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-257 |
1.34e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLG---VHECSLDIAEGETLVLMGLSGSGKSTLLRTI--NRLIKPVEGNIYVgnagKEINVTTASSDElryv 106
Cdd:cd03217 2 EIKDLHVSVGGkeiLKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILF----KGEDITDLPPEE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRL-VSMVFQQfglfPwrtvadnigfgLEVAGVPkkqrqaiIAEQLdlvglnewanRMVTE-LSGGMQQRIGLARAFAT 184
Cdd:cd03217 74 RARLgIFLAFQY----P-----------PEIPGVK-------NADFL----------RYVNEgFSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 185 GAPVLLMDEPFSALDplIRN-HLQDELLELQKRLNKTLIFVSH--DLDEAIKmGNRIAIMEDGRILQCGTAqEIVL 257
Cdd:cd03217 122 EPDLAILDEPDSGLD--IDAlRLVAEVINKLREEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRIVKSGDK-ELAL 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
47-243 |
3.53e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAG--KEINvttassdeLRYVRTRlVSMVFQQFGLFPwR 124
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlKDIN--------LKWWRSK-IGVVSQDPLLFS-N 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 125 TVADNIGFGL---------------------------------------------------------------EVAGVPK 141
Cdd:PTZ00265 475 SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 142 KQR-----QAIIAEQLDLVGLNewanrmVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKR 216
Cdd:PTZ00265 555 KVLihdfvSALPDKYETLVGSN------ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628
|
250 260
....*....|....*....|....*..
gi 1946638175 217 LNKTLIFVSHDLdEAIKMGNRIAIMED 243
Cdd:PTZ00265 629 ENRITIIIAHRL-STIRYANTIFVLSN 654
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
47-255 |
3.81e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEgniyvgNAGKEINVTTASSDElryvrtrlVSMVFQQfglfpwrTV 126
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE------TSSVVIRGSVAYVPQ--------VSWIFNA-------TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 ADNIGFGLEVAgvPKKQRQAI----IAEQLDLVG---LNEWANRMVTeLSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:PLN03232 696 RENILFGSDFE--SERYWRAIdvtaLQHDLDLLPgrdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 200 PLIRNHLQDELLELQKRlNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PLN03232 773 AHVAHQVFDSCMKDELK-GKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-228 |
5.54e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 4 VIIDHVSVVFGNRRkqaldladqgasraeikdltntVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGN 83
Cdd:PRK09544 5 VSLENVSVSFGQRR----------------------VL--SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 84 IyvgnagkeinvttASSDELRyvrtrlVSMVFQQFGLFPwrTVADNIG-FGLEVAGVpkkqRQAIIAEQLDLVGLNEWAN 162
Cdd:PRK09544 61 I-------------KRNGKLR------IGYVPQKLYLDT--TLPLTVNrFLRLRPGT----KKEDILPALKRVQAGHLID 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 163 RMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDL 228
Cdd:PRK09544 116 APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
49-227 |
7.16e-10 |
|
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: 58.57 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 49 DIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKEINVTTASSDELRYVRTRLVSMVfQQFGLFP-WRTVa 127
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSSIT-KDFYTHPyFKTE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 128 dnigfglevagvpkkqrqaiIAEQLDLVGLNEwanRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQ 207
Cdd:cd03237 99 --------------------IAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180
....*....|....*....|
gi 1946638175 208 DELLELQKRLNKTLIFVSHD 227
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHD 175
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
47-255 |
8.37e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTIN--RLIKpvEGNIYVgnAGKEInvttASSDELRYVRTRLVSMVfQQFG--LFP 122
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEV--LGGDM----ADARHRRAVCPRIAYMP-QGLGknLYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLI 202
Cdd:NF033858 92 TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 203 RNH---LQDELleLQKRLNKTLIFVSHDLDEAIKMgNRIAIMEDGRILQCGTAQEI 255
Cdd:NF033858 172 RRQfweLIDRI--RAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
43-259 |
9.12e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagkeinvttassdelryvrTRLVSMVFQQfglfP 122
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA---------------------ERSIAYVPQQ----A 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 W---RTVADNIGFGLEVAgvPKKQRQAIIAEQL--DLV----GLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDE 193
