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Conserved domains on  [gi|493864995|ref|WP_006811701|]
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MULTISPECIES: glycine betaine/L-proline ABC transporter ATP-binding protein ProV [Enterobacter]

Protein Classification

glycine betaine/L-proline ABC transporter ATP-binding protein( domain architecture ID 11484565)

ABC transporter ATP-binding protein involved in uptake of osmoprotectant glycine betaine/L-proline, thereby allowing bacterial growth in a high-osmolarity environment; contains a CBS-pair domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1-400 0e+00

proline/glycine betaine ABC transporter ATP-binding protein ProV;


:

Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 743.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK10070   1 MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHA 160
Cdd:PRK10070  81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISHVFSAKDIARRTPNGIIRKTPGFGPRSALKLLQDEDREYGYLVERGNKF 320
Cdd:PRK10070 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 321 VGVVSIDSLKTALSENQGIDAALIDAPLAVDAETPLSELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALDREGTNNG 400
Cdd:PRK10070 321 VGAVSIDSLKTALTQQQGLDAALIDAPLAVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALDREGVNNG 400
 
Name Accession Description Interval E-value
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1-400 0e+00

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 743.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK10070   1 MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHA 160
Cdd:PRK10070  81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISHVFSAKDIARRTPNGIIRKTPGFGPRSALKLLQDEDREYGYLVERGNKF 320
Cdd:PRK10070 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 321 VGVVSIDSLKTALSENQGIDAALIDAPLAVDAETPLSELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALDREGTNNG 400
Cdd:PRK10070 321 VGAVSIDSLKTALTQQQGLDAALIDAPLAVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALDREGVNNG 400
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
3-393 0e+00

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 666.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   3 IKLEVKNLYKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:COG4175    2 PKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  83 GQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYP 162
Cdd:COG4175   82 GEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:COG4175  162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 243 VVQVGTPDEILNNPANDYVRTFFRGVDISHVFSAKDIARRTPNGIIRKTpgfGPRSALKLLQDEDREYGYLVERGNKFVG 322
Cdd:COG4175  242 IVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKD---GPRVALRRMREEGISSLYVVDRDRRLLG 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 323 VVSIDSLKTALSENQGIDAALIDAPLAVDAETPLSELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALD 393
Cdd:COG4175  319 VVTADDALEAVKGEKDLEEILLTDVPTVSPDTPLRDLLPLVAESPYPLAVVDEDGRLLGVISRGSLLAALA 389
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
36-396 0e+00

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: 576.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSF 115
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  116 ALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISHVFS 275
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  276 AKDIARRTPNGIIRKTPGFGPRSALKLLQDEDREYGYLVERGNKFVGVVSIDSLKTALSENQGIDAALIDAPLAVDAETP 355
Cdd:TIGR01186 241 AERIAQRMNTGPITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKKAQGLQDVLIDDIYTVDAGTL 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 493864995  356 LSELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALD--REG 396
Cdd:TIGR01186 321 LRETVRKVLKAGIKVPVVDEDQRLVGIVTRGSLVDALYdsREG 363
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
5-273 0e+00

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: 511.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03294    1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03294   81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03294  161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
                        250       260
                 ....*....|....*....|....*....
gi 493864995 245 QVGTPDEILNNPANDYVRTFFRGVDISHV 273
Cdd:cd03294  241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
7-265 3.84e-60

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 198.68  E-value: 3.84e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   7 VKNLYKIFGehpqrafkyieKGLTKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL 86
Cdd:NF040933   5 VENVTKIFK-----------KGKKEVVAL---------DNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIY 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  87 IDGVDIARISDAELrEVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELS 166
Cdd:NF040933  65 FDDKLVASPGKIIV-PPEDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 167 GGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEMQDELVK-LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:NF040933 144 GGQQQRVALARALVKNPQVLLLDEPFSNLDARIR-DSARALVKkIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQ 222
                        250       260
                 ....*....|....*....|
gi 493864995 246 VGTPDEILNNPANDYVRTFF 265
Cdd:NF040933 223 VGKPEEIYDNPANIFVARLI 242
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
44-193 1.40e-45

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: 153.96  E-value: 1.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995  124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAH----AYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:pfam00005  77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
44-252 9.67e-29

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 118.69  E-value: 9.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIarisDAELREVRRKKIAMVfQSFALMPHMTV 123
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIATRRRVGYMS-QAFSLYGELTV 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493864995 204 QDELVKLQAKHQRTIvFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF033858 437 WRLLIELSREDGVTI-FIStHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
44-238 1.16e-23

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 96.92  E-value: 1.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiarisdaelREVRRKKIAMVFQSFAL---MPh 120
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVpdsLP- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 MTVLDNTAFG----MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:NF040873  72 LTVRDLVAMGrwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493864995 197 PLIRTEMqDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIM 238
Cdd:NF040873 152 AESRERI-IALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
43-245 6.59e-13

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.82  E-value: 6.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGvDIARISDaeLREVRRKKIAMVFQSFA 116
Cdd:NF040905  13 GVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDG-EVCRFKD--IRDSEALGIVIIHQELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 117 LMPHMTVLDNTAFGMELAGTPA---QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:NF040905  89 LIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493864995 194 ALDPLIRTEMQDELVKLQAkHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:NF040905 169 ALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
46-253 1.61e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 65.92  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEptRGQVLIDGVDIArisDAELREVRRKKIAMVFQSFA--LMPHM 121
Cdd:NF033858  19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMA---DARHRRAVCPRIAYMPQGLGknLYPTL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGTPAQERQEKALDALRQVGLenyaHAYPD----ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:NF033858  94 SVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 198 LIRTEMQDELVKLQAKHQRTIVFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:NF033858 170 LSRRQFWELIDRIRAERPGMSVLVAtAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
139-252 1.12e-09

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 59.36  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 139 QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDElVKLQAKHQRTI 218
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATV 197
                         90       100       110
                 ....*....|....*....|....*....|....
gi 493864995 219 VFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
54-237 3.63e-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: 55.07  E-value: 3.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaelrevrrkkiamvfqsfalmphmtvldntafgmel 133
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL--------------------------------------- 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   134 agtpaqerqekalDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTEMQDELV 208
Cdd:smart00382  43 -------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLL 109
                          170       180
                   ....*....|....*....|....*....
gi 493864995   209 KLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
 
Name Accession Description Interval E-value
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1-400 0e+00

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 743.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK10070   1 MAIKLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHA 160
Cdd:PRK10070  81 TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISHVFSAKDIARRTPNGIIRKTPGFGPRSALKLLQDEDREYGYLVERGNKF 320
Cdd:PRK10070 241 GEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTPGFGPRSALKLLQDEDREYGYVIERGNKF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 321 VGVVSIDSLKTALSENQGIDAALIDAPLAVDAETPLSELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALDREGTNNG 400
Cdd:PRK10070 321 VGAVSIDSLKTALTQQQGLDAALIDAPLAVDAQTPLSELLSHVGQAPCAVPVVDEDQQYVGIISKGMLLRALDREGVNNG 400
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
3-393 0e+00

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 666.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   3 IKLEVKNLYKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:COG4175    2 PKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  83 GQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYP 162
Cdd:COG4175   82 GEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 163 DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:COG4175  162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 243 VVQVGTPDEILNNPANDYVRTFFRGVDISHVFSAKDIARRTPNGIIRKTpgfGPRSALKLLQDEDREYGYLVERGNKFVG 322
Cdd:COG4175  242 IVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKD---GPRVALRRMREEGISSLYVVDRDRRLLG 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 323 VVSIDSLKTALSENQGIDAALIDAPLAVDAETPLSELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALD 393
Cdd:COG4175  319 VVTADDALEAVKGEKDLEEILLTDVPTVSPDTPLRDLLPLVAESPYPLAVVDEDGRLLGVISRGSLLAALA 389
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
36-396 0e+00

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: 576.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSF 115
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  116 ALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISHVFS 275
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  276 AKDIARRTPNGIIRKTPGFGPRSALKLLQDEDREYGYLVERGNKFVGVVSIDSLKTALSENQGIDAALIDAPLAVDAETP 355
Cdd:TIGR01186 241 AERIAQRMNTGPITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKKAQGLQDVLIDDIYTVDAGTL 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 493864995  356 LSELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALD--REG 396
Cdd:TIGR01186 321 LRETVRKVLKAGIKVPVVDEDQRLVGIVTRGSLVDALYdsREG 363
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
5-273 0e+00

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: 511.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03294    1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03294   81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03294  161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
                        250       260
                 ....*....|....*....|....*....
gi 493864995 245 QVGTPDEILNNPANDYVRTFFRGVDISHV 273
Cdd:cd03294  241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-265 1.94e-100

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 302.40  E-value: 1.94e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG3842    2 AMPALELENVSKRYGDVT------------------------ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISdAELREvrrkkIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHA 160
Cdd:COG3842   58 DSGRILLDGRDVTGLP-PEKRN-----VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG3842  132 YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND 211
                        250       260
                 ....*....|....*....|....*
gi 493864995 241 GEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:COG3842  212 GRIEQVGTPEEIYERPATRFVADFI 236
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
44-265 6.53e-99

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: 294.21  E-value: 6.53e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFALMPHMTV 123
Cdd:cd03295   17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR----RKIGYVIQQIGLFPHMTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLE--NYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:cd03295   93 EENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:cd03295  173 QLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
5-247 1.68e-95

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: 284.41  E-value: 1.68e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03259    1 LELKGLSKTYGSVR------------------------ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaelREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03259   57 ILIDGRDVTG------VPPERRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03259  131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210

                 ...
gi 493864995 245 QVG 247
Cdd:cd03259  211 QVG 213
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-265 7.16e-95

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 288.12  E-value: 7.16e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAiKLEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG3839    1 MA-SLELENVSKSYGGVE------------------------ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDP 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARIsdaelrEVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHA 160
Cdd:COG3839   56 TSGEILIGGRDVTDL------PPKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDR 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG3839  130 KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
                        250       260
                 ....*....|....*....|....*
gi 493864995 241 GEVVQVGTPDEILNNPANDYVRTFF 265
Cdd:COG3839  210 GRIQQVGTPEELYDRPANLFVAGFI 234
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-249 3.55e-91

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 275.04  E-value: 3.55e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPQRAfkyiekgltkeQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1116    4 AAPALELRGVSKRFPTGGGGV-----------TALD---------DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKP 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISDaelrevrrkKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHA 160
Cdd:COG1116   64 TSGEVLVDGKPVTGPGP---------DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG1116  135 YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA 214
                        250
                 ....*....|....
gi 493864995 241 G-----EVVQVGTP 249
Cdd:COG1116  215 RpgrivEEIDVDLP 228
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
5-246 3.58e-90

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: 271.27  E-value: 3.58e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGeHPQRAFKyiekgltkeqILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03293    1 LEVRNVSKTYG-GGGGAVT----------ALE---------DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaelrevRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03293   61 VLVDGEPVTG---------PGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQ 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN--GE 242
Cdd:cd03293  132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGR 211

                 ....
gi 493864995 243 VVQV 246
Cdd:cd03293  212 IVAE 215
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1-265 6.77e-89

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: 268.77  E-value: 6.77e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPqrafkyiekgltkeqILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1127    2 SEPMIEVRNLTKSFGDRV---------------VL---------DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGM-ELAGTPAQERQEKALDALRQVGLENYAH 159
Cdd:COG1127   58 DSGEILVDGQDITGLSEKELYELRRR-IGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAAD 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 160 AYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:COG1127  137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIrELRDELGLTSVVVTHDLDSAFAIADRVAVL 215
                        250       260
                 ....*....|....*....|....*..
gi 493864995 239 QNGEVVQVGTPDEILNNPaNDYVRTFF 265
Cdd:COG1127  216 ADGKIIAEGTPEELLASD-DPWVRQFL 241
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
5-268 3.44e-86

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 265.40  E-value: 3.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFgEHPQRAFKyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1135    2 IELENLSKTF-PTKGGPVT-------------------ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:COG1135   62 VLVDGVDLTALSERELRAARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:COG1135  141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
                        250       260
                 ....*....|....*....|....
gi 493864995 245 QVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1135  221 EQGPVLDVFANPQSELTRRFLPTV 244
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
5-263 9.66e-84

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: 264.46  E-value: 9.66e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPQRAFKyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1123  261 LEVRNLSKRYPVRGKGGVR-------------------AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKkIAMVFQ--SFALMPHMTVLDNTAFGMELAGT-PAQERQEKALDALRQVGL-ENYAHA 160
Cdd:COG1123  322 ILFDGKDLTKLSRRSLRELRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADR 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:COG1123  401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
                        250       260
                 ....*....|....*....|...
gi 493864995 241 GEVVQVGTPDEILNNPANDYVRT 263
Cdd:COG1123  481 GRIVEDGPTEEVFANPQHPYTRA 503
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
44-287 9.71e-84

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 259.31  E-value: 9.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARIsdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:COG1118   18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-----LPPRERRVGFVFQHYALFPHMTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:COG1118   93 AENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV------RTFFRGVDISHVFSAK 277
Cdd:COG1118  173 RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVarflgcVNVLRGRVIGGQLEAD 252
                        250
                 ....*....|
gi 493864995 278 DIARRTPNGI 287
Cdd:COG1118  253 GLTLPVAEPL 262
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
32-264 2.55e-82

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: 251.77  E-value: 2.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaelreVRRKKIAMV 111
Cdd:cd03300    4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP------PHKRPVNTV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 112 FQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:cd03300   78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03300  158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
5-268 5.99e-82

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 250.68  E-value: 5.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1126    2 IEIENLHKSFGDL---------------EVL---------KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIArISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFG-MELAGTPAQERQEKALDALRQVGLENYAHAYPD 163
Cdd:COG1126   58 ITVDGEDLT-DSKKDINKLRRK-VGMVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDE----LVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:COG1126  136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEvldvMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMD 210
                        250       260
                 ....*....|....*....|....*....
gi 493864995 240 NGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1126  211 GGRIVEEGPPEEFFENPQHERTRAFLSKV 239
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
5-256 8.92e-80

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: 245.18  E-value: 8.92e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPQRAfkyiekgltkeqilektglsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03258    2 IELKNVSKVFGDTGGKV--------------------TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03258   62 VLVDGTDLTLLSGKELRKARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03258  141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
                        250
                 ....*....|..
gi 493864995 245 QVGTPDEILNNP 256
Cdd:cd03258  221 EEGTVEEVFANP 232
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
5-264 1.09e-79

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: 245.10  E-value: 1.09e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03261    1 IELRGLTKSFGGR---------------TVL---------KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGM-ELAGTPAQERQEKALDALRQVGLENYAHAYPD 163
Cdd:cd03261   57 VLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03261  136 ELSGGMKKRVALARALALDPELLLYDEPTAGLDP-IASGVIDDLIrSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
                        250       260
                 ....*....|....*....|..
gi 493864995 243 VVQVGTPDEILNNPaNDYVRTF 264
Cdd:cd03261  215 IVAEGTPEELRASD-DPLVRQF 235
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
5-243 4.30e-75

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: 232.38  E-value: 4.30e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEhpqrafkyiekGLTKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03255    1 IELKNLSKTYGG-----------GGEKVQAL---------KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03255   61 VRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEV 243
Cdd:cd03255  141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-244 6.79e-75

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 232.24  E-value: 6.79e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEhpqrafkyiekGLTKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1136    1 MSPLLELRNLTKSYGT-----------GEGEVTAL---------RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRP 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHA 160
Cdd:COG1136   61 TSGEVLIDGQDISSLSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDH 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQN 240
Cdd:COG1136  141 RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRD 219

                 ....
gi 493864995 241 GEVV 244
Cdd:COG1136  220 GRIV 223
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
5-247 2.03e-74

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: 230.60  E-value: 2.03e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03301    1 VELENVTKRFGNVT------------------------ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAElrevrrKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03301   57 IYIGGRDVTDLPPKD------RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03301  131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210

                 ...
gi 493864995 245 QVG 247
Cdd:cd03301  211 QIG 213
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
5-242 2.79e-74

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: 229.00  E-value: 2.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHpqrafkyiekgltkeqilektglsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03229    1 LELKNVSKRYGQK------------------------TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDaeLREVRRKKIAMVFQSFALMPHMTVLDNTAFGmelagtpaqerqekaldalrqvglenyahaypde 164
Cdd:cd03229   57 ILIDGEDLTDLED--ELPPLRRRIGMVFQDFALFPHLTVLENIALG---------------------------------- 100
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03229  101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
43-289 6.24e-73

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 231.23  E-value: 6.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMT 122
Cdd:PRK11153  20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ-IGMIFQHFNLLSSRT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 123 VLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtE 202
Cdd:PRK11153  99 VFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP----A 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 203 MQDELVKLQAKHQR----TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR---GVDISHVFS 275
Cdd:PRK11153 175 TTRSILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQstlHLDLPEDYL 254
                        250
                 ....*....|....*.
gi 493864995 276 AKDIARRTPNG--IIR 289
Cdd:PRK11153 255 ARLQAEPTTGSgpLLR 270
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
44-256 5.18e-72

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: 224.90  E-value: 5.18e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdAELREVRRKkIAMVFQS-----FAlm 118
Cdd:COG1122   17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRK-VGLVFQNpddqlFA-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 phMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG1122   91 --PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 199 IRTEMQDELVKLQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:COG1122  169 GRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
5-257 6.57e-71