Cdd:PTZ00243 731 WimnATVRGNILFFDEED--AARLADAVRVSQLeaDLAqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 194 PFSALDPLIRNHLQDELLeLQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEIVLTP 259
Cdd:PTZ00243 809 PLSALDAHVGERVVEECF-LGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
53-246 |
1.11e-09 |
|
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: 56.23 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 53 GETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNAGKeinvttassdelryvrtrlvsmvfqqfglfpwrtvadnigf 132
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGED----------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 133 glevagvpkkqrqaiIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDE--- 209
Cdd:smart00382 41 ---------------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 1946638175 210 --LLELQKRLNKTLIFVSHDLDEAIKMGnrIAIMEDGRI 246
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKDLGPAL--LRRRFDRRI 142
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
32-256 |
1.86e-09 |
|
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: 57.94 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLT-------NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKpVEGNIYVGNagkeINVTTASSDELR 104
Cdd:cd03289 4 TVKDLTakyteggNAVL--ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG----VSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 YVRTRLVSMVFQQFGLFP--------------WRtVADNIGFGLEVAGVPkkqrqaiiaEQLDLVGLNEWAnrmvtELSG 170
Cdd:cd03289 77 KAFGVIPQKVFIFSGTFRknldpygkwsdeeiWK-VAEEVGLKSVIEQFP---------GQLDFVLVDGGC-----VLSH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 171 GMQQRIGLARAFATGAPVLLMDEPFSALDPL----IRNHLQdellelQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGRI 246
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLDPItyqvIRKTLK------QAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
250
....*....|
gi 1946638175 247 LQCGTAQEIV 256
Cdd:cd03289 215 RQYDSIQKLL 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
43-201 |
2.61e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGniyvgnagkEINVTTASSDELRYVRTRLVSMVFQQFGLFP 122
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG---------EILFERQSIKKDLCTYQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 123 WRTVADNIGFGLEVAGVPKKqrqaiIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
47-244 |
4.94e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEINVTTA-SSDELRyvrtrlVSMVFQQFGLFPWRT 125
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY--LGKEVTFNGPkSSQEAG------IGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 126 VADNIGFGLEV----AGVPKKQRQAIIAEQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:PRK10762 96 IAENIFLGREFvnrfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1946638175 202 IRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDG 244
Cdd:PRK10762 176 ETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-227 |
1.23e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDLTNTVLG---VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnagkeinvttassdelryvrT 108
Cdd:PRK11147 321 EMENVNYQIDGkqlVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG--------------------T 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 109 RLVSMVFQQF--GLFPWRTVADNIGFG---LEVAGVPkkqRQAIIAEQlDLVGLNEWANRMVTELSGGMQQRIGLARAFA 183
Cdd:PRK11147 381 KLEVAYFDQHraELDPEKTVMDNLAEGkqeVMVNGRP---RHVLGYLQ-DFLFHPKRAMTPVKALSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1946638175 184 TGAPVLLMDEPfsaldpliRNHLQDELLELQKRL----NKTLIFVSHD 227
Cdd:PRK11147 457 KPSNLLILDEP--------TNDLDVETLELLEELldsyQGTVLLVSHD 496
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-246 |
1.31e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 25 DQGASRAEIKDLTNTvlGVHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnAGKEInVTTASSDELR 104
Cdd:PRK10762 252 APGEVRLKVDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL--DGHEV-VTRSPQDGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 105 YvrtrlvSMVFqqfglfpwrTVADNIGFGLeVAGVPKKQRQAIIA-EQL--DLVGLNEWANRMVTE-------------- 167
Cdd:PRK10762 327 N------GIVY---------ISEDRKRDGL-VLGMSVKENMSLTAlRYFsrAGGSLKHADEQQAVSdfirlfniktpsme 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 168 -----LSGGMQQRIGLARAFATGAPVLLMDEPFSALD--------PLIRNHLQDELlelqkrlnkTLIFVSHDLDEAIKM 234
Cdd:PRK10762 391 qaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgakkeiyQLINQFKAEGL---------SIILVSSEMPEVLGM 461
|
250
....*....|..
gi 1946638175 235 GNRIAIMEDGRI 246
Cdd:PRK10762 462 SDRILVMHEGRI 473
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
43-251 |
2.01e-08 |
|
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: 53.96 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIyvgnagkEINVTTASSDELRYVRTRLvSMVFQQFGLFP 122
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-------EIDGIDISTIPLEDLRSSL-TIIPQDPTLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNigfgLEVAGvpkKQRQAIIAEQLDLV--GLNewanrmvteLSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:cd03369 96 -GTIRSN----LDPFD---EYSDEEIYGALRVSegGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1946638175 201 LIRNHLQDELLELQKrlNKTLIFVSHDLDEAIKMgNRIAIMEDGRILQCGT 251
Cdd:cd03369 159 ATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
32-252 |
2.20e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 32 EIKDL---TNTVLGVHECSLDIAEGETLVLMGLSGSGKSTLLRTI--NRLIKPVEGNIYVgnagKEINVTTASSDElryv 106
Cdd:CHL00131 9 EIKNLhasVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILF----KGESILDLEPEE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 107 RTRL-VSMVFQqfglFPwrtvadnigfgLEVAGVP------------KKQRQ----------AIIAEQLDLVGLNE-WAN 162
Cdd:CHL00131 81 RAHLgIFLAFQ----YP-----------IEIPGVSnadflrlaynskRKFQGlpeldpleflEIINEKLKLVGMDPsFLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 163 RMVTE-LSGGMQQRIGLARAFATGAPVLLMDEPFSALDplIrnhlqDELLELQKRLN------KTLIFVSH--DLDEAIK 233
Cdd:CHL00131 146 RNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLD--I-----DALKIIAEGINklmtseNSIILITHyqRLLDYIK 218
|
250
....*....|....*....
gi 1946638175 234 mGNRIAIMEDGRILQCGTA 252
Cdd:CHL00131 219 -PDYVHVMQNGKIIKTGDA 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
88-256 |
3.43e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 88 NAGK----EINVTTASSDELRyvrtRLVSMVFQQFGLFPwRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVglNEWANR 163
Cdd:PTZ00265 1275 NSGKilldGVDICDYNLKDLR----NLFSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAIDEFI--ESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVT-------ELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLdEAIKMGN 236
Cdd:PTZ00265 1348 YDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSD 1426
|
170 180
....*....|....*....|....*
gi 1946638175 237 RIAIMED----GRILQC-GTAQEIV 256
Cdd:PTZ00265 1427 KIVVFNNpdrtGSFVQAhGTHEELL 1451
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
50-269 |
5.41e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 50 IAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGnaGKEInvttaSSDELRYVRTRLvSMVFQQFGLFpwrtvADN 129
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID--GIDI-----SKLPLHTLRSRL-SIILQDPILF-----SGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 130 IGFGL--EVAGVPKKQRQAIIAEQLDLV--GLNEWANRMVTE----LSGGMQQRIGLARAFATGAPVLLMDEPFSALDPL 201
Cdd:cd03288 111 IRFNLdpECKCTDDRLWEALEIAQLKNMvkSLPGGLDAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 202 IRNHLQDelLELQKRLNKTLIFVSHDLdEAIKMGNRIAIMEDGRILQCGTAQEIvLTPANEHVANFVR 269
Cdd:cd03288 191 TENILQK--VVMTAFADRTVVTIAHRV-STILDADLVLVLSRGILVECDTPENL-LAQEDGVFASLVR 254
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
43-256 |
7.63e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagKEINVTTASSDELRyvrtRLVSMVFQQFGLFP 122
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI----DDCDVAKFGLTDLR----RVLSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 wRTVADNIGFGLE--VAGVPKKQRQAIIAEQLDL--VGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSAL 198
Cdd:PLN03232 1324 -GTVRFNIDPFSEhnDADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 199 DPLIRNHLQDELLELQKRLnkTLIFVSHDLDEAIKMgNRIAIMEDGRILQCGTAQEIV 256
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSC--TMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
47-255 |
9.18e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRlikpvEGNIYVGNAGKEIN-VTTAS--------SDELRYVRTRLVSMVFQQ 117