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: 225.32  E-value: 6.57e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFgehpqrafkYIEKGLTKeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---T 81
Cdd:COG0444    2 LEVRNLKVYF---------PTRRGVVK-----------AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiT 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  82 RGQVLIDGVDIARISDAELREVRRKKIAMVFQSF--ALMPHMTVLDNTAFGMEL-AGTPAQERQEKALDALRQVGL---E 155
Cdd:COG0444   62 SGEILFDGEDLLKLSEKELRKIRGREIQMIFQDPmtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpE 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 156 NYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:COG0444  142 RRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRV 221
                        250       260
                 ....*....|....*....|..
gi 493864995 236 AIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0444  222 AVMYAGRIVEEGPVEELFENPR 243
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
5-254 6.72e-71

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 222.25  E-value: 6.72e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1131    1 IEVRGLTKRYGDKT------------------------ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:COG1131   57 VRVLGEDVAR----DPAEVRRR-IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGT 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:COG1131  132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
                        250
                 ....*....|
gi 493864995 245 QVGTPDEILN 254
Cdd:COG1131  211 ADGTPDELKA 220
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
5-247 3.23e-70

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: 220.46  E-value: 3.23e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEH--PQRAfkyiekgltkeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:cd03257    2 LEVKNLSVSFPTGggSVKA----------------------LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  83 GQVLIDGVDIARISDaELREVRRKKIAMVFQ--SFALMPHMTVLDNTAFGMELAG--TPAQERQEKALDALRQVGL-ENY 157
Cdd:cd03257   60 GSIIFDGKDLLKLSR-RLRKIRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEV 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 158 AHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:cd03257  139 LNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
                        250
                 ....*....|
gi 493864995 238 MQNGEVVQVG 247
Cdd:cd03257  219 MYAGKIVEEG 228
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1-264 5.29e-70

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: 220.29  E-value: 5.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIklEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:cd03296    1 MSI--EVRNVSKRFGDFV------------------------ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDIARISdaelreVRRKKIAMVFQSFALMPHMTVLDNTAFGMEL----AGTPAQERQEKALDALRQVGLEN 156
Cdd:cd03296   55 DSGTILFGGEDATDVP------VQERNVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDW 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 157 YAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:cd03296  129 LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVV 208
                        250       260
                 ....*....|....*....|....*...
gi 493864995 237 IMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03296  209 VMNKGRIEQVGTPDEVYDHPASPFVYSF 236
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
59-272 1.32e-69

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: 222.37  E-value: 1.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdAELREvrrkkIAMVFQSFALMPHMTVLDNTAFGMELAGTPA 138
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRH-----INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  139 QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTI 218
Cdd:TIGR01187  75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  219 VFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF------FRGVDISH 272
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFigeinvFEATVIER 214
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
5-307 3.09e-69

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 222.90  E-value: 3.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:PRK09452  15 VELRGISKSFDGK---------------EVI---------SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISdAELREVRrkkiaMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:PRK09452  71 IMLDGQDITHVP-AENRHVN-----TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 245 QVGTPDEILNNPANDYVRTFfrgVDISHVFSAKDIARRTPNGI----------IRKTPGFGPRSALK-LLQDED 307
Cdd:PRK09452 225 QDGTPREIYEEPKNLFVARF---IGEINIFDATVIERLDEQRVranvegrecnIYVNFAVEPGQKLHvLLRPED 295
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
5-243 1.95e-68

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: 215.47  E-value: 1.95e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03262    1 IEIKNLHKSFGDF---------------HVL---------KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIArISDAELREVRrKKIAMVFQSFALMPHMTVLDNTAFG-MELAGTPAQERQEKALDALRQVGLENYAHAYPD 163
Cdd:cd03262   57 IIIDGLKLT-DDKKNINELR-QKVGMVFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03262  135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
44-252 2.45e-67

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 213.77  E-value: 2.45e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTV 123
Cdd:COG3638   19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR-IGMIFQQFNLVPRLSV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMeLAGTPA---------QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:COG3638   98 LTNVLAGR-LGRTSTwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVAS 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:COG3638  177 LDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
5-268 3.40e-67

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: 213.51  E-value: 3.40e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPQRafKYIekgltkeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1124    2 LEVRNLSVSYGQGGRR--VPV------------------LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAElrevRRKKIAMVFQSF--ALMPHMTVLDNTAFGMELAGTPaqERQEKALDALRQVGL-ENYAHAY 161
Cdd:COG1124   62 VTFDGRPVTRRRRKA----FRRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRY 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:COG1124  136 PHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG 215
                        250       260
                 ....*....|....*....|....*..
gi 493864995 242 EVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:COG1124  216 RIVEELTVADLLAGPKHPYTRELLAAS 242
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
44-262 9.67e-66

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 212.28  E-value: 9.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQ-SFA-LMPHM 121
Cdd:COG4608   34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRR-MQMVFQdPYAsLNPRM 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAG-TPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:COG4608  113 TVGDIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4608  193 QAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-257 1.63e-65

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: 217.08  E-value: 1.63e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPQRAfkyiekgltkeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG1123    1 MTPLLEVRDLSVRYPGGDVPA----------------------VDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 T---RGQVLIDGVDIARISDAelreVRRKKIAMVFQSF--ALMPhMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLE 155
Cdd:COG1123   59 GgriSGEVLLDGRDLLELSEA----LRGRRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLE 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 156 NYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:COG1123  134 RRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRV 213
                        250       260
                 ....*....|....*....|..
gi 493864995 236 AIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG1123  214 VVMDDGRIVEDGPPEEILAAPQ 235
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
45-238 3.86e-65

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 208.56  E-value: 3.86e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARiSDAElREVrrkkiamVFQSFALMPHMTVL 124
Cdd:COG4525   24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD-RGV-------VFQKDALLPWLNVL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:COG4525   95 DNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQ 174
                        170       180       190
                 ....*....|....*....|....*....|....
gi 493864995 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:COG4525  175 ELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
5-252 5.42e-65

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: 207.42  E-value: 5.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEhpqrafkyiekgltkeqilEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03256    1 IEVENLSKTYPN-------------------GKKAL----KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGS 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGM--------ELAGTPAQERQEKALDALRQVGLEN 156
Cdd:cd03256   58 VLIDGTDINKLKGKALRQLRRQ-IGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLD 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 157 YAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:cd03256  137 KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIV 216
                        250
                 ....*....|....*.
gi 493864995 237 IMQNGEVVQVGTPDEI 252
Cdd:cd03256  217 GLKDGRIVFDGPPAEL 232
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
35-264 4.00e-64

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: 204.88  E-value: 4.00e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDaelrevRRKKIAMVFQS 114
Cdd:cd03299    6 LSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------EKRDISYVPQN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 115 FALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03299   80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:cd03299  160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEF 229
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
47-264 4.64e-64

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 204.60  E-value: 4.64e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAElrevrrKKIAMVFQSFALMPHMTVLDN 126
Cdd:COG3840   18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPVSMLFQENNLFPHLTVAQN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 127 TAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
Cdd:COG3840   92 IGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 207 LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:COG3840  172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
22-268 6.51e-64

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 204.56  E-value: 6.51e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  22 FKYIEKGLTKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaRISDAELR 101
Cdd:PRK09493   4 FKNVSKHFGPTQVL---------HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDER 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 102 EVRRKKiAMVFQSFALMPHMTVLDNTAFG-MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALA 180
Cdd:PRK09493  74 LIRQEA-GMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 181 INPDILLMDEAFSALDPLIRTE----MQDelvklQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEvlkvMQD-----LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
                        250
                 ....*....|..
gi 493864995 257 ANDYVRTFFRGV 268
Cdd:PRK09493 228 PSQRLQEFLQHV 239
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
34-254 2.15e-63

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: 203.74  E-value: 2.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  34 ILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAElrevRRKK 107
Cdd:COG1120    1 MLEAENLSVGyggrpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 108 IAMVFQSFALMPHMTVLDNTAFG----MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINP 183
Cdd:COG1120   77 IAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1120  157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
5-252 1.25e-62

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: 201.37  E-value: 1.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    5 LEVKNLYKIFGEHPQrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:TIGR02315   2 LEVENLSKVYPNGKQ-----------------------ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGS 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   85 VLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGmELAGTPA---------QERQEKALDALRQVGLE 155
Cdd:TIGR02315  59 ILLEGTDITKLRGKKLRKLRRR-IGMIFQHYNLIERLTVLENVLHG-RLGYKPTwrsllgrfsEEDKERALSALERVGLA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  156 NYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:TIGR02315 137 DKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRI 216
                         250
                  ....*....|....*..
gi 493864995  236 AIMQNGEVVQVGTPDEI 252
Cdd:TIGR02315 217 VGLKAGEIVFDGAPSEL 233
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
5-305 1.96e-62

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 205.45  E-value: 1.96e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIF-GEHpqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:PRK11607  20 LEIRNLTKSFdGQH-------------------------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  84 QVLIDGVDIARISDaelrevRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPD 163
Cdd:PRK11607  75 QIMLDGVDLSHVPP------YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPH 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 244 VQVGTPDEILNNPANDYVRTFFRGVDishVFSAKdIARRTPNGIIRKTPGFgpRSALKLLQD 305
Cdd:PRK11607 229 VQIGEPEEIYEHPTTRYSAEFIGSVN---VFEGV-LKERQEDGLVIDSPGL--VHPLKVDAD 284
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
44-247 1.41e-61

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 197.97  E-value: 1.41e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTV 123
Cdd:COG2884   18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR-IGVVFQDFRLLPDRTV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEM 203
Cdd:COG2884   97 YENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP----ET 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493864995 204 QDELVKL-QAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:COG2884  173 SWEIMELlEEINRRgtTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
46-264 1.45e-61

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 202.24  E-value: 1.45e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaelreVRRKKIAMVFQSFALMPHMTVLD 125
Cdd:PRK10851  20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------ARDRKVGFVFQHYALFRHMTVFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 126 NTAFGMELagTPAQER------QEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10851  94 NIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK10851 172 RKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF 236
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
44-252 1.77e-61

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: 197.79  E-value: 1.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIARISDAELrEVRRKkIAMVFQSfALM 118
Cdd:cd03260   16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVL-ELRRR-VGMVFQK-PNP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 PHMTVLDNTAFGMELAGT-PAQERQEKALDALRQVGLENYAH--AYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:cd03260   93 FPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 196 DPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03260  173 DPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
45-242 2.33e-61

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: 196.92  E-value: 2.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFA---LMPhm 121
Cdd:cd03225   18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDdqfFGP-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:cd03225   92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 493864995 202 EMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd03225  172 ELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
44-255 6.46e-61

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: 197.65  E-value: 6.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiaRISDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:TIGR04520  18 LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK-VGMVFQN----PDnqf 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  121 --MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:TIGR04520  91 vgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995  199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:TIGR04520 171 GRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
7-265 3.84e-60

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 198.68  E-value: 3.84e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   7 VKNLYKIFGehpqrafkyieKGLTKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL 86
Cdd:NF040933   5 VENVTKIFK-----------KGKKEVVAL---------DNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIY 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  87 IDGVDIARISDAELrEVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELS 166
Cdd:NF040933  65 FDDKLVASPGKIIV-PPEDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 167 GGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEMQDELVK-LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:NF040933 144 GGQQQRVALARALVKNPQVLLLDEPFSNLDARIR-DSARALVKkIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQ 222
                        250       260
                 ....*....|....*....|
gi 493864995 246 VGTPDEILNNPANDYVRTFF 265
Cdd:NF040933 223 VGKPEEIYDNPANIFVARLI 242
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
44-263 1.76e-59

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: 201.45  E-value: 1.76e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGVDIARISDAELREVRRKkIAMVFQS-FA-LMPHM 121
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQDpFGsLSPRM 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMEL--AGTPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:COG4172  380 TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
Cdd:COG4172  460 VQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
5-257 2.30e-57

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: 188.32  E-value: 2.30e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGehpqrafkyiekGLTkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG0411    5 LEVRGLTKRFG------------GLV------------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDaelREVRRKKIAMVFQSFALMPHMTVLDN----------TAFGMELAGTPAQERQE-----KALDAL 149
Cdd:COG0411   61 ILFDGRDITGLPP---HRIARLGIARTFQNPRLFPELTVLENvlvaaharlgRGLLAALLRLPRARREEreareRAEELL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 150 RQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAM 229
Cdd:COG0411  138 ERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVM 217
                        250       260
                 ....*....|....*....|....*...
gi 493864995 230 RIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0411  218 GLADRIVVLDFGRVIAEGTPAEVRADPR 245
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
5-262 3.94e-57

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 188.12  E-value: 3.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHpqrafkyieKGLTKEQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4167    5 LEVRNLSKTFKYR---------TGLFRRQQFE------AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGV-----DIARisdaelrevRRKKIAMVFQ--SFALMPHMTV---LD-----NTAFgmelagtPAQERQEKALDAL 149
Cdd:COG4167   70 ILINGHkleygDYKY---------RCKHIRMIFQdpNTSLNPRLNIgqiLEeplrlNTDL-------TAEEREERIFATL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 150 RQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEA 228
Cdd:COG4167  134 RLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIV 213
                        250       260       270
                 ....*....|....*....|....*....|....
gi 493864995 229 MRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4167  214 KHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTK 247
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
27-280 4.00e-57

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: 187.37  E-value: 4.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  27 KGLTKeqileKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAelrevRRK 106
Cdd:COG4555    5 ENLSK-----KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----ARR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDIL 186
Cdd:COG4555   75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFr 266
Cdd:COG4555  155 LLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF- 232
                        250
                 ....*....|....
gi 493864995 267 gvdISHVFSAKDIA 280
Cdd:COG4555  233 ---VALIGSEEGEA 243
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
2-267 2.53e-56

ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 185.77  E-value: 2.53e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   2 AIKLEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT 81
Cdd:COG4598    6 PPALEVRDLHKSFGDL---------------EVL---------KGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPD 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  82 RGQVLIDGVDIARISD-------AELREVR--RKKIAMVFQSFALMPHMTVLDNTAFG-MELAGTPAQERQEKALDALRQ 151
Cdd:COG4598   62 SGEIRVGGEEIRLKPDrdgelvpADRRQLQriRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 152 VGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDELVKLQ---AKHQRTIVFISHDLDEA 228
Cdd:COG4598  142 VGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP----ELVGEVLKVMrdlAEEGRTMLVVTHEMGFA 217
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 493864995 229 MRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:COG4598  218 RDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
44-262 3.07e-55

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: 190.28  E-value: 3.07e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQ--SFAL 117
Cdd:COG4172   26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRIAMIFQepMTSL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 MPHMTVLDNTAFGMEL-AGTPAQERQEKALDALRQVGL---ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:COG4172  106 NPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTT 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:COG4172  186 ALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTR 254
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
44-264 5.33e-55

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 185.31  E-value: 5.33e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK11432  22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRDICMVFQSYALFPHMSL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11432  96 GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
45-264 6.34e-55

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 185.62  E-value: 6.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREvrrKKIAMVFQSFALMPHMTVL 124
Cdd:PRK11000  20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPAE---RGVGMVFQSYALYPHLSVA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK11000  94 ENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGF 233
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
5-257 1.23e-54

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: 180.33  E-value: 1.23e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGehpqrafkyiekGLTkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03219    1 LEVRGLTKRFG------------GLV------------ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDaelREVRRKKIAMVFQSFALMPHMTVLDN--------TAFGMELAGTPAQERQ--EKALDALRQVGL 154
Cdd:cd03219   57 VLFDGEDITGLPP---HEIARLGIGRTFQIPRLFPELTVLENvmvaaqarTGSGLLLARARREEREarERAEELLERVGL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 155 ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDR 234
Cdd:cd03219  134 ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADR 212
                        250       260
                 ....*....|....*....|...
gi 493864995 235 IAIMQNGEVVQVGTPDEILNNPA 257
Cdd:cd03219  213 VTVLDQGRVIAEGTPDEVRNNPR 235
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-261 2.27e-54

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 180.62  E-value: 2.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE- 79
Cdd:COG1117    8 LEPKIEVRNLNVYYGDK---------------QAL---------KDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDl 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  80 -P---TRGQVLIDGVDIARiSDAELREVRRKkIAMVFQS---FAlmphMTVLDNTAFGMELAG-TPAQERQEKALDALRQ 151
Cdd:COG1117   64 iPgarVEGEILLDGEDIYD-PDVDVVELRRR-VGMVFQKpnpFP----KSIYDNVAYGLRLHGiKSKSELDEIVEESLRK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 152 VGLenyahayPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELVkLQAKHQRTIVF 220
Cdd:COG1117  138 AAL-------WDEvkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP-ISTAKIEELI-LELKKDYTIVI 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 493864995 221 ISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN----DYV 261
Cdd:COG1117  209 VTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDkrteDYI 253
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
44-252 1.05e-53

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 179.44  E-value: 1.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaRISDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:PRK13635  23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ-VGMVFQN----PDnqf 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 --MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13635  95 vgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
5-243 9.00e-53

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: 173.35  E-value: 9.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03230    1 IEVRNLSKRYGKKT------------------------ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaELREVRRKkIAMVFQSFALMPHMTVLDNTafgmelagtpaqerqekaldalrqvglenyahaypdE 164
Cdd:cd03230   57 IKVLGKDIKK----EPEEVKRR-IGYLPEEPSLYENLTVRENL------------------------------------K 95
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03230   96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
45-243 2.26e-52

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 173.85  E-value: 2.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFALMPhMTVL 124
Cdd:COG4619   17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWR----RQVAYVPQEPALWG-GTVR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAGTPAQErqEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:COG4619   92 DNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493864995 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:COG4619  170 EELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
45-251 3.24e-52

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: 174.16  E-value: 3.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVL 124
Cdd:COG4181   29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARHVGFVFQSFQLLPTLTAL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAGTPaqERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:COG4181  109 ENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQII 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493864995 205 DELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDE 251
Cdd:COG4181  187 DLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAATA 232
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
5-252 9.92e-52