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG-----ELPLLSGERQSQFShITRLSfeqlqklvSDEWQRNNTDMLSPGEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 118 FGlfpwRTVADNIgfgleVAGVPKKQRQAIIAEQLdlvGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:PRK10938 98 TG----RTTAEII-----QDEVKDPARCEQLAQQF---GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 198 LDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
50-254 |
1.37e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 50 IAEGETLVLMGLSGSGKSTLLrtiNRLIKPVEGNIYVGNAgkEINVTTASSDELRyvRTRLVSmvfQQFGLFPWRTVADN 129
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTI--LANNRKPTKQILK--RTGFVT---QDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 130 IGFgLEVAGVPK---KQRQAIIAEQ-LDLVGLNEWANRMVTE-----LSGGMQQRIGLARAFATGAPVLLMDEPFSALDP 200
Cdd:PLN03211 161 LVF-CSLLRLPKsltKQEKILVAESvISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 201 LIRNHLQDELLELQKRlNKTLIFVSHDLDEAI-KMGNRIAIMEDGRILQCGTAQE 254
Cdd:PLN03211 240 TAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
44-231 |
1.99e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTI---------NRL------------IKPVEGNI-YVgnagkeinvttASSD 101
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgrrrgsgetIWDIKKHIgYV-----------SSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 102 ELRY-----VRTRLVSMVFQQFGLFpwRTVADnigfglevagvpkkqRQAIIAEQ-LDLVGLNEW-ANRMVTELSGGmQQ 174
Cdd:PRK10938 346 HLDYrvstsVRNVILSGFFDSIGIY--QAVSD---------------RQQKLAQQwLDILGIDKRtADAPFHSLSWG-QQ 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1946638175 175 RIGL-ARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEA 231
Cdd:PRK10938 408 RLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-255 |
4.49e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.26 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 10 SVVFGNRRKQALDLADQG---------ASRAEIKDLT------NTVLgvHECSLDIAEGETLVLMGLSGSGKSTLLRTIN 74
Cdd:PRK10790 311 AVVAGERVFELMDGPRQQygnddrplqSGRIDIDNVSfayrddNLVL--QNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 75 RLIKPVEGNIYVGNAgkeiNVTTASSDELRyvrtRLVSMVfQQFGLFPWRTVADNIGFGLEVAgvpkkqrQAIIAEQLDL 154
Cdd:PRK10790 389 GYYPLTEGEIRLDGR----PLSSLSHSVLR----QGVAMV-QQDPVVLADTFLANVTLGRDIS-------EEQVWQALET 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 155 VGLNEWANRMV-----------TELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELqkRLNKTLIF 223
Cdd:PRK10790 453 VQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVV 530
|
250 260 270
....*....|....*....|....*....|..
gi 1946638175 224 VSHDLdEAIKMGNRIAIMEDGRILQCGTAQEI 255
Cdd:PRK10790 531 IAHRL-STIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-228 |
5.46e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 51 AEGETLVLMGLSGSGKSTLLRTINRLIKPvegNIyvGNAGKEINVTTASS----DELRYVRTRL------VSMVFQQFGL 120
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKP---NL--GKFDDPPDWDEILDefrgSELQNYFTKLlegdvkVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 121 FPwRTVADNIGFGLEvaGVPKKQRQAIIAEQLDLVGLNEwanRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD- 199
Cdd:cd03236 99 IP-KAVKGKVGELLK--KKDERGKLDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDi 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1946638175 200 -------PLIRNHLQDEllelqkrlnKTLIFVSHDL 228
Cdd:cd03236 173 kqrlnaaRLIRELAEDD---------NYVLVVEHDL 199
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
43-226 |
9.64e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.52 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTIN--------RLIKPVEGNIYvgnagkeinvttassdelrYVRTRlvsmv 114
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLF-------------------YVPQR----- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 115 fQQFGLfpwRTVADNIGFGLEVAGVPKKQ-RQAIIAEQLDLVGLNEWANRMVT---------ELSGGMQQRIGLARAFAT 184
Cdd:TIGR00954 524 -PYMTL---GTLRDQIIYPDSSEDMKRRGlSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1946638175 185 GAPVLLMDEPFSALDPlirnHLQDELLELQKRLNKTLIFVSH 226
Cdd:TIGR00954 600 KPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
47-235 |
1.43e-06 |
|
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: 47.70 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTInrlIKPVEGNIYVgnagkeinvttasSDELRYVRTRLVSMvfqqfglfpwrtv 126
Cdd:cd03238 15 DVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLI-------------SFLPKFSRNKLIFI------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 127 adnigfglevagvpkKQRQAIIAEQLDLVGLNewanRMVTELSGGMQQRIGLARAFATGAP--VLLMDEPFSALDPLIRN 204
Cdd:cd03238 66 ---------------DQLQFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 1946638175 205 HLQDELLELqKRLNKTLIFVSHDL------DEAIKMG 235
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHNLdvlssaDWIIDFG 162
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
60-199 |
1.51e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 60 GLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRYVRtrlvsmvfQQFGLFPWRTVADNIGFGLEVAGV 139
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKN----CNINNIAKPYCTYIG--------HNLGLKLEMTVFENLKFWSEIYNS 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 140 PKKQRQAIIAEQLDlvglnEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:PRK13541 101 AETLYAAIHYFKLH-----DLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
60-239 |
1.86e-06 |
|
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: 49.55 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 60 GLSGSGKSTLLRTINRLIKPVEGNIYVGNAgkeinVTTASSDELRYvrtrlvsmvfqqfGLFPWRTVADNIGFGLEVAGV 139
Cdd:TIGR03719 355 GPNGAGKSTLFRMITGQEQPDSGTIEIGET-----VKLAYVDQSRD-------------ALDPNKTVWEEISGGLDIIKL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 140 PKKQ---RQAII------AEQLDLVGlnewanrmvtELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDEL 210
Cdd:TIGR03719 417 GKREipsRAYVGrfnfkgSDQQKKVG----------QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL 486
|
170 180 190
....*....|....*....|....*....|..
gi 1946638175 211 LELQkrlnKTLIFVSHD---LDeaikmgnRIA 239
Cdd:TIGR03719 487 LNFA----GCAVVISHDrwfLD-------RIA 507
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
53-254 |
2.23e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 53 GETLVLMGLSGSGKSTLLRTInrlikpvEGNIYVGNAGKEINVT--TASSDELRYVRTRLVSMVFQQFGLFPWRTVADNI 130
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTI-------ASNTDGFHIGVEGVITydGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 131 GF-------GLEVAGVPKKQRQAIIAE-QLDLVGLN-----EWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSA 197
Cdd:TIGR00956 160 DFaarcktpQNRPDGVSREEYAKHIADvYMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946638175 198 LDP-----LIRnhlqdeLLELQKRLNKTLIFVS--HDLDEAIKMGNRIAIMEDGRILQCGTAQE 254
Cdd:TIGR00956 240 LDSataleFIR------ALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
43-260 |
5.16e-06 |
|
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: 47.90 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTI-NRLIKPVEGNIYVGnaGKEINVTTAssdeLRYVRTRlVSMV---FQQF 118
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFIN--GKPVDIRNP----AQAIRAG-IAMVpedRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 119 GLFPWRTVADNIgfglEVAGVPKKQRQAIIAEQLDLVGLNEWANRM----------VTELSGGMQQRIGLARAFATGAPV 188
Cdd:TIGR02633 349 GIVPILGVGKNI----TLSVLKSFCFKMRIDAAAELQIIGSAIQRLkvktaspflpIGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 189 LLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRI----LQCGTAQEIVLTPA 260
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLkgdfVNHALTQEQVLAAA 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
168-246 |
5.66e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 5.66e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946638175 168 LSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
47-250 |
8.60e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLlrtinrlikpVEGNIYVgnAGKEINVTTASSdelrYVRTRLVSM----VFQQFGLFP 122