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: 172.30  E-value: 9.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPQRAfkyiekgltkeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03263    1 LQIRNLTKTYKKGTKPA----------------------VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03263   59 AYINGYSIRT----DRKAARQS-LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRART 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03263  134 LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211

                 ....*...
gi 493864995 245 QVGTPDEI 252
Cdd:cd03263  212 CIGSPQEL 219
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
44-264 1.53e-51

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 176.19  E-value: 1.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREvrrKKIAMVFQSFALMPHMTV 123
Cdd:PRK11650  20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG---RVVNELEPAD---RDIAMVFQNYALYPHMSV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11650  94 RENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK11650 174 RLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
44-254 8.92e-51

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: 181.19  E-value: 8.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:COG2274  491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL----RRQIGVVLQDVFLF-SGTI 565
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG2274  566 RENITLGDPDAT------DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEAT 639
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG2274  640 SALDAETEAIILENL--RRLLKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLA 698
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
44-255 1.85e-50

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 170.94  E-value: 1.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIariSDAELREVRrKKIAMVFQSfalmPH--- 120
Cdd:PRK13632  25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIR-KKIGIIFQN----PDnqf 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 --MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13632  97 igATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMrIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
44-255 3.09e-50

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 178.05  E-value: 3.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:COG1132  356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFLF-SGTI 430
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG1132  431 RENIRYGRPDAT------DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEAT 504
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 193 SALDPliRTEM--QDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG1132  505 SALDT--ETEAliQEALERL--MKGRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
46-257 4.47e-50

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: 172.21  E-value: 4.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG---VDIARISDaelREVRRKKIAMVFQSFALMPHMT 122
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIF---LPPHRRRIGYVFQEARLFPHLS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 123 VLDNTAFGMelAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:COG4148   94 VRGNLLYGR--KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG4148  172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
53-247 5.81e-50

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: 167.47  E-value: 5.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaRISDAELR---EVRRKKIAMVFQSFALMPHMTVLDNTAF 129
Cdd:cd03297   22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---VLFDSRKKinlPPQQRKIGLVFQQYALFPHLNVRENLAF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 130 GME-LAGTPAQERQEKALDALrqvGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
Cdd:cd03297   99 GLKrKRNREDRISVDELLDLL---GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493864995 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03297  176 QIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
44-256 1.13e-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: 167.64  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrrkkiaMVFQSFALMPHMTV 123
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  124 LDNTAFGME--LAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:TIGR01184  72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 493864995  202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGtpdEILNNP 256
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVP 203
CBS_pair_ABC_Gly_Pro_assoc cd09831
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
278-393 1.38e-49

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. 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: 341402 [Multi-domain]  Cd Length: 116  Bit Score: 163.11  E-value: 1.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 278 DIARRTPNGIIRKTpGFGPRSALKLLQDEDREYGYLVERGNKFVGVVSIDSLKTALSEN-QGIDAALIDAPLAVDAETPL 356
Cdd:cd09831    1 DIARKTQVTVIEKT-GDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENaQSLEDAFLTDVETVPADTSL 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 493864995 357 SELLSHVGQAPCAVPVVGEEQQYVGIISKRMLLQALD 393
Cdd:cd09831   80 SDILGLVASAPCPLPVVDEDGRYLGVISKASLLETLD 116
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
44-254 2.11e-49

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 167.19  E-value: 2.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaelrevRRKKIAMVFQSFALMPH--M 121
Cdd:COG1121   22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---------ARRRIGYVPQRAEVDWDfpI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFG----MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:COG1121   93 TVRDVVLMGrygrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 198 lirtEMQDELVKL---QAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILN 254
Cdd:COG1121  173 ----ATEEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
32-252 2.27e-49

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: 166.39  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaELREVRRKkIAMV 111
Cdd:cd03265    4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRR-IGIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 112 FQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:cd03265   79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:cd03265  159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
46-229 7.02e-49

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 166.03  E-value: 7.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdAElREVrrkkiamVFQSFALMPHMTVLD 125
Cdd:PRK11248  19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AE-RGV-------VFQNEGLLPWRNVQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 126 NTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:PRK11248  90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
                        170       180
                 ....*....|....*....|....
gi 493864995 206 ELVKLQAKHQRTIVFISHDLDEAM 229
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDIEEAV 193
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
35-247 3.92e-48

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: 162.66  E-value: 3.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLSLGVK--DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARIsdaelrEVRRKKIAMVF 112
Cdd:cd03298    3 LDKIRFSYGEQpmHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA------PPADRPVSMLF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 113 QSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03298   77 QENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03298  157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1-256 5.26e-48

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 163.65  E-value: 5.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIklEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:COG4161    1 MSI--QLKNINCFYGSH---------------QAL---------FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETP 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDGVDI---ARISDAELREVRRKkIAMVFQSFALMPHMTVLDN-TAFGMELAGTPAQERQEKALDALRQVGLEN 156
Cdd:COG4161   55 DSGQLNIAGHQFdfsQKPSEKAIRLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 157 YAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIA 236
Cdd:COG4161  134 KADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV-EIIRELSQTGITQVIVTHEVEFARKVASQVV 212
                        250       260
                 ....*....|....*....|
gi 493864995 237 IMQNGEVVQVGTPdEILNNP 256
Cdd:COG4161  213 YMEKGRIIEQGDA-SHFTQP 231
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
44-247 2.58e-47

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: 159.52  E-value: 2.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAElrevRRKKIAMVFQsfalmphmtv 123
Cdd:cd03214   15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ---------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 ldntafgmelagtpaqerqekaldALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03214   81 ------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493864995 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03214  137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
46-243 5.36e-47

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: 159.88  E-value: 5.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLD 125
Cdd:cd03292   19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQDFRLLPDRNVYE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 126 NTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:cd03292   98 NVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493864995 206 ELVKLqakHQR--TIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03292  178 LLKKI---NKAgtTVVVATHAKELVDTTRHRVIALERGKL 214
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
47-268 2.09e-46

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: 159.61  E-value: 2.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-------ARISDAELREVR--RKKIAMVFQSFAL 117
Cdd:TIGR03005  19 LNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrnGPLVPADEKHLRqmRNKIGMVFQSFNL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  118 MPHMTVLDN-TAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:TIGR03005  99 FPHKTVLDNvTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALD 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995  197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:TIGR03005 179 PELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSKV 250
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
44-242 1.14e-45

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: 154.32  E-value: 1.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQsfalmphmtv 123
Cdd:cd00267   15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYVPQ---------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 ldntafgmelagtpaqerqekaldalrqvglenyahaypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd00267   81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493864995 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:cd00267  120 LELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
44-193 1.40e-45

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: 153.96  E-value: 1.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995  124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAH----AYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:pfam00005  77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
44-242 1.40e-45

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: 154.85  E-value: 1.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTafgmelagtpaqerqekaldalrqvglenyahaypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03228   93 RENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493864995 204 QDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGE 242
Cdd:cd03228  136 LEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
48-262 4.23e-45

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 158.59  E-value: 4.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNrLIE-PTRGQVLIDGVDIARiSDAELREVRRKKIAMVFQS-FA-LMPHMTV- 123
Cdd:PRK11308  35 SFTLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVFQNpYGsLNPRKKVg 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 -------LDNTAFGmelagtpAQERQEKALDALRQVGL--ENYaHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK11308 113 qileeplLINTSLS-------AAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1-250 5.15e-45

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 155.56  E-value: 5.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIklEVKNLYKIFGEHpqrafkyiekgltkeQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
Cdd:PRK11124   1 MSI--QLNGINCFYGAH---------------QALF---------DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMP 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  81 TRGQVLIDG--VDI-ARISDAELREVRRKkIAMVFQSFALMPHMTVLDN-TAFGMELAGTPAQERQEKALDALRQVGLEN 156
Cdd:PRK11124  55 RSGTLNIAGnhFDFsKTPSDKAIRELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKP 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 157 YAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIA 236
Cdd:PRK11124 134 YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGI-TQVIVTHEVEVARKTASRVV 212
                        250
                 ....*....|....
gi 493864995 237 IMQNGEVVQVGTPD 250
Cdd:PRK11124 213 YMENGHIVEQGDAS 226
cbiO PRK13650
energy-coupling factor transporter ATPase;
44-252 6.10e-45

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 156.82  E-value: 6.10e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREVRRKkIAMVFQSfalmPH--- 120
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIRHK-IGMVFQN----PDnqf 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 --MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13650  95 vgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
44-247 6.10e-45

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: 154.61  E-value: 6.10e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaelrevRRKKIAMVFQSFAL---MPh 120
Cdd:cd03235   15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRSIdrdFP- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 MTVLDNTAFG----MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03235   85 ISVRDVVLMGlyghKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 197 PlirtEMQDELVKL---QAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVG 247
Cdd:cd03235  165 P----KTQEDIYELlreLRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
5-266 3.05e-44

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 153.75  E-value: 3.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFgeHPQRAFKYIEkgltkeqilektglslgvkdasLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:PRK11264   4 IEVKNLVKKF--HGQTVLHGID----------------------LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDI--ARISDAELREVR--RKKIAMVFQSFALMPHMTVLDNTAFG-MELAGTPAQERQEKALDALRQVGLENYAH 159
Cdd:PRK11264  60 IRVGDITIdtARSLSQQKGLIRqlRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKET 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 160 AYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:PRK11264 140 SYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMD 218
                        250       260
                 ....*....|....*....|....*..
gi 493864995 240 NGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK11264 219 QGRIVEQGPAKALFADPQQPRTRQFLE 245
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
48-254 8.53e-44

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 152.04  E-value: 8.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAelrevrRKKIAMVFQSFALMPHMTVLDNT 127
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 128 AFGME--LAGTPAQERQEKALdaLRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:PRK10771  93 GLGLNpgLKLNAAQREKLHAI--ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493864995 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
44-270 1.08e-43

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 154.86  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRrKKIAMVFQS--FALMPHM 121
Cdd:PRK15079  37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplASLNPRM 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTA-----FGMELagtPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK15079 116 TIGEIIAeplrtYHPKL---SRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI 270
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPI 267
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
4-267 1.48e-43

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 152.43  E-value: 1.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   4 KLEVKNLYKIFGEHpqrafkyiekgltkeQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:PRK10619   5 KLNVIDLHKRYGEH---------------EVL---------KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  84 QVLIDGVDI--ARISDAELR-------EVRRKKIAMVFQSFALMPHMTVLDNTAFG-MELAGTPAQERQEKALDALRQVG 153
Cdd:PRK10619  61 SIVVNGQTInlVRDKDGQLKvadknqlRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 154 LENYAHA-YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIG 232
Cdd:PRK10619 141 IDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVS 219
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 493864995 233 DRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK10619 220 SHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
cbiO PRK13637
energy-coupling factor transporter ATPase;
44-255 3.01e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 152.51  E-value: 3.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARiSDAELREVRrKKIAMVFQ--SFALMPHm 121
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIR-KKVGLVFQypEYQLFEE- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGTPAQERQEKALDALRQVGL--ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
44-257 4.97e-43

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: 158.01  E-value: 4.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVrrkkIAMVFQSFALMpHMTV 123
Cdd:COG4987  351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR----IAVVPQRPHLF-DTTL 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4987  426 RENLRLARPDAT------DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPT 499
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG4987  500 EGLDAATEQALLADL--LEALAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
34-251 5.60e-43

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 149.17  E-value: 5.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  34 ILEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI---EP---TRGQVLIDGVDIARISdaelreV 103
Cdd:COG4136    3 SLENLTITLGgrplLAPLSLTVAPGEILTLMGPSGSGKST---LLAAIAgtlSPafsASGEVLLNGRRLTALP------A 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 104 RRKKIAMVFQSFALMPHMTVLDNTAFGMElAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINP 183
Cdd:COG4136   74 EQRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 184 DILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIV-FISHDLDEAmrigdriaiMQNGEVVQVGTPDE 251
Cdd:COG4136  153 RALLLDEPFSKLDAALRAQFR-EFVFEQIRQRGIPAlLVTHDEEDA---------PAAGRVLDLGNWQH 211
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
22-255 9.28e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 151.01  E-value: 9.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  22 FKYIEKGLTKEQIlektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIariSDAELR 101
Cdd:PRK13633  12 YKYESNEESTEKL--------ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT---SDEENL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 102 EVRRKKIAMVFQSfalmPH-----MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLA 176
Cdd:PRK13633  81 WDIRNKAGMVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
42-257 1.21e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 150.94  E-value: 1.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIARISDAELREVRrKKIAMVFQsFAlmPH 120
Cdd:PRK13634  21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLR-KKVGIVFQ-FP--EH 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 M----TVLDNTAFGMELAGTPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13634  97 QlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
44-268 1.27e-42

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 149.61  E-value: 1.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIARiSDAELREVRRKkIAMVFQSFALM 118
Cdd:PRK14267  20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYS-PDVDPIEVRRE-VGMVFQYPNPF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 PHMTVLDNTAFGMELAG--TPAQERQEKALDALRQVGL----ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK14267  98 PHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 193 SALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:PRK14267 178 ANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
46-268 1.74e-42

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 149.92  E-value: 1.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRrKKIAMVFQSFALMPHMTVLD 125
Cdd:PRK11831  25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 126 NTAFGM-ELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLirteMQ 204
Cdd:PRK11831 104 NVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI----TM 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 205 DELVKL--QAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPaNDYVRTFFRGV 268
Cdd:PRK11831 180 GVLVKLisELNSALgvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
44-255 2.19e-42

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: 156.07  E-value: 2.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFALmPHMTV 123
Cdd:COG4988  353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR----RQIAWVPQNPYL-FAGTI 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAgTPAQERQekaldALRQVGLENYAHAYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4988  428 RENLRLGRPDA-SDEELEA-----ALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPT 501
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:COG4988  502 AHLDAETEAEILQAL--RRLAKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
46-278 5.37e-42

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: 151.03  E-value: 5.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  126 NTAFGMELAGTPAQERQEKALDALrqVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
Cdd:TIGR02142  95 NLRYGMKRARPSERRISFERVIEL--LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995  206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISHVFSAKD 278
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEGVVAEHD 245
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
27-243 6.99e-42

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 147.90  E-value: 6.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  27 KGLTKeQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdgvdiariSDAELREVRrK 106
Cdd:PRK11247  16 NAVSK-RYGERTVL----NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA--------GTAPLAEAR-E 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 107 KIAMVFQSFALMPHMTVLDNTAFGmeLAGtpaqERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDIL 186
Cdd:PRK11247  82 DTRLMFQDARLLPWKKVIDNVGLG--LKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
44-252 4.59e-41

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: 147.15  E-value: 4.59e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaELREVRRKkIAMVFQSFALMPHMTV 123
Cdd:TIGR01188   9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR----EPRKVRRS-IGIVPQYASVDEDLTG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:TIGR01188  84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 493864995  204 QDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:TIGR01188 164 WDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
5-252 4.61e-41

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 146.79  E-value: 4.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHpqRAfkyiekgltkeqilektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4152    2 LELKGLTKRFGDK--TA----------------------VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaelrEVRRKkiamvfqsFALMPH-------MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENY 157
Cdd:COG4152   58 VLWDGEPLDP-------EDRRR--------IGYLPEerglypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDR 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 158 AHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:COG4152  123 ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVI 201
                        250
                 ....*....|....*
gi 493864995 238 MQNGEVVQVGTPDEI 252
Cdd:COG4152  202 INKGRKVLSGSVDEI 216
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
5-262 5.13e-41

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 146.09  E-value: 5.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKifgehpqrAFKYiEKGLTKEQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:PRK15112   5 LEVRNLSK--------TFRY-RTGWFRRQTVE------AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIArISDAELREVRrkkIAMVFQ--SFALMPHMTVLDNTAFGMEL-AGTPAQERQEKALDALRQVGL-ENYAHA 160
Cdd:PRK15112  70 LLIDDHPLH-FGDYSYRSQR---IRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASY 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
                        250       260
                 ....*....|....*....|..
gi 493864995 241 GEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15112 226 GEVVERGSTADVLASPLHELTK 247
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
44-267 5.24e-41

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 145.44  E-value: 5.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFALM 118
Cdd:PRK14247  19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELR----RRVQMVFQIPNPI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 PHMTVLDNTAFGMEL--AGTPAQERQEKALDALRQVGL----ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK14247  95 PNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 193 SALDPlIRTEMQDELVkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK14247 175 ANLDP-ENTAKIESLF-LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTG 247
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
41-254 7.36e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 145.66  E-value: 7.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREVRrKKIAMVFQSfalmPH 120
Cdd:PRK13648  22 SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN---QAITDDNFEKLR-KHIGIVFQN----PD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 -----MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13648  94 nqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
cbiO PRK13640
energy-coupling factor transporter ATPase;
44-256 2.20e-40

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 144.56  E-value: 2.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIARISDAELREvrrkKIAMVFQSfalmPH 120
Cdd:PRK13640  23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE----KVGIVFQN----PD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 -----MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13640  95 nqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
25-267 2.27e-40

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 144.03  E-value: 2.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  25 IEKGLTKEQILEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE------PTRGQVLIDGVDI 92
Cdd:PRK14246   1 MEAGKSAEDVFNISRLYLYIndkailKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  93 ARISDAELrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKAL-DALRQVGLENYAH----AYPDELSG 167
Cdd:PRK14246  81 FQIDAIKL----RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVeECLRKVGLWKEVYdrlnSPASQLSG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 168 GMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
                        250       260
                 ....*....|....*....|
gi 493864995 248 TPDEILNNPANDYVRTFFRG 267
Cdd:PRK14246 235 SSNEIFTSPKNELTEKYVIG 254
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
5-247 3.25e-40

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: 142.03  E-value: 3.25e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03269    1 LEVENVTKRFGRVT------------------------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGvdiarisdAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDE 164
Cdd:cd03269   57 VLFDG--------KPLDIAARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEE 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03269  129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207