Cdd:cd03270 15 DVDIPRNKLVVITGVSGSGKSSL----------AFDTIYA--EGQRRYVESLSA----YARQFLGQMdkpdVDSIEGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 123 -----WRTVADN----IG--------FGLEVAGVPKKQRqaiiAEQLDLVGLNEWA-NRMVTELSGGMQQRIGLARAFAT 184
Cdd:cd03270 79 aiaidQKTTSRNprstVGtvteiydyLRLLFARVGIRER----LGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 185 GAPVLL--MDEPFSALDPliRNHlqDELLELQKRLNK---TLIFVSHDLDeAIKMGNRI------AIMEDGRILQCG 250
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHP--RDN--DRLIETLKRLRDlgnTVLVVEHDED-TIRAADHVidigpgAGVHGGEIVAQG 226
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
164-229 |
9.21e-06 |
|
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: 45.43 E-value: 9.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 164 MVTELSGGMQQRIGLARAFA----TGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNkTLIFVSHDLD 229
Cdd:cd03227 74 TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGA-QVIVITHLPE 142
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
43-226 |
1.29e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTI----------NRLIKPVEGNIyVGNAGKEINVTTASSDElryvRTRL-- 110
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkNCQILHVEQEV-VGDDTTALQCVLNTDIE----RTQLle 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 111 --VSMVFQQFGL-FPWRTVADNIGFGLEVAGVPKKQRQAIIAEQLDLV--------------GLN---EWANRMVTELSG 170
Cdd:PLN03073 268 eeAQLVAQQRELeFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIdaytaearaasilaGLSftpEMQVKATKTFSG 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 171 GMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLelqkRLNKTLIFVSH 226
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
58-231 |
1.32e-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: 46.85 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 58 LMGLSGSGKSTLLRTINRLIKPVEGniyvgnagkeinvttassdELRYVRTRLVSMVFQQFGLFPWRTVADNIGFGL--- 134
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNG-------------------EARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVaei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 135 --------EVA---GVPKKQRQAIIAEQ------LDLVGLNEWANRM---------------VTELSGGMQQRIGLARAF 182
Cdd:TIGR03719 97 kdaldrfnEISakyAEPDADFDKLAAEQaelqeiIDAADAWDLDSQLeiamdalrcppwdadVTKLSGGERRRVALCRLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 183 ATGAPVLLMDEPfsaldpliRNHLQDELLE-LQKRLNK---TLIFVSHD---LDEA 231
Cdd:TIGR03719 177 LSKPDMLLLDEP--------TNHLDAESVAwLERHLQEypgTVVAVTHDryfLDNV 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
43-260 |
2.27e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.08 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLLRTI-----NRLikpvEGNIYVgnAGKEINVTTaSSDELRYVrtrlVSMV--- 114
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGRW----EGEIFI--DGKPVKIRN-PQQAIAQG----IAMVped 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 115 FQQFGLFPWRTVADNIgfglEVAGVPKKQRQAIIAEQLDLVGLNEWANRM----------VTELSGGMQQRIGLARAFAT 184
Cdd:PRK13549 347 RKRDGIVPVMGVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRLkvktaspelaIARLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 185 GAPVLLMDEPFSALDPLIRNHLQDELLELQKRlNKTLIFVSHDLDEAIKMGNRIAIMEDGRI----LQCGTAQEIVLTPA 260
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLkgdlINHNLTQEQVMEAA 501
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-265 |
2.73e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 44 HECSLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVgnagKEINVTTASSDELRYVrtrlVSMVFQQFGLFpw 123
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI----DGCDISKFGLMDLRKV----LGIIPQAPVLF-- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 124 rtvADNIGFGLEvagvP-KKQRQAIIAEQLDLVGLNEWANR-------MVTE----LSGGMQQRIGLARAFATGAPVLLM 191
Cdd:PLN03130 1326 ---SGTVRFNLD----PfNEHNDADLWESLERAHLKDVIRRnslgldaEVSEagenFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 192 DEPFSAL----DPLIRNHLQDE-----LLELQKRLNkTLIfvshDLDeaikmgnRIAIMEDGRILQCGTAQEIVltpANE 262
Cdd:PLN03130 1399 DEATAAVdvrtDALIQKTIREEfksctMLIIAHRLN-TII----DCD-------RILVLDAGRVVEFDTPENLL---SNE 1463
|
...