                 ...
gi 493864995 245 QVG 247
Cdd:cd03269  208 LYG 210
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
27-253 4.97e-40

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: 149.18  E-value: 4.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   27 KGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI----DGVDIARISdAELRE 102
Cdd:TIGR03269 283 RNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG-PDGRG 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  103 VRRKKIAMVFQSFALMPHMTVLDN--TAFGMELagtPAQERQEKALDALRQVGL-ENYAHA----YPDELSGGMRQRVGL 175
Cdd:TIGR03269 362 RAKRYIGILHQEYDLYPHRTVLDNltEAIGLEL---PDELARMKAVITLKMVGFdEEKAEEildkYPDELSEGERHRVAL 438
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995  176 ARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
31-261 5.81e-40

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 142.61  E-value: 5.81e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  31 KEQILEKTGLSL------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEP---TRGQVLIDGVDI--ARISD 97
Cdd:PRK14239   2 TEPILQVSDLSVyynkkkALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  98 AELRevrrKKIAMVFQSFALMPhMTVLDNTAFGMELAGTPAQERQEKALD-ALRQVGL----ENYAHAYPDELSGGMRQR 172
Cdd:PRK14239  82 VDLR----KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkSLKGASIwdevKDRLHDSALGLSGGQQQR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 173 VGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
                        250
                 ....*....|...
gi 493864995 253 LNNPAN----DYV 261
Cdd:PRK14239 235 FMNPKHketeDYI 247
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
44-276 1.39e-39

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 141.79  E-value: 1.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRrkkiAMVFQ----SFALmp 119
Cdd:COG4559   17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR----AVLPQhsslAFPF-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 hmTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAH-AYPdELSGGMRQRVGLARALA-------INPDILLMDEA 191
Cdd:COG4559   91 --TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 192 FSALDPL--IRTeMQdeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrtffrgvd 269
Cdd:COG4559  168 TSALDLAhqHAV-LR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL------------ 232

                 ....*..
gi 493864995 270 ISHVFSA 276
Cdd:COG4559  233 LERVYGA 239
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
45-253 5.97e-39

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: 139.60  E-value: 5.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiarISDAELREVRRkKIAMVFQSFALMPhMTVL 124
Cdd:cd03249   20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRWLRS-QIGLVSQEPVLFD-GTIA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAgtpaqeRQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03249   95 ENIRYGKPDA------TDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 194 ALDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03249  169 ALDAESEKLVQEALDR--AMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELM 225
cbiO PRK13646
energy-coupling factor transporter ATPase;
44-254 8.23e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 140.69  E-value: 8.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-ARISDAELREVRrKKIAMVFQsfalMPHMT 122
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVR-KRIGMVFQ----FPESQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 123 VLDNTA-----FGMELAGTPAQERQEKALDALRQVGLE-NYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13646  98 LFEDTVereiiFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
44-245 9.06e-39

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 139.82  E-value: 9.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQSF--ALMPHM 121
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDSisAVNPRK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGME-LAGTPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10419 107 TVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 493864995 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
44-253 1.18e-38

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: 138.51  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREvrrkKIAMVFQSFALMPHmTV 123
Cdd:cd03254   19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS----MIGVVLQDTFLFSG-TI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAgtpaqeRQEKALDALRQVG-------LENYAHAYPDE----LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03254   94 MENIRLGRPNA------TDEEVIEAAKEAGahdfimkLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEAT 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLDeAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03254  168 SNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
44-245 1.58e-38

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 138.41  E-value: 1.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK11629  25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493864995 204 QDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQ 245
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-252 2.08e-38

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 144.01  E-value: 2.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGehpqrafkyiekgltkeqilektglslGVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL 77
Cdd:COG1129    1 AEPLLEMRGISKSFG---------------------------GVKaldGVSLELRPGEVHALLGENGAGKSTLMKILSGV 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  78 IEPTRGQVLIDG--VDIARISDAElrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPA---QERQEKALDALRQV 152
Cdd:COG1129   54 YQPDSGEILLDGepVRFRSPRDAQ-----AAGIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 153 GLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP--------LIRtemqdelvKLQAKHqRTIVFISHD 224
Cdd:COG1129  129 GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEreverlfrIIR--------RLKAQG-VAIIYISHR 199
                        250       260       270
                 ....*....|....*....|....*....|...
gi 493864995 225 LDEAMRIGDRIAIMQNGEVVQVG-----TPDEI 252
Cdd:COG1129  200 LDEVFEIADRVTVLRDGRLVGTGpvaelTEDEL 232
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
5-228 2.08e-38

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: 137.23  E-value: 2.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPqrafkyiekgltkeqILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4133    3 LEAENLSCRRGERL---------------LFS---------GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaeLREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQekALDALRQVGLENYAHAYPDE 164
Cdd:COG4133   59 VLWNGEPIRD-----AREDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQ 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEA 228
Cdd:COG4133  132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLEL 194
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
45-256 3.29e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 138.67  E-value: 3.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaRISDAELREVRrKKIAMVFQS-----FAlmP 119
Cdd:PRK13639  19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNpddqlFA--P 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 hmTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK13639  95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 200 RTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13639 173 ASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
45-254 3.32e-38

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: 137.36  E-value: 3.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMpHMTVL 124
Cdd:cd03253   18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQDTVLF-NDTIG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:cd03253   93 YNIRYGRPDAT------DEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATS 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 194 ALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:cd03253  167 ALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
cbiO PRK13644
energy-coupling factor transporter ATPase;
44-257 1.10e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 137.43  E-value: 1.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaELREVRrKKIAMVFQSfalmPHM-- 121
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIR-KLVGIVFQN----PETqf 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 ---TVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13644  91 vgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 199 IRTEMQDELVKLQAKhQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
cbiO PRK13641
energy-coupling factor transporter ATPase;
35-256 1.11e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 137.65  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-ARISDAELREVRrKKIAMVFQ 113
Cdd:PRK13641  18 MEKKGLD----NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 114 -SFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:PRK13641  93 fPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 192 FSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
44-254 1.12e-37

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 136.75  E-value: 1.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFALMPHMTV 123
Cdd:COG4604   17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KRLAILRQENHINSRLTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGme--laGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:COG4604   93 RELVAFGrfpyskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSV 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493864995 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG4604  173 QMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
35-255 1.30e-37

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: 135.64  E-value: 1.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaeLREVRRKKI 108
Cdd:cd03224    1 LEVENLNAGygksqiLFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP---PHERARAGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 109 AMVFQSFALMPHMTVLDNTAFGME-LAGTPAQERQEKALD---ALRQVglenyAHAYPDELSGGMRQRVGLARALAINPD 184
Cdd:cd03224   78 GYVPEGRRIFPELTVEENLLLGAYaRRRAKRKARLERVYElfpRLKER-----RKQLAGTLSGGEQQMLAIARALMSRPK 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 185 ILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:cd03224  153 LLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1-254 1.90e-37

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 135.59  E-value: 1.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIF--GEHPQRAFKYIEKGLTKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI 78
Cdd:COG1134    1 MSSMIEVENVSKSYrlYHEPSRSLKELLLRRRRTRREEFWAL----KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  79 EPTRGQVLIDGvdiaRISdaELREVrrkkiamvfqSFALMPHMTVLDNTAFGMELAGTPAQERQEKaldaLRQV----GL 154
Cdd:COG1134   77 EPTSGRVEVNG----RVS--ALLEL----------GAGFHPELTGRENIYLNGRLLGLSRKEIDEK----FDEIvefaEL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 155 ENYAHA----YpdelSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMR 230
Cdd:COG1134  137 GDFIDQpvktY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRR 211
                        250       260
                 ....*....|....*....|....
gi 493864995 231 IGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1134  212 LCDRAIWLEKGRLVMDGDPEEVIA 235
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-251 3.86e-37

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 140.93  E-value: 3.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGehpqrafkyiekgltkeqilektglslGV---KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL 77
Cdd:COG3845    2 MPPALELRGITKRFG---------------------------GVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  78 IEPTRGQVLIDG--VDIARISDAelrevRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQE--KALDAL-RQV 152
Cdd:COG3845   55 YQPDSGEILIDGkpVRIRSPRDA-----IALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAarARIRELsERY 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 153 GLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTemqdeLVKLQAKhQRTIVFISHDLDE 227
Cdd:COG3845  130 GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPqeadeLFEI-----LRRLAAE-GKSIIFITHKLRE 203
                        250       260
                 ....*....|....*....|....
gi 493864995 228 AMRIGDRIAIMQNGEVVQVGTPDE 251
Cdd:COG3845  204 VMAIADRVTVLRRGKVVGTVDTAE 227
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
5-262 5.11e-37

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 141.00  E-value: 5.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLykifgehpQRAFKyIEKGLTKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQ 84
Cdd:PRK15134 276 LDVEQL--------QVAFP-IRKGILKRTVDHNVVV----KNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGE 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAELREVRRKkIAMVFQ--SFALMPHMTVLDNTAFGMEL--AGTPAQERQEKALDALRQVGLE-NYAH 159
Cdd:PRK15134 342 IWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRH 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 160 AYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLR 500
                        250       260
                 ....*....|....*....|...
gi 493864995 240 NGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15134 501 QGEVVEQGDCERVFAAPQQEYTR 523
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
44-253 6.47e-37

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: 133.90  E-value: 6.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03251   18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQDVFLF-NDTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03251   93 AENIAYGRPGAT------REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 193 SALDplIRTEM--QDELVKLQAkhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03251  167 SALD--TESERlvQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELL 224
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
39-267 4.66e-36

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 132.60  E-value: 4.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIEPTR--GQVLIDGVDIARiSDAELREVRRKkIAMVFQ 113
Cdd:PRK14243  21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRveGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 114 SFALMPHmTVLDNTAFGMELAGTPAQ--ERQEKAL----------DALRQVGLEnyahaypdeLSGGMRQRVGLARALAI 181
Cdd:PRK14243  99 KPNPFPK-SIYDNIAYGARINGYKGDmdELVERSLrqaalwdevkDKLKQSGLS---------LSGGQQQRLCIARAIAV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 182 NPDILLMDEAFSALDPlIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIM---------QNGEVVQVGTPDEI 252
Cdd:PRK14243 169 QPEVILMDEPCSALDP-ISTLRIEELMH-ELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKI 246
                        250
                 ....*....|....*
gi 493864995 253 LNNPANDYVRTFFRG 267
Cdd:PRK14243 247 FNSPQQQATRDYVSG 261
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
5-244 7.91e-36

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: 128.70  E-value: 7.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPqrafkyiekgltkeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:cd03216    1 LELRGITKRFGGVK------------------------ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDaelREVRRKKIAMVFQsfalmphmtvldntafgmelagtpaqerqekaldalrqvglenyahaypde 164
Cdd:cd03216   57 ILVDGKEVSFASP---RDARRAGIAMVYQ--------------------------------------------------- 82
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03216   83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
44-247 9.42e-36

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: 130.39  E-value: 9.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaeLREVRRKKIAMVFQSFALMPHMTV 123
Cdd:cd03264   16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-----QPQKLRRRIGYLPQEFGVYPNFTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03264   90 REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493864995 204 QDELVKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03264  170 RNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
44-253 1.21e-35

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: 130.68  E-value: 1.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03252   18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQENVLF-NRSI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFgmelaGTPAQERqEKALDALRQVGlenyAHAYPDE---------------LSGGMRQRVGLARALAINPDILLM 188
Cdd:cd03252   93 RDNIAL-----ADPGMSM-ERVIEAAKLAG----AHDFISElpegydtivgeqgagLSGGQRQRIAIARALIHNPRILIF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 189 DEAFSALDplirteMQDELVKLQAKHQ----RTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03252  163 DEATSALD------YESEHAIMRNMHDicagRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
4-267 1.95e-35

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 130.15  E-value: 1.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   4 KLEVKNLYKIFGehpqrafkyiekgltKEQIlektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:COG1137    3 TLEAENLVKSYG---------------KRTV---------VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  84 QVLIDGVDIARISdaeLREVRRKKI------AMVFQsfalmpHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENY 157
Cdd:COG1137   59 RIFLDGEDITHLP---MHKRARLGIgylpqeASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 158 AHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQakhQRTI-VFIS-HDLDEAMRIGDRI 235
Cdd:COG1137  130 RKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK---ERGIgVLITdHNVRETLGICDRA 206
                        250       260       270
                 ....*....|....*....|....*....|..
gi 493864995 236 AIMQNGEVVQVGTPDEILNNPAndyVRTFFRG 267
Cdd:COG1137  207 YIISEGKVLAEGTPEEILNNPL---VRKVYLG 235
cbiO PRK13642
energy-coupling factor transporter ATPase;
48-253 2.60e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 130.98  E-value: 2.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREVRRKkIAMVFQS-FALMPHMTVLDN 126
Cdd:PRK13642  27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRRK-IGMVFQNpDNQFVGATVEDD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 127 TAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493864995 207 LVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
3-257 4.07e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 131.51  E-value: 4.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   3 IKLEVKNLYKIFGEHPQRAFKYIEkgltkeqilektglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:PRK13631  20 IILRVKNLYCVFDEKQENELVALN-------------------NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  83 GQVLIDGVDIARISDAELREVR------------RKKIAMVFQ--SFALMPHmTVLDNTAFGMELAGTPAQERQEKALDA 148
Cdd:PRK13631  81 GTIQVGDIYIGDKKNNHELITNpyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 149 LRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHDLDE 227
Cdd:PRK13631 160 LNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEH 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 493864995 228 AMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK13631 239 VLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
44-247 4.72e-35

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: 128.64  E-value: 4.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaELREVRRKkIAMVFQSFALMPHMTV 123
Cdd:cd03266   21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEARRR-LGFVSDSTGLYDRLTA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQErQEKALDALRQV-GLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:cd03266   96 RENLEYFAGLYGLKGDE-LTARLEELADRlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRA 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493864995 203 MQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03266  175 LREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
cbiO PRK13649
energy-coupling factor transporter ATPase;
46-252 8.83e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 129.86  E-value: 8.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAriSDAELREVR--RKKIAMVFQsFA--LMPHM 121
Cdd:PRK13649  25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT--STSKNKDIKqiRKKVGLVFQ-FPesQLFEE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGTPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 201 TEMQDELVKLqakHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK13649 182 KELMTLFKKL---HQSgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
44-264 1.47e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 128.62  E-value: 1.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDG-VDIARISDAELR---EVRRKKIAMVFQSFALMP 119
Cdd:PRK14258  23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrVEFFNQNIYERRvnlNRLRRQVSMVHPKPNLFP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 hMTVLDNTAFGMELAG-TPAQERQEKALDALRQVGL----ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN-----GEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREY 255
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
3-281 1.64e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 129.82  E-value: 1.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   3 IKLEVKNLYKIFGEHPQRAFKYIekgltkeqilektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR 82
Cdd:PRK13651   1 MQIKVKNIVKIFNKKLPTELKAL-------------------DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDT 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  83 GQVLIDGVDIARISDAELREVR--------------------RKKIAMVFQsFA--LMPHMTVLDNTAFGMELAGTPAQE 140
Cdd:PRK13651  62 GTIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikkikeiRRRVGVVFQ-FAeyQLFEQTIEKDIIFGPVSMGVSKEE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 141 RQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIV 219
Cdd:PRK13651 141 AKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTII 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 220 FISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN----------PAN--DYVRTFF-RGVDISHVFSAKDIAR 281
Cdd:PRK13651 220 LVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDnkfliennmePPKllNFVNKLEkKGIDVPKVTSIEELAS 294
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
44-254 2.87e-34

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 127.58  E-value: 2.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAEL---REVRRKKIAMVFqSFalmph 120
Cdd:PRK13548  18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAVLPQHSSLSF-PF----- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 mTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAH-AYPdELSGGMRQRVGLARALA------INPDILLMDEAFS 193
Cdd:PRK13548  92 -TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 194 ALDPL--IRTeMQdeLVK-LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13548 170 ALDLAhqHHV-LR--LARqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
44-257 3.83e-34

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: 126.50  E-value: 3.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIariSDAELREVRRKKIAMVFQSFALMPHMTV 123
Cdd:cd03218   16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPMHKRARLGIGYLPQEASIFRKLTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03218   93 EENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 204 QDELVKLQakhQRTI-VFIS-HDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:cd03218  173 QKIIKILK---DRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
32-256 4.19e-34

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 127.03  E-value: 4.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  32 EQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDaelREVRR 105
Cdd:PRK11300   3 QPLLSVSGLMmrfgglLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG---HQIAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 106 KKIAMVFQSFALMPHMTVLDN----------TAFGMELAGTPA-----QERQEKALDALRQVGLENYAHAYPDELSGGMR 170
Cdd:PRK11300  80 MGVVRTFQHVRLFREMTVIENllvaqhqqlkTGLFSGLLKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239

                 ....*.
gi 493864995 251 EILNNP 256
Cdd:PRK11300 240 EIRNNP 245
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
44-284 6.05e-34

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 133.06  E-value: 6.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQS--FALMPHM 121
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPRQ 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGT-PAQERQEKALDALRQVGLE-NYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDIShvfsakDI 279
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA------DP 572

                 ....*
gi 493864995 280 ARRTP 284
Cdd:PRK10261 573 SRQRP 577
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
44-284 1.04e-33

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 132.67  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----------VDIARISDAELREVRRKKIAMVFQ 113
Cdd:PRK10261  32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGADMAMIFQ 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 114 S--FALMPHMTVLDNTAFGMELAGTPAQERQ----EKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASREEAmveaKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
                        250
                 ....*....|....*..
gi 493864995 268 VDISHVFSAKDIARRTP 284
Cdd:PRK10261 272 VPQLGAMKGLDYPRRFP 288
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1-241 1.83e-33

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: 124.85  E-value: 1.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   1 MAIKLEVKNLYKIFGEHPQRafkyiekgltkeqilektGLSL-GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE 79
Cdd:COG4778    1 MTTLLEVENLSKTFTLHLQG------------------GKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYL 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  80 PTRGQVLID----GVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGL- 154
Cdd:COG4778   63 PDSGSILVRhdggWVDLAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLp 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 155 ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP--------LIRtemqdelvklQAKHQ-RTIVFISHDL 225
Cdd:COG4778  143 ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanravvveLIE----------EAKARgTAIIGIFHDE 212
                        250
                 ....*....|....*.
gi 493864995 226 DEAMRIGDRIAIMQNG 241
Cdd:COG4778  213 EVREAVADRVVDVTPF 228
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
44-244 2.33e-33

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: 124.24  E-value: 2.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMpHMTV 123
Cdd:cd03245   20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLF-YGTL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTpaqerqEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03245   95 RDNITLGAPLADD------ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 193 SALDplIRTEMQ--DELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
Cdd:cd03245  169 SAMD--MNSEERlkERLRQLLG--DKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
cbiO PRK13645
energy-coupling factor transporter ATPase;
43-255 4.79e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 125.51  E-value: 4.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-ARISdaELREVR--RKKIAMVFQ--SFAL 117
Cdd:PRK13645  26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLK--KIKEVKrlRKEIGLVFQfpEYQL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 MPHmTVLDNTAFGMELAGTPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
44-244 5.80e-33

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: 122.71  E-value: 5.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAelrevrRKKIAMVFQSFALMPHMTV 123
Cdd:cd03268   16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIGALIEAPGFYPNLTA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNtafgMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03268   90 REN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 493864995 204 QDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03268  166 RELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
44-254 8.55e-33

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: 123.66  E-value: 8.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI------DGVDIARIsdaelrevrRKKIAMVFQSFA- 116
Cdd:COG1119   19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWEL---------RKRIGLVSPALQl 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 117 -LMPHMTVLDN--TAF--GMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:COG1119   90 rFPRDETVLDVvlSGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG1119  170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
45-254 1.37e-32

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 129.69  E-value: 1.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARIsdaELREVRRKkIAMVFQSFALMPHmTVL 124
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVRRQ-LGVVLQNGRLMSG-SIF 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  125 DNTAFGmelagtpAQERQEKALDALRQVGLENYAHAYP-------DE----LSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:TIGR03797 545 ENIAGG-------APLTLDEAWEAARMAGLAEDIRAMPmgmhtviSEgggtLSGGQRQRLLIARALVRKPRILLFDEATS 617
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995  194 ALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR03797 618 ALDNRTQAIVSESLERLKV----TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
44-254 1.38e-32

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: 128.38  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEPTRGQVLI----------------DG--------------VD 91
Cdd:TIGR03269  16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGepcpvcggtlepeeVD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   92 IARISDAELREVRrKKIAMVFQ-SFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMR 170
Cdd:TIGR03269  96 FWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPD 254

                  ....
gi 493864995  251 EILN 254
Cdd:TIGR03269 255 EVVA 258
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
44-257 1.58e-32

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: 122.40  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdAElrEVRRKKIAMVFQSFALMPHMTV 123
Cdd:COG0410   19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP-PH--RIARLGIGYVPEGRRIFPSLTV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQ--EKALDA-------LRQVGlenyahaypDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:COG0410   96 EENLLLGAYARRDRAEVRAdlERVYELfprlkerRRQRA---------GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 195 LDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:COG0410  167 LAPLIVEEIFEIIRRLNREGV-TILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
cbiO PRK13643
energy-coupling factor transporter ATPase;
46-253 1.85e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 123.69  E-value: 1.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIARISDAELREVR--RKKIAMVFQ-SFALMPHMT 122
Cdd:PRK13643  24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKEIKpvRKKVGVVFQfPESQLFEET 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 123 VLDNTAFGMELAGTPAQERQEKALDALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 202 EMqdeLVKLQAKHQ--RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13643 182 EM---MQLFESIHQsgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
44-253 2.06e-32

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 128.30  E-value: 2.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIArisDAELREVRRKkIAMVFQSFALMPHmTV 123
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA---DYTLASLRRQ-VALVSQDVVLFND-TI 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  124 LDNTAFGmelagTPAQERQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR02203 423 ANNIAYG-----RTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEAT 497
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995  193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR02203 498 SALDNESERLVQAALERLM--QGRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNELL 555
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
34-253 3.61e-32

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 122.04  E-value: 3.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  34 ILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKK 107
Cdd:PRK11231   2 TLRTENLTVGygtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL----ARR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 108 IAMVFQSFALMPHMTVLDNTAFG----MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINP 183
Cdd:PRK11231  78 LALLPQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
44-266 3.68e-32

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 123.70  E-value: 3.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-PTR---GQVLIDGVDIARISDAELREVRRKKIAMVFQS--FAL 117
Cdd:PRK11022  23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 MPHMTVldntAFGMELA-----GTPAQERQEKALDALRQVGLENYA---HAYPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK11022 103 NPCYTV----GFQIMEAikvhqGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
5-244 3.72e-32

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 122.12  E-value: 3.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGehpqrafkyiekgltKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG1101    2 LELKNLSKTFN---------------PGTVNEKRAL----DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGS 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARISDAElrevRRKKIAMVFQSfALM---PHMTVLDNTA--------FGMELAGTPAQERQEKALDALRQVG 153
Cdd:COG1101   63 ILIDGKDVTKLPEYK----RAKYIGRVFQD-PMMgtaPSMTIEENLAlayrrgkrRGLRRGLTKKRRELFRELLATLGLG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 154 LENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPliRT-----EMQDELVKlqaKHQRTIVFISHDLDEA 228
Cdd:COG1101  138 LENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTaalvlELTEKIVE---ENNLTTLMVTHNMEQA 212
                        250
                 ....*....|....*.
gi 493864995 229 MRIGDRIAIMQNGEVV 244
Cdd:COG1101  213 LDYGNRLIMMHEGRII 228
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
44-244 4.84e-32

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: 120.05  E-value: 4.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIArisdaelREVRRKKIAMVFQsfalmpHM-- 121
Cdd:cd03226   16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQ------DVdy 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 -----TVLDNTAFGMELAGtpaqERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03226   83 qlftdSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493864995 197 PlIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03226  159 Y-KNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
43-253 5.15e-32

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 127.38  E-value: 5.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSfALMPHMT 122
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQD-AGLFNRS 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 123 VLDNTAFG--------MELAGTPAQ-----ERQEKALDALrqVGLENYAhaypdeLSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK13657 425 IEDNIRVGrpdatdeeMRAAAERAQahdfiERKPDGYDTV--VGERGRQ------LSGGERQRLAIARALLKDPPILILD 496
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 190 EAFSALDplIRTEmqdelVKLQA-----KHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13657 497 EATSALD--VETE-----AKVKAaldelMKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDELV 557
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
45-244 5.38e-32

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 127.53  E-value: 5.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVL 124
Cdd:PRK10535  25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493864995 205 DELVKLQAKHQrTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
Cdd:PRK10535 185 AILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
44-257 1.67e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 120.61  E-value: 1.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIariSDAELREVRrKKIAMVFQS-----FAlm 118
Cdd:PRK13647  21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVR-SKVGLVFQDpddqvFS-- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 phMTVLDNTAFG---MELAGTPAQERQEKALDAlrqVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:PRK13647  95 --STVWDDVAFGpvnMGLDKDEVERRVEEALKA---VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 196 DPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPdEILNNPA 257
Cdd:PRK13647 170 DPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
45-253 9.35e-31

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: 123.78  E-value: 9.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVrrkkIAMVfqsfalmPHMTVL 124
Cdd:COG5265  375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA----IGIV-------PQDTVL 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 ------DNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILL 187
Cdd:COG5265  444 fndtiaYNIAYGRPDAS------EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILI 517
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 188 MDEAFSALDPliRTEM--QDELVKLqAKHQRTIVfISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:COG5265  518 FDEATSALDS--RTERaiQAALREV-ARGRTTLV-IAHRLSTIVD-ADEILVLEAGRIVERGTHAELL 580
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
45-256 1.05e-30

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 124.06  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMPHmTVL 124
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SVR 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  125 DNTAFGmeLAGTPAQERQEKALDALRQVGLENYAHAYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDp 197
Cdd:TIGR00958 573 ENIAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995  198 lirTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:TIGR00958 650 ---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
44-262 1.98e-30

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 122.51  E-value: 1.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRLIEP----TRGQVLIDGVDIARISDAELREVRRKKIAMVFQS--FA 116
Cdd:PRK15134  25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpmVS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 117 LMPHMTVLDNTAfgmELAGTPAQERQEKA----LDALRQVGLENYA---HAYPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK15134 105 LNPLHTLEKQLY---EVLSLHRGMRREAArgeiLNCLDRVGIRQAAkrlTDYPHQLSGGERQRVMIAMALLTRPELLIAD 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
32-243 4.67e-30

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: 114.07  E-value: 4.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  32 EQILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaeLREVRRKKIA 109
Cdd:cd03215    2 EPVLEVRGLSVKgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---PRDAIRAGIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 110 MV---FQSFALMPHMTVLDNTAFgmelagtpaqerqekaldalrqvglenyahayPDELSGGMRQRVGLARALAINPDIL 186
Cdd:cd03215   79 YVpedRKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:cd03215  127 ILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
59-257 9.17e-30

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 117.67  E-value: 9.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaRI-SDAELR-----EVRRkkIAMVFQSFALMPHMTVLDNTAFGMe 132
Cdd:PRK11144  29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG----RVlFDAEKGiclppEKRR--IGYVFQDARLFPHYKVRGNLRYGM- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 133 lagtpAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQA 212
Cdd:PRK11144 102 -----AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 493864995 213 KHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
39-249 1.84e-29

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: 113.74  E-value: 1.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaeLREVRRkKIAMVFQsfalm 118
Cdd:cd03244   15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRS-RISIIPQ----- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 phmtvlDNTAFgmelAGT------PAQERQEKAL-DALRQVGLENYAHAYPDEL-----------SGGMRQRVGLARALA 180
Cdd:cd03244   86 ------DPVLF----SGTirsnldPFGEYSDEELwQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 181 INPDILLMDEAFSALDP--------LIRTEMQDelvklqakhqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
Cdd:cd03244  156 RKSKILVLDEATASVDPetdaliqkTIREAFKD----------CTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
59-256 2.49e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 114.90  E-value: 2.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREVRrKKIAMVFQS-----FAlmphMTVLDNTAFGMEL 133
Cdd:PRK13652  35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---EPITKENIREVR-KFVGLVFQNpddqiFS----PTVEQDIAFGPIN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 134 AGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK 213
Cdd:PRK13652 107 LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 493864995 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK13652 187 YGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
44-243 3.12e-29

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: 111.54  E-value: 3.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFALmphmtv 123
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----DHVGYLPQDDEL------ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 ldntafgmeLAGTPAqerqekaldalrqvglENYahaypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03246   88 ---------FSGSIA----------------ENI-------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493864995 204 QDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEV 243
Cdd:cd03246  136 NQAIAALKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
44-256 4.23e-29

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 116.86  E-value: 4.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFAL------ 117
Cdd:PRK09536  19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA----SRRVASVPQDTSLsfefdv 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 --------MPHMTVLDntafGMELAGTPAQERqekaldALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK09536  95 rqvvemgrTPHRSRFD----TWTETDRAAVER------AMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 190 EAFSALD--PLIRTEmqdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK09536 165 EPTASLDinHQVRTL---ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
48-260 4.60e-29

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 115.39  E-value: 4.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIARISDAELREVRRKKIAMVFQ--SFALMPHM 121
Cdd:COG4170   27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQepSSCLDPSA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGM---ELAGT---PAQERQEKALDALRQVGLENYAH---AYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:COG4170  107 KIGDQLIEAIpswTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQPRLLIADEPT 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
Cdd:COG4170  187 NAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPY 254
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
39-260 7.18e-29

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 114.82  E-value: 7.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIARISDAELREVRRKKIAMVFQS- 114
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRAEQISMIFQDp 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 115 -FALMPHMTVLDNTafgME-------LAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDIL 186
Cdd:PRK09473 107 mTSLNPYMRVGEQL---MEvlmlhkgMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
44-252 9.67e-29

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 118.69  E-value: 9.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIarisDAELREVRRKKIAMVfQSFALMPHMTV 123
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIATRRRVGYMS-QAFSLYGELTV 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493864995 204 QDELVKLQAKHQRTIvFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF033858 437 WRLLIELSREDGVTI-FIStHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
49-235 1.99e-28

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 111.02  E-value: 1.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
Cdd:PRK10584  31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 129 FGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
                        170       180
                 ....*....|....*....|....*..
gi 493864995 209 KLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQLAARCDRRL 217
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
5-247 2.15e-28

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: 111.09  E-value: 2.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFgehpqRAFKYIEKGLTKEQILEKTGLS---LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT 81
Cdd:cd03220    1 IELENVSKSY-----PTYKGGSSSLKKLGILGRKGEVgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  82 RGQVLIDGvdiaRISdaelrevrrkkiAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAY 161
Cdd:cd03220   76 SGTVTVRG----RVS------------SLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLP 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:cd03220  140 VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKG 218

                 ....*.
gi 493864995 242 EVVQVG 247
Cdd:cd03220  219 KIRFDG 224
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
44-253 2.67e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 112.25  E-value: 2.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIARISDAELREvrrkKIAMVFQS-----FA 116
Cdd:PRK13636  22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRE----SVGMVFQDpdnqlFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 117 lmphMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13636  98 ----ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
44-225 7.44e-28

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: 114.77  E-value: 7.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrkKIAMVFQSFALMPHMTV 123
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-----RRVSVCAQDAHLFDTTV 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  124 LDNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR02868 426 RENLRLARPDAT------DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
                         170       180       190
                  ....*....|....*....|....*....|...
gi 493864995  193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDL 225
Cdd:TIGR02868 500 EHLDAETADELLEDL--LAALSGRTVVLITHHL 530
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
43-238 7.57e-28

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: 115.08  E-value: 7.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSfalmPHM- 121
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQH----PFLf 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  122 --TVLDNTAFGmELAGTPAQERQekaldALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLM 188
Cdd:TIGR02857 409 agTIAENIRLA-RPDASDAEIRE-----ALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLL 482
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 493864995  189 DEAFSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIM 238
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRL-ALAALADRIVVL 529
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
49-266 8.06e-28

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 110.49  E-value: 8.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLI---EPTRGQVLIDGVDIARISDAElREVR--RKKIAMVFQSFALMPHMTV 123
Cdd:PRK09984  25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLA-RDIRksRANTGYIFQQFNLVNRLSV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGmELAGTP---------AQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:PRK09984 104 LENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINR 254
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
44-243 1.74e-27

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: 108.71  E-value: 1.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREVRRkKIAMVFQSFALMPHmTV 123
Cdd:cd03248   30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQYEHKYLHS-KVSLVGQEPVLFAR-SL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGmeLAGTPAQERQEKALDALRQVGLENYAHAYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03248  105 QDNIAYG--LQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493864995 197 plIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEV 243
Cdd:cd03248  183 --AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
16-249 2.19e-27

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: 114.73  E-value: 2.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    16 EHPQRAFKYIEKGLTKeqILEKTGLSlGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARI 95
Cdd:TIGR01257  921 ELPGLVPGVCVKNLVK--IFEPSGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN 997
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    96 SDAElrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGL 175
Cdd:TIGR01257  998 LDAV-----RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995   176 ARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
44-254 3.12e-27

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: 113.30  E-value: 3.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVrrkkIAMVFQSFALMPHmTV 123
Cdd:COG4618  348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELFDG-TI 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTA-FGmelAGTPaqerqEKALDALRQVGlenyAHA----YPD-----------ELSGGMRQRVGLARALAINPDILL 187
Cdd:COG4618  423 AENIArFG---DADP-----EKVVAAAKLAG----VHEmilrLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVV 490
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 188 MDEAFSALDP-----LIRTemqdelVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:COG4618  491 LDEPNSNLDDegeaaLAAA------IRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
33-263 3.24e-27

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 108.63  E-value: 3.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  33 QILEKTGLSLG-----VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRL---IEPTRGQVLIDGVDIArisdaeLREV 103
Cdd:PRK10418   3 QQIELRNIALQaaqplVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVA------PCAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 104 RRKKIAMVFQS--FALMPHMTVLDNTAFGMELAGTPAQERQekALDALRQVGLENYA---HAYPDELSGGMRQRVGLARA 178
Cdd:PRK10418  77 RGRKIATIMQNprSAFNPLHTMHTHARETCLALGKPADDAT--LTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH 234

                 ....*
gi 493864995 259 DYVRT 263
Cdd:PRK10418 235 AVTRS 239
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
45-255 4.13e-27

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 113.00  E-value: 4.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREvrrkKIAMVFQSFALMPHmTVL 124
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ----AISVVSQRVHLFSA-TLR 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAfgmeLAGTPAQErqEKALDALRQVGLENyaHAYPDE------------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK11160 432 DNLL----LAAPNASD--EALIEVLQQVGLEK--LLEDDKglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPT 503
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 193 SALDPliRTEMQdeLVKLQAKH--QRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK11160 504 EGLDA--ETERQ--ILELLAEHaqNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
54-244 4.32e-27