gi 1946638175 263 HVA 265
Cdd:PLN03130 1464 GSA 1466
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
47-256 |
2.79e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.09 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYVGNagkeINVTTASSDELRYVRTRLVS--MVFQ---QFGLF 121
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----LNIAKIGLHDLRFKITIIPQdpVLFSgslRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 122 PWRTVAD-NIGFGLEVAGVpkkqrQAIIAEQLDlvGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD- 199
Cdd:TIGR00957 1382 PFSQYSDeEVWWALELAHL-----KTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDl 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946638175 200 -------PLIRNHLQD-ELLELQKRLNKTLIFvshdldeaikmgNRIAIMEDGRILQCGTAQEIV 256
Cdd:TIGR00957 1455 etdnliqSTIRTQFEDcTVLTIAHRLNTIMDY------------TRVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
47-227 |
4.53e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 47 SLDIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEG------NIYVG--------NAGKEINV-------TTASSDELRy 105
Cdd:PRK15064 339 NLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGtvkwseNANIGyyaqdhayDFENDLTLfdwmsqwRQEGDDEQA- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 106 VRTRLVSMVFQQfglfpwrtvaDNIgfglevagvpkkqrqaiiaeqldlvglnewaNRMVTELSGGMQQRIGLARAFATG 185
Cdd:PRK15064 418 VRGTLGRLLFSQ----------DDI-------------------------------KKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1946638175 186 APVLLMDEPfsaldpliRNHLQDELLE-LQKRLNK---TLIFVSHD 227
Cdd:PRK15064 457 PNVLVMDEP--------TNHMDMESIEsLNMALEKyegTLIFVSHD 494
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
49-199 |
4.74e-05 |
|
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: 45.16 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 49 DIAEGETLVLMGLSGSGKSTLLRTINRLIKPVEGNIYvgnagKEINVT------TASSDELryVRTRLVSMVFQQFGLFP 122
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-----EDLKISykpqyiSPDYDGT--VEEFLRSANTDDFGSSY 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 123 WRTVadnigfglevagvpkkqrqaiIAEQLdlvGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD 199
Cdd:COG1245 435 YKTE---------------------IIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
167-242 |
6.49e-05 |
|
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: 42.94 E-value: 6.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 167 ELSGGMQQRIGLARAFATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNKTLIFVSHDLDEAIKMGNRIAIME 242
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
148-228 |
6.74e-05 |
|
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: 44.78 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 148 IAEQLdlvGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD--------PLIRnhlqdELLElqkrLNK 219
Cdd:COG1245 196 LAEKL---GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlnvaRLIR-----ELAE----EGK 263
|
....*....
gi 1946638175 220 TLIFVSHDL 228
Cdd:COG1245 264 YVLVVEHDL 272
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
150-228 |
7.62e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 150 EQLDLVGLNEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPFSALD--------PLIRnhlqdELLElqkrlNKTL 221
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrlnvaRLIR-----ELAE-----GKYV 264
|
....*..
gi 1946638175 222 IFVSHDL 228
Cdd:PRK13409 265 LVVEHDL 271
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
158-229 |
1.11e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 1.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 158 NEWANRMVTELSGGMQQRIGLARAFATGAPVLLMDEPfsaldpliRNHLQ-DELLELQKRLNK---TLIFVSHDLD 229
Cdd:PRK10636 140 NEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP--------TNHLDlDAVIWLEKWLKSyqgTLILISHDRD 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
163-227 |
1.21e-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: 42.59 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 163 RMVTELSGGmQQ-------RIGLARAFATGAPVLLMDEPFSALDP-LIRNHLQDELLELQKRLNKTLIFVSHD 227
Cdd:cd03240 111 DMRGRCSGG-EKvlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-255 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 144 RQAIIAEQ-----------LDLVGLNEWA-NRMVTELSGGMQQRIGLARAFATG-APVL-LMDEPFSALdplirnHLQD- 208
Cdd:TIGR00630 453 EEKKIAEEvlkeirerlgfLIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGL------HQRDn 526
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 209 -ELLELQKRLNK---TLIFVSHDlDEAIKMGNRI------AIMEDGRILQCGTAQEI 255
Cdd:TIGR00630 527 rRLINTLKRLRDlgnTLIVVEHD-EDTIRAADYVidigpgAGEHGGEVVASGTPEEI 582
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
43-246 |
2.14e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 43 VHECSLDIAEGETLVLMGLSGSGKSTLL-----RTINRLIKpveGNIYVGnaGKEI---NVTTASSDELRYV---Rtrlv 111
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgRSYGRNIS---GTVFKD--GKEVdvsTVSDAIDAGLAYVtedR---- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 112 smvfQQFGLfpwrTVADNIGFGLEVAGVPKKQRQAIIAEQLDLVGLNEWANRM----------VTELSGGMQQRIGLARA 181
Cdd:NF040905 347 ----KGYGL----NLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMniktpsvfqkVGNLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946638175 182 FATGAPVLLMDEPFSALDP-------LIRNHLQDEllelqkrlNKTLIFVSHDLDEAIKMGNRIAIMEDGRI 246
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVgakyeiyTIINELAAE--------GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
166-228 |
7.76e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 7.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 166 TELSGGMQQRIGLA---RAFATGAPVLLMDEPFSALDPLIRNHLQdELLELQKRLNKTLIFVSHDL 228
Cdd:pfam13304 235 FELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKLLRRLL-ELLKELSRNGAQLILTTHSP 299
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
301-345 |
1.13e-03 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 38.31 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1946638175 301 PDTSLPDLISVCDRKN-GAIGV-AEDGRVIGVITEEDIIHHLAEHQK 345
Cdd:COG0517 16 PDATVREALELMSEKRiGGLPVvDEDGKLVGIVTDRDLRRALAAEGK 62
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
166-229 |
1.15e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 1.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946638175 166 TELSGGMQQRIGLARAF---ATGAPVLLMDEPFSALDPLIRNHLQDELLELQKRLNkTLIFVSHDLD 229
Cdd:cd03271 168 TTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLD 233
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
162-270 |
1.25e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 162 NRMVTELSGGMQQRIGLARAFatGAPVL----LMDEPFSALDPLIRNHLQDELLELQKRLNkTLIFVSHD------LDEA 231
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDeqmislADRI 547
|
90 100 110
....*....|....*....|....*....|....*....