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 107.27  E-value: 4.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFGMEL 133
Cdd:PRK10908  28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTVYDNVAIPLII 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 134 AGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAK 213
Cdd:PRK10908 107 AGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEGILRLFEE 182
                        170       180       190
                 ....*....|....*....|....*....|....
gi 493864995 214 HQR---TIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK10908 183 FNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
59-268 4.85e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 108.64  E-value: 4.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  59 IMGLSGSGKSTMVRLLNRLIEPTRG-----QVLIDGVDIARISDaeLREVRRKkIAMVFQSFALMPhMTVLDNTAFGMEL 133
Cdd:PRK14271  52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRR-VGMLFQRPNPFP-MSIMDNVLAGVRA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 134 AG-TPAQERQEKALDALRQVGL----ENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTEMQDELV 208
Cdd:PRK14271 128 HKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP-TTTEKIEEFI 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 209 KLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
Cdd:PRK14271 207 RSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
35-227 6.61e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 107.11  E-value: 6.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDaelrEVRRKKIAM 110
Cdd:PRK10247  10 LQNVGYLAGdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP----EIYRQQVSY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 111 VFQSFALMPHmTVLDNTAFGMELAGtpaQERQEKAL-DALRQVGL-ENYAHAYPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:PRK10247  86 CAQTPTLFGD-TVYDNLIFPWQIRN---QQPDPAIFlDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493864995 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDE 227
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
32-253 1.75e-26

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 107.97  E-value: 1.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaelrEVRRKKIAMV 111
Cdd:PRK13537  11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-----RHARQRVGVV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 112 FQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:PRK13537  86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 192 FSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
44-254 2.06e-26

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 111.57  E-value: 2.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaelREVRRKKIAMVFQSFALMpHMTV 123
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP----REVLANSVAMVDQDIFLF-EGTV 569
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  124 LDNTAFgmeLAGTPAQERQEKAL-DA------LRQVGlenyahAYPDEL-------SGGMRQRVGLARALAINPDILLMD 189
Cdd:TIGR03796 570 RDNLTL---WDPTIPDADLVRACkDAaihdviTSRPG------GYDAELaegganlSGGQRQRLEIARALVRNPSILILD 640
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995  190 EAFSALDPlirtemQDELVKLQAKHQR--TIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR03796 641 EATSALDP------ETEKIIDDNLRRRgcTCIIVAHRL-STIRDCDEIIVLERGKVVQRGTHEELWA 700
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
42-247 5.51e-26

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: 104.28  E-value: 5.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLIDGVDIARisdaelrEVRRKKIAMVFQSFALM 118
Cdd:cd03234   21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP-------DQFQKCVAYVRQDDILL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 PHMTVLDNTAFGMELAG----TPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03234   94 PGLTVRETLTYTAILRLprksSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493864995 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03234  174 LDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
44-254 1.21e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 106.07  E-value: 1.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI---ARISdaelrevrRKKIAMVFQSFALMPH 120
Cdd:PRK13536  57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparARLA--------RARIGVVPQFDNLDLE 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 MTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
Cdd:PRK13536 129 FTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 201 TEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK13536 209 HLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
43-260 5.34e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 102.70  E-value: 5.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-----VDIARISDAELREVRRKKIAMVFQSFAL 117
Cdd:PRK11701  21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTEWGFVHQHPRD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 MPHMTVLDNTAFGMELAGTPAQ---ERQEKALDALRQVGLE-NYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK11701 101 GLRMQVSAGGNIGERLMAVGARhygDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTG 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
Cdd:PRK11701 181 GLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPY 247
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
48-256 5.68e-25

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 102.56  E-value: 5.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARI-SDAELREVrrkkiAMVFQSFALMPHMTVLDN 126
Cdd:PRK10575  31 SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsSKAFARKV-----AYLPQQLPAAEGMTVREL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 127 TAFGME----LAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:PRK10575 106 VAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
45-254 7.44e-25

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 106.26  E-value: 7.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiarISDAELREVrRKKIAMVFQSFALMpHMTVL 124
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASL-RNQVALVSQNVHLF-NDTIA 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFG---------MELAGTPAQ-----ERQEKALDALrqVGlENYAhaypdELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:PRK11176 435 NNIAYArteqysreqIEEAARMAYamdfiNKMDNGLDTV--IG-ENGV-----LLSGGQRQRIAIARALLRDSPILILDE 506
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 191 AFSALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQ--KNRTSLVIAHRL-STIEKADEILVVEDGEIVERGTHAELLA 567
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
32-260 8.04e-25

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: 101.83  E-value: 8.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   32 EQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-----VDIARISDAEL 100
Cdd:TIGR02323   1 KPLLQVSGLSksygggKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  101 REVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQER---QEKALDALRQVGLE-NYAHAYPDELSGGMRQRVGLA 176
Cdd:TIGR02323  81 RRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYgniRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240

                  ....
gi 493864995  257 ANDY 260
Cdd:TIGR02323 241 QHPY 244
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
29-253 1.30e-24

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 101.60  E-value: 1.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  29 LTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDaelREVRRKkI 108
Cdd:PRK10253   8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---KEVARR-I 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 109 AMVFQSFALMPHMTVLDNTAFG----MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPD 184
Cdd:PRK10253  84 GLLAQNATTPGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
44-247 2.73e-24

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: 98.78  E-value: 2.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEP-TRGQVLIDGVDIARISdaelrevRRKKIAMVFQSFALMPHM 121
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLDKRS-------FRKIIGYVPQDDILHPTL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGtpaqerqekaldalrqvglenyahaypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDP---- 197
Cdd:cd03213   98 TVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSssal 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493864995 198 -LIRTemqdeLVKLqAKHQRTIVFISHDL-DEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03213  149 qVMSL-----LRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
34-252 4.01e-24

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 103.94  E-value: 4.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  34 ILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIARISDAelrevRRKKIA 109
Cdd:COG1129  256 VLEVEGLSVGgvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDA-----IRAGIA 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 110 MV---FQSFALMPHMTVLDNTAFG-MELAGT-----PAQERQ--EKALDALR--------QVGlenyahaypdELSGGMR 170
Cdd:COG1129  331 YVpedRKGEGLVLDLSIRENITLAsLDRLSRgglldRRRERAlaEEYIKRLRiktpspeqPVG----------NLSGGNQ 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 171 QRVGLARALAINPDILLMDE--------AfsaldpliRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:COG1129  401 QKVVLAKWLATDPKVLILDEptrgidvgA--------KAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGR 471
                        250
                 ....*....|
gi 493864995 243 VVQVGTPDEI 252
Cdd:COG1129  472 IVGELDREEA 481
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
44-268 6.95e-24

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 101.03  E-value: 6.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL----NRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSfalmP 119
Cdd:PRK15093  23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE----P 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 HMTVLDNTAFGMELA---------GTPAQE---RQEKALDALRQVGLENYA---HAYPDELSGGMRQRVGLARALAINPD 184
Cdd:PRK15093  99 QSCLDPSERVGRQLMqnipgwtykGRWWQRfgwRKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPR 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQAL 258

                 ....
gi 493864995 265 FRGV 268
Cdd:PRK15093 259 IRAI 262
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
44-238 1.16e-23

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 96.92  E-value: 1.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiarisdaelREVRRKKIAMVFQSFAL---MPh 120
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVpdsLP- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 MTVLDNTAFG----MELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:NF040873  72 LTVRDLVAMGrwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493864995 197 PLIRTEMqDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIM 238
Cdd:NF040873 152 AESRERI-IALLAEEHARGATVVVVTHDLELVRRA-DPCVLL 191
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
44-255 1.89e-23

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 98.04  E-value: 1.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaeLREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK10895  19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQEASIFRRLSV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQE-RQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
Cdd:PRK10895  96 YDNLMAVLQIRDDLSAEqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 203 mqdelVKLQAKHQRT----IVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PRK10895 176 -----IKRIIEHLRDsglgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
44-247 4.09e-23

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: 95.07  E-value: 4.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIArisdaELREVRRKKIAMVFQSfalmPHM-- 121
Cdd:cd03247   18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS-----DLEKALSSLISVLNQR----PYLfd 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 -TVLDNtafgmelagtpaqerqekaldalrqVGLEnyahaypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPliR 200
Cdd:cd03247   89 tTLRNN-------------------------LGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDP--I 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493864995 201 TEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
Cdd:cd03247  133 TERQLLSLIFEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
32-253 2.72e-22

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 95.46  E-value: 2.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  32 EQILEktGLSLgvkDASLAIEEGeifvIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIARISDAELREvrrkKIA 109
Cdd:PRK13638  14 EPVLK--GLNL---DFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQ----QVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 110 MVFQSFALMPHMTVLD-NTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:PRK13638  81 TVFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 189 DEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13638 161 DEPTAGLDPAGRTQMI-AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
25-286 7.33e-22

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 97.16  E-value: 7.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  25 IEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVr 104
Cdd:PRK09700   2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 105 rkKIAMVFQSFALMPHMTVLDNTAFGMELA----GTPA---QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLAR 177
Cdd:PRK09700  81 --GIGIIYQELSVIDELTVLENLYIGRHLTkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 178 ALAINPDILLMDEAFSALdplirteMQDELVKLQA------KHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL-------TNKEVDYLFLimnqlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 493864995 252 IlnnpANDYVRTFFRGVDISHVFSAKDIARRTPNG 286
Cdd:PRK09700 232 V----SNDDIVRLMVGRELQNRFNAMKENVSNLAH 262
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
48-253 3.10e-21

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 91.83  E-value: 3.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRL--IEPTRGQVLIDGVDIARISDAELREVRrkkiAMVFQSFALMPHMTVLD 125
Cdd:COG4138   16 SAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 126 NTAFGMelAGTPAQERQEKALDAL-RQVGLENYAHAYPDELSGGMRQRVGLARAL-----AINPD--ILLMDEAFSALDp 197
Cdd:COG4138   89 YLALHQ--PAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD- 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 198 lIRTE-MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:COG4138  166 -VAQQaALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
30-252 6.15e-21

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 94.32  E-value: 6.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  30 TKEQILEKTGLSL-------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaeLRE 102
Cdd:COG3845  253 PGEVVLEVENLSVrddrgvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRE 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 103 VRRKKIAMV---FQSFALMPHMTVLDNTAFG----MELAGTP------AQERQEKALDAL--RQVGLENYAHAypdeLSG 167
Cdd:COG3845  330 RRRLGVAYIpedRLGRGLVPDMSVAENLILGryrrPPFSRGGfldrkaIRAFAEELIEEFdvRTPGPDTPARS----LSG 405
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 168 GMRQRVGLARALAINPDILLMDEAFSALDP----LIRtemqDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:COG3845  406 GNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIH----QRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480

                 ....*....
gi 493864995 244 VQVGTPDEI 252
Cdd:COG3845  481 VGEVPAAEA 489
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
44-249 7.38e-21

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: 89.78  E-value: 7.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARIsdaELREVRRkkiamvfqSFALMPHMTV 123
Cdd:cd03369   24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRS--------SLTIIPQDPT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LdntafgmeLAGT------PAQERQEKAL-DALR-QVGLENyahaypdeLSGGMRQRVGLARALAINPDILLMDEAFSAL 195
Cdd:cd03369   93 L--------FSGTirsnldPFDEYSDEEIyGALRvSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 196 D--------PLIRTEMQDElvklqakhqrTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
Cdd:cd03369  157 DyatdaliqKTIREEFTNS----------TILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
5-244 1.09e-20

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: 90.08  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   5 LEVKNLYKIFGEHPQRA-FKYIEKGLTKEQILEKTGLslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
Cdd:cd03267    1 IEVSNLSKSYRVYSKEPgLIGSLKSLFKRKYREVEAL----KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  84 QVLIDGVDiarisDAELREVRRKKIAMVF-------------QSFALMPHMTVLDNTAFgmelagtpaQERQEKALDALR 150
Cdd:cd03267   77 EVRVAGLV-----PWKRRKKFLRRIGVVFgqktqlwwdlpviDSFYLLAAIYDLPPARF---------KKRLDELSELLD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 151 qvgLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMR 230
Cdd:cd03267  143 ---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEA 219
                        250
                 ....*....|....
gi 493864995 231 IGDRIAIMQNGEVV 244
Cdd:cd03267  220 LARRVLVIDKGRLL 233
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
37-253 1.13e-20

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: 94.63  E-value: 1.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrkkiamvFQsFA 116
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR----------FK-IT 1363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   117 LMPHMTVLDNTAFGMELagTP-AQERQEKALDALRQVGLENYAHAYPDE-----------LSGGMRQRVGLARALAINPD 184
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNL--DPfSQYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTK 1441
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995   185 ILLMDEAFSALD--------PLIRTEMQDelvklqakhqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR00957 1442 ILVLDEATAAVDletdnliqSTIRTQFED----------CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLL 1507
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
29-267 1.61e-20

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 89.55  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  29 LTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiarISDAELREVRRKKI 108
Cdd:PRK11614   6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAKIMREAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 109 AMVFQSFALMPHMTVLDNTAFGMELAG-TPAQERQEKALDALRQvgLENYAHAYPDELSGGMRQRVGLARALAINPDILL 187
Cdd:PRK11614  83 AIVPEGRRVFSRMTVEENLAMGGFFAErDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 188 MDEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpANDYVRTFFRG 267
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGM-TIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL---ANEAVRSAYLG 236
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
36-242 1.72e-20

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: 88.68  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI---EPTRGQVLIDGvdiarisdaelrevrrkKIAMVF 112
Cdd:cd03250   13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALLgelEKLSGSVSVPG-----------------SIAYVS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 113 QSFALMPhMTVLDNTAFGMELAgtpaQERQEKALDA--LRQvGLENYAHAypDE---------LSGGMRQRVGLARALAI 181
Cdd:cd03250   73 QEPWIQN-GTIRENILFGKPFD----EERYEKVIKAcaLEP-DLEILPDG--DLteigekginLSGGQKQRISLARAVYS 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGE 242
Cdd:cd03250  145 DADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
48-256 4.12e-20

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 92.22  E-value: 4.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIE--PTRGQVLIDGVdiarisdaELREVR----RKKIAMVFQSfALMPHM 121
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTS---LLNALLGflPYQGSLKINGI--------ELRELDpeswRKHLSWVGQN-PQLPHG 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:PRK11174 438 TLRDNVLLGNPDAS------DEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 191 AFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK11174 512 PTASLD--AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
44-242 1.27e-19

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 90.80  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIarisDAELREVRRKKIAMVFQSFALMPHMtv 123
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV----TAEQPEDYRKLFSAVFTDFHLFDQL-- 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 ldntafgMELAGTPAQERQ-EKALDAL---RQVGLENYAHAYPDeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:PRK10522 413 -------LGPEGKPANPALvEKWLERLkmaHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 493864995 200 RTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGE 242
Cdd:PRK10522 485 RREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
45-256 1.51e-19

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 90.54  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSFALMPHmTVL 124
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR----SRLAVVSQTPFLFSD-TVA 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAgTPAQERQEKAL-----DALR-------QVGLENYAhaypdeLSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK10789 407 NNIALGRPDA-TQQEIEHVARLasvhdDILRlpqgydtEVGERGVM------LSGGQKQRISIARALLLNAEILILDDAL 479
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 193 SALDPliRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK10789 480 SAVDG--RTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
48-197 2.20e-19

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: 85.49  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIArisdaELREVRRKKIAMVFQSFALMPHMTVLDNT 127
Cdd:TIGR01189  20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPELSALENL 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  128 AFGMELAGTpaqeRQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:TIGR01189  95 HFWAAIHGG----AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
6-255 2.95e-19

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 87.84  E-value: 2.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   6 EVKNLYKIFGEHPQRA-FKYIEKGLTKEQILEKTGlslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
Cdd:COG4586    3 EVENLSKTYRVYEKEPgLKGALKGLFRREYREVEA----VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  85 VLIDGVDIARisdaelREVR-RKKIAMVF-QSFALMPHMTVLDNTAFGMELAGTPAQERQEKaLDALRQV-GLENYAHAY 161
Cdd:COG4586   79 VRVLGYVPFK------RRKEfARRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKR-LDELVELlDLGELLDTP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
Cdd:COG4586  152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
                        250
                 ....*....|....
gi 493864995 242 EVVQVGTPDEILNN 255
Cdd:COG4586  232 RIIYDGSLEELKER 245
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
11-295 7.82e-19

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 88.57  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   11 YKIFGEHPQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP---TRGQVLI 87
Cdd:TIGR00955   8 SDVFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   88 DGVDIarisdaELREVRRKKiAMVFQSFALMPHMTVLDNTAFGMEL---AGTPAQERQEKALDALRQVGLENYAH---AY 161
Cdd:TIGR00955  88 NGMPI------DAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANtriGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  162 PDE---LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
Cdd:TIGR00955 161 PGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  239 QNGEVVQVGTPDEILN-------------NPANDYVRTfFRGVD------------ISHVFSAKDIAR---RTPNGIIRK 290
Cdd:TIGR00955 241 AEGRVAYLGSPDQAVPffsdlghpcpenyNPADFYVQV-LAVIPgsenesreriekICDSFAVSDIGRdmlVNTNLWSGK 319

                  ....*
gi 493864995  291 TPGFG 295
Cdd:TIGR00955 320 AGGLV 324
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
48-196 1.43e-18

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 83.31  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaeLREVRRKKIAMVFQSFALMPHMTVLDNT 127
Cdd:PRK13538  21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYHQDLLYLGHQPGIKTELTALENL 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 128 AFGMELAGTPaqeRQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13538  96 RFYQRLHGPG---DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
45-252 1.49e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 87.41  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVrrkKIAMVFQSFALMPHMTVL 124
Cdd:PRK15439  28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPLLFPNLSVK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGmeLAGTPAQERQEKALdaLRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
Cdd:PRK15439 105 ENILFG--LPKRQASMQKMKQL--LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLF 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493864995 205 DELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:PRK15439 181 SRIRELLAQGV-GIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
PLN03130 PLN03130
ABC transporter C family member; Provisional
48-255 1.80e-18