gi 1946638175 232 IKMGNRIAIMeDGRILQCGTAQEIvLTPANEHVANFVRH 270
Cdd:PRK00635 548 IDIGPGAGIF-GGEVLFNGSPREF-LAKSDSLTAKYLRQ 584
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
57-228 |
1.59e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 57 VLMGLSGSGKSTLLRTI--------NRLIKPVEGNIYVGNAGKEINVtTASSDELRYVRTRLVSMvFQQFGLFPWRTVAD 128
Cdd:COG0419 27 LIVGPNGAGKSTILEAIryalygkaRSRSKLRSDLINVGSEEASVEL-EFEHGGKRYRIERRQGE-FAEFLEAKPSERKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946638175 129 NIG--FGLEV-------AGVPKKQRQAIIAEQLDLVGLNEWANRMVTE------LSGGMQQRIGLARAFAtgapvLLMDe 193
Cdd:COG0419 105 ALKrlLGLEIyeelkerLKELEEALESALEELAELQKLKQEILAQLSGldpietLSGGERLRLALADLLS-----LILD- 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1946638175 194 pFSALDPLIRNHLQDELLELQkrlnktliFVSHDL 228
Cdd:COG0419 179 -FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| CBS_pair_bac_euk |
cd04623 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
301-343 |
1.70e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 37.78 E-value: 1.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1946638175 301 PDTSLPDLISVCDRKN-GAIGVAED-GRVIGVITEEDIIHHLAEH 343
Cdd:cd04623 9 PDATVAEALRLLAEKNiGALVVVDDgGRLVGILSERDYVRKLALR 53
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
22-77 |
2.11e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 2.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946638175 22 DLADQGASRAEIKDLTNTVLGVHECS----------LDIAEGETLVLMGLSGSGKSTLlrtINRLI 77
Cdd:cd01854 44 DLVDDEELEELLEIYEKLGYPVLAVSaktgegldelRELLKGKTSVLVGQSGVGKSTL---LNALL 106
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
165-229 |
2.20e-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: 40.00 E-value: 2.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946638175 165 VTELSGGMQQRIGLARAF---ATGAPVLLMDEPFSALdplirnHLQD--ELLELQKRLNK---TLIFVSHDLD 229
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL------HFDDikKLLEVLQRLVDkgnTVVVIEHNLD 893
|
|
| CBS_pair_BON_assoc |
cd04586 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
299-343 |
3.07e-03 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 37.41 E-value: 3.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1946638175 299 AKPDTSLPDLISV-CDRK-NGAIGVAEDGRVIGVITEEDIIHHLAEH 343
Cdd:cd04586 8 VTPDTSVREAARLlLEHRiSGLPVVDDDGKLVGIVSEGDLLRREEPG 54
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
300-342 |
3.42e-03 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 38.33 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1946638175 300 KPDTSLPDLISVCDRKN-GAIGVAEDGRVIGVITEEDIIHHLAE 342
Cdd:COG2524 100 SPDTTLEEALELMLEKGiSGLPVVDDGKLVGIITERDLLKALAE 143
|
|
| |