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 87.87  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVrrkkiamvfqsFALMPHMTVLdnt 127
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-----------LGIIPQAPVL--- 1324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  128 afgmeLAGT------PAQERQEKAL----------DALRQ--VGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PLN03130 1325 -----FSGTvrfnldPFNEHNDADLweslerahlkDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995  190 EAFSALDplIRTemqDELVklqakhQRTI---------VFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PLN03130 1400 EATAAVD--VRT---DALI------QKTIreefksctmLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
48-196 1.83e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 83.00  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIArisDAELREVrrkkIAMVFQSFALMPHMTVLDNT 127
Cdd:PRK13539  22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEA----CHYLGHRNAMKPALTVAENL 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 128 AFGMELAGTpaqeRQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:PRK13539  95 EFWAAFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
43-248 2.74e-18

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 86.52  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGVDI--ARISDAElrevrRKKIAMVFQS 114
Cdd:PRK13549  17 GVKaldNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELqaSNIRDTE-----RAGIAIIHQE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 115 FALMPHMTVLDNTAFGMELagTPA-----QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK13549  91 LALVKELSVLENIFLGNEI--TPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 190 EAFSALdplirTEMQDE----LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGT 248
Cdd:PRK13549 169 EPTASL-----TESETAvlldIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
45-259 3.48e-18

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 87.01  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIARISDAELREvRRKKIAMVFQSFALMPHmTVL 124
Cdd:PTZ00265  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKW-WRSKIGVVSQDPLLFSN-SIK 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  125 DNTAFGM-------------ELAGTPAQERQEK--------------------------------------ALDALRQVG 153
Cdd:PTZ00265  478 NNIKYSLyslkdlealsnyyNEDGNDSQENKNKrnscrakcagdlndmsnttdsneliemrknyqtikdseVVDVSKKVL 557
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  154 LENYAHAYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFIS 222
Cdd:PTZ00265  558 IHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 493864995  223 HDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
Cdd:PTZ00265  638 HRL-STIRYANTIFVLSNRERGSTVDVDIIGEDPTKD 673
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
44-223 3.72e-18

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 86.40  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQvlidgvdIARISDAElrevrrkkiaMVF---QSFalMPH 120
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR-------IARPAGAR----------VLFlpqRPY--LPL 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 121 MTVLDNTAFgmelagtPAQERQ---EKALDALRQVGLENYAH------AYPDELSGGMRQRVGLARALAINPDILLMDEA 191
Cdd:COG4178  440 GTLREALLY-------PATAEAfsdAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
                        170       180       190
                 ....*....|....*....|....*....|....
gi 493864995 192 FSALDPlirtEMQDELVKL--QAKHQRTIVFISH 223
Cdd:COG4178  513 TSALDE----ENEAALYQLlrEELPGTTVISVGH 542
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
45-253 6.03e-18

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 85.54  E-value: 6.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELrevrRKKIAMVFQSFALMPHmTVL 124
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLAD-TFL 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAgtpaqerQEKALDALRQVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK10790 433 ANVTLGRDIS-------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATA 505
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 194 ALDPLIRTEMQDELVKLqaKHQRTIVFISHDLD---EAmrigDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10790 506 NIDSGTEQAIQQALAAV--REHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHQQLL 562
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
29-250 7.91e-18

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: 84.88  E-value: 7.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   29 LTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGvdiARISDAELREVRR 105
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSG---SPLKASNIRDTER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  106 KKIAMVFQSFALMPHMTVLDNTAFGMELA------GTPAQERQEKALdaLRQVGLENYAHAYP-DELSGGMRQRVGLARA 178
Cdd:TIGR02633  78 AGIVIIHQELTLVPELSVAENIFLGNEITlpggrmAYNAMYLRAKNL--LRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995  179 LAINPDILLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEvvQVGTPD 250
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKD 224
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
48-256 8.60e-18

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 82.29  E-value: 8.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTmvrLLNRL--IEPTRGQVLIDGVDIARISDAELREVR-------RKKIAM-VFQSFAL 117
Cdd:PRK03695  16 SAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRaylsqqqTPPFAMpVFQYLTL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 mpHMTvldntafgmelAGTPAQErQEKALDAL-RQVGLENYAHAYPDELSGGMRQRVGLARAL-----AINPD--ILLMD 189
Cdd:PRK03695  93 --HQP-----------DKTRTEA-VASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 190 EAFSALDPLIRTEMqDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PRK03695 159 EPMNSLDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
83-254 1.24e-17

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 85.47  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   83 GQVLIDGVDIArisDAELREVRrKKIAMVFQSFALMpHMTVLDNTAFGMELAGTPAQERQEK--ALDALRQVGLENY--- 157
Cdd:PTZ00265 1277 GKILLDGVDIC---DYNLKDLR-NLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKfaAIDEFIESLPNKYdtn 1351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  158 AHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAI 237
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
                         170       180
                  ....*....|....*....|..
gi 493864995  238 MQN----GEVVQV-GTPDEILN 254
Cdd:PTZ00265 1431 FNNpdrtGSFVQAhGTHEELLS 1452
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
45-243 1.47e-17

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 84.35  E-value: 1.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiarisdaelrevRRKKIAMVFQSFALMPHMTVL 124
Cdd:COG0488   15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLTVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DN-------------------------TAFGMELA----------GTPAQERQEKALDALrqvGLENYAHAYP-DELSGG 168
Cdd:COG0488   80 DTvldgdaelraleaeleeleaklaepDEDLERLAelqeefealgGWEAEARAEEILSGL---GFPEEDLDRPvSELSGG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 169 MRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD---LDeamRIGDRIAIMQNGEV 243
Cdd:COG0488  157 WRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDryfLD---RVATRILELDRGKL 227
PLN03232 PLN03232
ABC transporter C family member; Provisional
48-262 1.49e-17

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 85.03  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVrrkkIAMVFQSFALMPHMTVLDNT 127
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLFSGTVRFNID 1331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  128 AFGmELAGTPAQERQEKA--LDALRQ--VGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTem 203
Cdd:PLN03232 1332 PFS-EHNDADLWEALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD--VRT-- 1406
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995  204 qDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
Cdd:PLN03232 1407 -DSLIQRTIREEFkscTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
41-263 2.27e-17

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: 84.68  E-value: 2.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDI-ARISDaelrevrrkkiamVFQSFALMP 119
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISD-------------VHQNMGYCP 2018
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   120 HMTVLDNTAFGME-------LAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR01257 2019 QFDAIDDLLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995   193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVT 2168
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
44-253 4.63e-17

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: 79.11  E-value: 4.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLI-----EPTRGQVLIDGVDIArisDAELREVRRKKIAMVFQSFALM 118
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKST---LAKTIMghpkyEVTEGEILFKGEDIT---DLPPEERARLGIFLAFQYPPEI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 PHMTVLDntaFgmelagtpaqerqekaldaLRQVGlenyahaypDELSGGMRQRVGLARALAINPDILLMDEAFSALDpL 198
Cdd:cd03217   90 PGVKNAD---F-------------------LRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-I 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 199 IRTEMQDELVKLQAKHQRTIVFISH-----DLDEAmrigDRIAIMQNGEVVQVGTPDEIL 253
Cdd:cd03217  138 DALRLVAEVINKLREEGKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKELAL 193
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
48-196 6.85e-17

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 78.69  E-value: 6.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREvrrkkIAMVFQSFALMPHMTVLDNT 127
Cdd:cd03231   20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG-----LLYLGHAPGIKTTLSVLENL 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 128 AFGMELAGTpaqerqEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
Cdd:cd03231   95 RFWHADHSD------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
47-244 8.77e-17

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 81.88  E-value: 8.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIARISDAelreVR---------RKKIAMVfqsf 115
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDA----IRagimlcpedRKAEGII---- 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 116 almPHMTVLDNTAFGMELAGTPA----QERQEKALdALRQVGLENYAHAYPDE----LSGGMRQRVGLARALAINPDILL 187
Cdd:PRK11288 344 ---PVHSVADNINISARRHHLRAgcliNNRWEAEN-ADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVIL 419
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 188 MDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
46-253 9.83e-17

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 79.47  E-value: 9.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiarisdaelrevrrkKIAMVFQSFALMPHMTVLD 125
Cdd:PRK13546  42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------------EVSVIAISAGLSGQLTGIE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 126 NTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpliRTEMQD 205
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFAQK 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 493864995 206 ELVKLQ--AKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13546 182 CLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
43-245 3.10e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 80.34  E-value: 3.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREvrrKKIAMVFQSFALMP 119
Cdd:PRK11288  16 GVKaldDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA---AGVAIIYQELHLVP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 HMTVLDN-------TAFGMELAGTPAQErqekALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK11288  93 EMTVAENlylgqlpHKGGIVNRRLLNYE----AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 193 SAL-----DPLIR--TEMQDElvklqakhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:PRK11288 169 SSLsareiEQLFRviRELRAE--------GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
45-250 7.82e-16

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 76.26  E-value: 7.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDiarISDAELREVRRKKIAMVFQSFALMPHMT 122
Cdd:COG0396   17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGED---ILELSPDERARAGIFLAFQYPVEIPGVS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 123 VLD--NTAFG-MELAGTPAQERQEKALDALRQVGL-ENYAHAYPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALD- 196
Cdd:COG0396   94 VSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDi 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 197 ----PLIRT--EMQDElvklqakhQRTIVFISH-----DLDEAmrigDRIAIMQNGEVVQVGTPD 250
Cdd:COG0396  174 dalrIVAEGvnKLRSP--------DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGKE 226
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
32-246 1.69e-15

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 74.99  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  32 EQILEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE--PTRGQVLIDGVDIARisdaelrev 103
Cdd:COG2401   28 AIVLEAFGVELRVveryvlRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR--------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 104 rrkkiamvfqsfalmpHMTVLDNTAfgmeLAGTPAQerqekALDALRQVGL-ENYAH-AYPDELSGGMRQRVGLARALAI 181
Cdd:COG2401   99 ----------------EASLIDAIG----RKGDFKD-----AVELLNAVGLsDAVLWlRRFKELSTGQKFRFRLALLLAE 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISH--DLDEAMrIGDRIAIMQNGEVVQV 246
Cdd:COG2401  154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDL-QPDLLIFVGYGGVPEE 219
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
44-273 4.43e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 74.92  E-value: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaelrEVRRKKIAMVFQS------FAL 117
Cdd:PRK15056  23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSeevdwsFPV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 MPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:PRK15056  96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 198 LIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDrIAIMQNGEVVQVGtPDEILNNPANdyVRTFFRGVdISHV 273
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG-PTETTFTAEN--LELAFSGV-LRHV 245
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
39-235 8.36e-15

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: 73.60  E-value: 8.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  39 GLSLGVKDASlaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIArisdaelreVRRKKIAMVFQsfalm 118
Cdd:cd03237   12 EFTLEVEGGS--ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKADYE----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 119 phMTVLDNTAFGMELAGTPAQERQEkaldALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:cd03237   76 --GTVRDLLSSITKDFYTHPYFKTE----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 493864995 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:cd03237  150 QRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL 186
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
44-291 8.68e-15

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: 74.12  E-value: 8.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiarisdaelrevrrkKIAMVFQSFALMPHmTV 123
Cdd:cd03291   53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPG-TI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMelagTPAQERQEKALDALRqvgLENYAHAYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:cd03291  115 KENIIFGV----SYDEYRYKSVVKACQ---LEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 193 SALDPLIRTEMQDELV-KLQAKHQRTIVfisHDLDEAMRIGDRIAIMQNGEVVQVGTPDEiLNNPANDYvRTFFRGVDIS 271
Cdd:cd03291  188 GYLDVFTEKEIFESCVcKLMANKTRILV---TSKMEHLKKADKILILHEGSSYFYGTFSE-LQSLRPDF-SSKLMGYDTF 262
                        250       260
                 ....*....|....*....|
gi 493864995 272 HVFSAKdiaRRtpNGIIRKT 291
Cdd:cd03291  263 DQFSAE---RR--NSILTET 277
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
44-223 1.31e-14

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: 71.03  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiarisdaelrevRRKKIAMVFQSfalmPHMTv 123
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------------EGEDLLFLPQR----PYLP- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 ldntafgmelAGTpaqerqekaldaLRQvglenyAHAYP--DELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirt 201
Cdd:cd03223   77 ----------LGT------------LRE------QLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE---- 124
                        170       180
                 ....*....|....*....|..
gi 493864995 202 EMQDELVKLQAKHQRTIVFISH 223
Cdd:cd03223  125 ESEDRLYQLLKELGITVISVGH 146
hmuV PRK13547
heme ABC transporter ATP-binding protein;
44-253 1.82e-14

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 72.94  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPT-------RGQVLIDGVDIARIsDAELREVRRKKIAMVFQ-S 114
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAI-DAPRLARLRAVLPQAAQpA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 115 FALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALA---------INPDI 185
Cdd:PRK13547  96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRY 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 186 LLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
11-255 1.94e-14

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 74.93  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  11 YKIFGEHPQRAFKYIEKGLTKEQIL----EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL 86
Cdd:PRK13545   3 YKVKFEHVTKKYKMYNKPFDKLKDLffrsKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  87 IDGvdiarisdaelrevrrkKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDALRQVGLENYAHAYPDELS 166
Cdd:PRK13545  83 IKG-----------------SAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 167 GGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
Cdd:PRK13545 146 SGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEY 224

                 ....*....
gi 493864995 247 GTPDEILNN 255
Cdd:PRK13545 225 GDIKEVVDH 233
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
51-263 2.06e-14

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: 72.63  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREvrrkKIAMVFQS---------FALMPHM 121
Cdd:cd03288   44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsirFNLDPEC 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAF-GMELAGTPAQERQ-EKALDALRQVGLENYahaypdelSGGMRQRVGLARALAINPDILLMDEAFSALDplI 199
Cdd:cd03288  120 KCTDDRLWeALEIAQLKNMVKSlPGGLDAVVTEGGENF--------SVGQRQLFCLARAFVRKSSILIMDEATASID--M 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL---NNPANDYVRT 263
Cdd:cd03288  190 ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLaqeDGVFASLVRT 255
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
44-241 2.35e-14

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: 71.59  E-value: 2.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREVRRKKIAMVFQSFALMpHMTV 123
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGmelagTPAQERQEKAL-DALR-QVGLENYAHAYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSA 194
Cdd:cd03290   96 EENITFG-----SPFNKQRYKAVtDACSlQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 493864995 195 LDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNG 241
Cdd:cd03290  171 LDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
PTZ00243 PTZ00243
ABC transporter; Provisional
39-256 3.61e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 74.43  E-value: 3.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaeLREVRRKkiamvfqsFALM 118
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQ--------FSMI 1389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  119 PHMTVL-DNTA------F----------GMELAGTpaQER---QEKALDALRQVGLENYahaypdelSGGMRQRVGLARA 178
Cdd:PTZ00243 1390 PQDPVLfDGTVrqnvdpFleassaevwaALELVGL--RERvasESEGIDSRVLEGGSNY--------SVGQRQLMCMARA 1459
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995  179 -LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
Cdd:PTZ00243 1460 lLKKGSGFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
48-250 5.89e-14

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: 73.29  E-value: 5.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIarisDAELREVRRKKIAMVFQSFALMPHmtvldnt 127
Cdd:COG4615  352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV----TADNREAYRQLFSAVFSDFHLFDR------- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 128 afgmeLAGTPAQERQEKALDALRQVGLEnyaH--AYPD------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:COG4615  421 -----LLGLDGEADPARARELLERLELD---HkvSVEDgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEF 492
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493864995 200 RTEMQDELV-KLQAKhQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPD 250
Cdd:COG4615  493 RRVFYTELLpELKAR-GKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
PLN03211 PLN03211
ABC transporter G-25; Provisional
9-223 5.94e-14

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 73.38  E-value: 5.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   9 NLYKIFGeHPQRAFKyiekglTKEQILEKTGLSlGVKDAslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT--RGQVL 86
Cdd:PLN03211  60 NIKRILG-HKPKISD------ETRQIQERTILN-GVTGM---ASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTIL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  87 IDGVDIARISdaelrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGTPAQERQEKALDA---LRQVGL---EN--YA 158
Cdd:PLN03211 129 ANNRKPTKQI--------LKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAesvISELGLtkcENtiIG 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 159 HAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISH 223
Cdd:PLN03211 201 NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
35-256 8.32e-14

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 70.53  E-value: 8.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiarISDAELRevrrkkIAM 110
Cdd:PRK09544   7 LENVSVSFGqrrvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR------IGY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 111 VFQSFALMPHMTvLDNTAFGMELAGTpaqeRQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDE 190
Cdd:PRK09544  72 VPQKLYLDTTLP-LTVNRFLRLRPGT----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILNNP 256
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP 211
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
44-254 1.04e-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: 73.02  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiarisdaelrevrrkKIAMVFQSFALMPHmTV 123
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG-TI 503
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   124 LDNTAFGMelagTPAQERQEKALDALRqvgLENYAHAYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR01271  504 KDNIIFGL----SYDEYRYTSVIKACQ---LEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 576
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995   193 SALDPLIRTEMQDE-LVKLQAKHQRTIVfiSHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
Cdd:TIGR01271  577 THLDVVTEKEIFEScLCKLMSNKTRILV--TSKL-EHLKKADKILLLHEGVCYFYGTFSELQA 636
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
43-243 1.10e-13

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 72.39  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAElrevrRKKIAMVF-----QSFAL 117
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGL 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 118 MPHMTVLDNT-AFGMELAGTPAQERQEKALdalrqvgLENYAHA------YPDE----LSGGMRQRVGLARALAINPDIL 186
Cdd:PRK15439 353 YLDAPLAWNVcALTHNRRGFWIKPARENAV-------LERYRRAlnikfnHAEQaartLSGGNQQKVLIAKCLEASPQLL 425
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 187 LMDEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
45-242 1.53e-13

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: 67.47  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGVDIArisdaelrevrrkkiamvfqsfalmphmtv 123
Cdd:cd03221   17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIG------------------------------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 ldntafgmelagtpaqerqekaldalrqvglenyahaYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
Cdd:cd03221   67 -------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493864995 204 QDELVklqaKHQRTIVFISHD---LDeamRIGDRIAIMQNGE 242
Cdd:cd03221  110 EEALK----EYPGTVILVSHDryfLD---QVATKIIELEDGK 144
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
7-253 2.37e-13

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 71.25  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   7 VKNLYKIFGEHPQRAFKYIEKGLTKE-----QILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN 75
Cdd:COG0488  283 IKALEKLEREEPPRRDKTVEIRFPPPerlgkKVLELEGLSKSygdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  76 RLIEPTRGQVLIdGVDIarisdaelrevrrkKIAMVFQSFA-LMPHMTVLDNtafgMELAGTPAQERQEKAL-------- 146
Cdd:COG0488  363 GELEPDSGTVKL-GETV--------------KIGYFDQHQEeLDPDKTVLDE----LRDGAPGGTEQEVRGYlgrflfsg 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 147 -DALRQVGlenyahaypdELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDELVKLQAKHQRTIVFISHD- 224
Cdd:COG0488  424 dDAFKPVG----------VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDr 489
                        250       260       270
                 ....*....|....*....|....*....|..
gi 493864995 225 --LDeamRIGDRIAIMQNGEVVQ-VGTPDEIL 253
Cdd:COG0488  490 yfLD---RVATRILEFEDGGVREyPGGYDDYL 518
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
44-309 2.46e-13

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: 69.88  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIARISDAELRevrrkkiamvfQSFALMPHMTV 123
Cdd:cd03289   20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR-----------KAFGVIPQKVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELagTP-AQERQEKALDALRQVGLENYAHAYPDEL-----------SGGMRQRVGLARALAINPDILLMDEA 191
Cdd:cd03289   88 IFSGTFRKNL--DPyGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 192 FSALDPLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpandyvRTFFRGVdIS 271
Cdd:cd03289  166 SAHLDPITYQVIRKTLK--QAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE------KSHFKQA-IS 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 493864995 272 HVFSAKDIARRTPNGIIRKtpgfgPRSALKLLQDEDRE 309
Cdd:cd03289  236 PSDRLKLFPRRNSSKSKRK-----PRPQIQALQEETEE 268
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
51-197 3.45e-13

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 68.34  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdAElrevRRKKIAMVFQSFALMPHMTVLDNTAFG 130
Cdd:PRK13543  34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GD----RSRFMAYLGHLPGLKADLSTLENLHFL 106
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 131 MELAGTPAQERQEKALDAlrqVGLENYAHAYPDELSGGMRQRVGLARaLAINPDIL-LMDEAFSALDP 197
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDL 170
GguA NF040905
sugar ABC transporter ATP-binding protein;
43-245 6.59e-13

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.82  E-value: 6.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPT---RGQVLIDGvDIARISDaeLREVRRKKIAMVFQSFA 116
Cdd:NF040905  13 GVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDG-EVCRFKD--IRDSEALGIVIIHQELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 117 LMPHMTVLDNTAFGMELAGTPA---QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:NF040905  89 LIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493864995 194 ALDPLIRTEMQDELVKLQAkHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
Cdd:NF040905 169 ALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
44-243 3.28e-12

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: 67.93  E-value: 3.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-RGQVLIDG--VDIARISDAelrevRRKKIAMVFQS---FAL 117
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-----IRAGIAMVPEDrkrHGI 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  118 MPHM--------TVLDNTAFGMELagtPAQERQEKALDALRQVGLENYAHAYP-DELSGGMRQRVGLARALAINPDILLM 188
Cdd:TIGR02633 351 VPILgvgknitlSVLKSFCFKMRI---DAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 493864995  189 DEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PTZ00243 PTZ00243
ABC transporter; Provisional
44-247 4.02e-12

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 68.27  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiarisdAElrevrrKKIAMVFQSFALMpHMTV 123
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AE------RSIAYVPQQAWIM-NATV 737
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  124 LDNTAFGMElagtpaqERQEKALDALR--QV---------GLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PTZ00243  738 RGNILFFDE-------EDAARLADAVRvsQLeadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 493864995  193 SALDPLIRTEMQDELVkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVG 247
Cdd:PTZ00243  811 SALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
45-250 9.04e-12

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 64.59  E-value: 9.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIArisDAELREVRRKKIAMVFQSFALMPHMT 122
Cdd:TIGR01978  17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLL---ELEPDERARAGLFLAFQYPEEIPGVS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  123 VLDntaFGMELAGTPAQERQEKALDALRQVGL-----------ENYAHAYPDE-LSGGMRQRVGLARALAINPDILLMDE 190
Cdd:TIGR01978  94 NLE---FLRSALNARRSARGEEPLDLLDFEKLlkeklalldmdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDE 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995  191 AFSALDPLIRTEMQDELVKLQAKHqRTIVFISHDLdeamRIGDRIA-----IMQNGEVVQVGTPD 250
Cdd:TIGR01978 171 IDSGLDIDALKIVAEGINRLREPD-RSFLIITHYQ----RLLNYIKpdyvhVLLDGRIVKSGDVE 230
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
48-264 9.75e-12

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: 66.89  E-value: 9.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIARISDAELRE-------VRRKKIAMVFQSF 115
Cdd:TIGR00957  658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpQQAWIQNDSLREnilfgkaLNEKYYQQVLEAC 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   116 ALMPHMTVL---DNTAFGmelagtpaqerqEKALDalrqvglenyahaypdeLSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:TIGR00957  738 ALLPDLEILpsgDRTEIG------------EKGVN-----------------LSGGQKQRVSLARAVYSNADIYLFDDPL 788
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995   193 SALDPLIRTEMQDELVKLQAK-HQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL--NNPANDYVRTF 264
Cdd:TIGR00957  789 SAVDAHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLqrDGAFAEFLRTY 862
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
44-246 1.05e-11

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 66.35  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKStmvRLLNRL--IEPTR-GQVLIDGVDIARISD--------AELREVRRKKiaMVF 112
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRT---ELMNCLfgVDKRAgGEIRLNGKDISPRSPldavkkgmAYITESRRDN--GFF 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 113 QSFALMPHMTVLDNTAFGmELAGT-----PAQER----QEKALDALRQVGLENYAhaypDELSGGMRQRVGLARALAINP 183
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDG-GYKGAmglfhEVDEQrtaeNQRELLALKCHSVNQNI----TELSGGNQQKVLISKWLCCCP 428
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493864995 184 DILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
46-253 1.61e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 65.92  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEptRGQVLIDGVDIArisDAELREVRRKKIAMVFQSFA--LMPHM 121
Cdd:NF033858  19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMA---DARHRRAVCPRIAYMPQGLGknLYPTL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTAFGMELAGTPAQERQEKALDALRQVGLenyaHAYPD----ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
Cdd:NF033858  94 SVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 198 LIRTEMQDELVKLQAKHQRTIVFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
Cdd:NF033858 170 LSRRQFWELIDRIRAERPGMSVLVAtAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
43-244 1.80e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 65.52  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELREvrrKKIAMVFQSFALMP 119
Cdd:PRK10982  10 GVKaldNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 HMTVLDNtafgMELAGTPAQE---RQEKALDALRQVGLENYAHAYPDE----LSGGMRQRVGLARALAINPDILLMDEAF 192
Cdd:PRK10982  87 QRSVMDN----MWLGRYPTKGmfvDQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 193 SALdplirTEMQ-DELVKLQAKHQRT---IVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK10982 163 SSL-----TEKEvNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
46-244 2.79e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 64.97  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-VDIARISDAELREVRRkkiamvfqsfalmphmTVL 124
Cdd:PRK11147  21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARLQQDPPRNVEG----------------TVY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 125 DNTAFGMELAGTP-----------AQERQEKAL-----------------------DALRQVGLEnyAHAYPDELSGGMR 170
Cdd:PRK11147  85 DFVAEGIEEQAEYlkryhdishlvETDPSEKNLnelaklqeqldhhnlwqlenrinEVLAQLGLD--PDAALSSLSGGWL 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 171 QRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
43-242 4.57e-11

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 64.25  E-value: 4.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  43 GVK---DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiARISDAELREVRRKKIAMVFQSFALMP 119
Cdd:PRK10762  16 GVKalsGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSQEAGIGIIHQELNLIP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 HMTVLDNTAFGMELAGTPA----QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAfsaL 195
Cdd:PRK10762  93 QLTIAENIFLGREFVNRFGridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---T 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 493864995 196 DPLIRTEMQdELVK----LQAKHqRTIVFISHDLDEAMRIGDRIAIMQNGE 242
Cdd:PRK10762 170 DALTDTETE-SLFRvireLKSQG-RGIVYISHRLKEIFEICDDVTVFRDGQ 218
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
44-243 4.89e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 64.18  E-value: 4.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRlIEPTR--GQVLIDG--VDIARISDAelrevRRKKIAMVFQS---FA 116
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNPQQA-----IAQGIAMVPEDrkrDG 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 117 LMPHMTV--------LDNTAFGMELAGTPAQERQEKALDALRqvglenYAHAYPD----ELSGGMRQRVGLARALAINPD 184
Cdd:PRK13549 352 IVPVMGVgknitlaaLDRFTGGSRIDDAAELKTILESIQRLK------VKTASPElaiaRLSGGNQQKAVLAKCLLLNPK 425
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493864995 185 ILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
44-309 1.33e-10

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: 63.39  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIARISDAELRevrrkkiamvfQSFALMPHMTV 123
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR-----------KAFGVIPQKVF 1302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   124 LDNTAFGMELagTP-AQERQEKALDALRQVGLENYAHAYPDEL-----------SGGMRQRVGLARALAINPDILLMDEA 191
Cdd:TIGR01271 1303 IFSGTFRKNL--DPyEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEP 1380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   192 FSALDP----LIRTEMQdelvklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpandyvRTFFRG 267
Cdd:TIGR01271 1381 SAHLDPvtlqIIRKTLK------QSFSNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNE------TSLFKQ 1447
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 493864995   268 VdISHVFSAKDIARRTPNGIIRKtpgfgPRSALKLLQDEDRE 309
Cdd:TIGR01271 1448 A-MSAADRLKLFPLHRRNSSKRK-----PQPKITALREEAEE 1483
PLN03130 PLN03130
ABC transporter C family member; Provisional
36-255 1.58e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 63.22  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   36 EKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTmvrllnrLIEPTRGQvlidgvdIARISDAELreVRRKKIAMVFQsF 115
Cdd:PLN03130  629 ERPTLS----NINLDVPVGSLVAIVGSTGEGKTS-------LISAMLGE-------LPPRSDASV--VIRGTVAYVPQ-V 687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  116 ALMPHMTVLDNTAFGMELAgtpaQERQEKALDAlrqVGLENYAHAYPD-----------ELSGGMRQRVGLARALAINPD 184
Cdd:PLN03130  688 SWIFNATVRDNILFGSPFD----PERYERAIDV---TALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSD 760
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995  185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PLN03130  761 VYIFDDPLSALDAHVGRQVFDKCIKDELRG-KTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
24-244 2.32e-10

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 59.58  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  24 YIEKGLTKEQILektglslgvKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT---RGQVLIDGVDIArisdaEL 100
Cdd:cd03233   12 TTGKGRSKIPIL---------KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK-----EF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 101 REVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGtpaqerqekaldalrqvglenyaHAYPDELSGGMRQRVGLARALA 180
Cdd:cd03233   78 AEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALV 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493864995 181 INPDILLMDEAFSALDPLIRTEMQDELvKLQAKHQRTIVFIS--HDLDEAMRIGDRIAIMQNGEVV 244
Cdd:cd03233  135 SRASVLCWDNSTRGLDSSTALEILKCI-RTMADVLKTTTFVSlyQASDEIYDLFDKVLVLYEGRQI 199
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
139-252 1.12e-09

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 59.36  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 139 QERQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDElVKLQAKHQRTI 218
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATV 197
                         90       100       110
                 ....*....|....*....|....*....|....
gi 493864995 219 VFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
31-243 1.15e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 59.74  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  31 KEQILEKTGLSL----GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAE------- 99
Cdd:PRK10982 247 GEVILEVRNLTSlrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfa 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 100 -LREVRRKKIAMVFQSFALMPHMTVLDN--TAFGMeLAGTPAQERQEKALDALRQVGLENYAHAypDELSGGMRQRVGLA 176
Cdd:PRK10982 327 lVTEERRSTGIYAYLDIGFNSLISNIRNykNKVGL-LDNSRMKSDTQWVIDSMRVKTPGHRTQI--GSLSGGNQQKVIIG 403
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
PLN03232 PLN03232
ABC transporter C family member; Provisional
35-255 1.32e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 60.37  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   35 LEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVR-LLNRLIEPTRGQVLIDGV-----DIARISDAELREvrrkki 108
Cdd:PLN03232  628 TSKPTLS----DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSvayvpQVSWIFNATVRE------ 697
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  109 AMVFQS-FALMPHMTVLDNTAFGMELAGTPAQERQEkaldaLRQVGLEnyahaypdeLSGGMRQRVGLARALAINPDILL 187
Cdd:PLN03232  698 NILFGSdFESERYWRAIDVTALQHDLDLLPGRDLTE-----IGERGVN---------ISGGQKQRVSMARAVYSNSDIYI 763
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  188 MDEAFSALDPLIRTEMQDELVK--LQAKhqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
Cdd:PLN03232  764 FDDPLSALDAHVAHQVFDSCMKdeLKGK---TRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSKS 829
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
14-225 1.83e-09

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 59.41  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  14 FGEHPQRAFKyiekglTKEQILEKTGLSLGVKDASLAIEEGEIFV-----IMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
Cdd:COG1245  327 FEVHAPRREK------EEETLVEYPDLTKSYGGFSLEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEGEVDED 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  89 gVDIA----RIS---DAELREVRRKKIAmvfqsfalmphmTVLDNTAFGMELAgtpaqerqekaldalRQVGLENYAHAY 161
Cdd:COG1245  401 -LKISykpqYISpdyDGTVEEFLRSANT------------DDFGSSYYKTEII---------------KPLGLEKLLDKN 452
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 162 PDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDL 225
Cdd:COG1245  453 VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
48-253 1.87e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 59.26  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAELRevrrKKIAMVFQSfaLMPHMTVLDNT 127
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQ----KLVSDEWQR--NNTDMLSPGED 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 128 AFGMelagTPAQERQEKALDALR------QVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:PRK10938  97 DTGR----TTAEIIQDEVKDPARceqlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493864995 202 EMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Cdd:PRK10938 173 QLAELLASLHQSGI-TLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
61-224 2.26e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 59.14  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  61 GLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIARIS------------------DAELREVRRKKIAMvfqsFALmPHM 121
Cdd:PRK15064  34 GANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRqdqfafeeftvldtvimgHTELWEVKQERDRI----YAL-PEM 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLD-------NTAFGmELAGTPAQERqekALDALRQVGLENYAHAYP-DELSGGMRQRVGLARALAINPDILLMDEAFS 193
Cdd:PRK15064 109 SEEDgmkvadlEVKFA-EMDGYTAEAR---AGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
                        170       180       190
                 ....*....|....*....|....*....|...
gi 493864995 194 ALDplIRT--EMQDELVKLQAkhqrTIVFISHD 224
Cdd:PRK15064 185 NLD--INTirWLEDVLNERNS----TMIIISHD 211
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
54-237 3.63e-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: 55.07  E-value: 3.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARisdaelrevrrkkiamvfqsfalmphmtvldntafgmel 133
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL--------------------------------------- 42
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   134 agtpaqerqekalDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTEMQDELV 208
Cdd:smart00382  43 -------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLL 109
                          170       180
                   ....*....|....*....|....*....
gi 493864995   209 KLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
14-225 3.86e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 58.28  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  14 FGEHPQRAFKyiekglTKEQILEKTGLSLGVKDASLAIEEGEIFV-----IMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
Cdd:PRK13409 326 FEERPPRDES------ERETLVEYPDLTKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  89 gVDIA----RISDAELREVRrkkiamvfqsFALMPHMTVLDNTAFGMELAgtpaqerqekaldalRQVGLENYAHAYPDE 164
Cdd:PRK13409 400 -LKISykpqYIKPDYDGTVE----------DLLRSITDDLGSSYYKSEII---------------KPLQLERLLDKNVKD 453
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493864995 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDL 225
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI 514
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
35-243 1.00e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 56.94  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLS-LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISDAE--------LREVRR 105
Cdd:PRK10762 258 LKVDNLSgPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRK 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 106 KKiamvfqsfALMPHMTVLDN---TA---FGMELAGTPAQERQEKALDALR-----------QVGLenyahaypdeLSGG 168
Cdd:PRK10762 338 RD--------GLVLGMSVKENmslTAlryFSRAGGSLKHADEQQAVSDFIRlfniktpsmeqAIGL----------LSGG 399
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864995 169 MRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEV 243
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGL-SIILVSSEMPEVLGMSDRILVMHEGRI 473
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
297-390 1.36e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; 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: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 49.55  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 297 RSALKLLQDEDREYGYLVERGNKFVGVVSIDSLKTALSE-----NQGIDAALIDAPLAVDAETPLSELLSH-VGQAPCAV 370
Cdd:cd02205   14 REALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEgglalDTPVAEVMTPDVITVSPDTDLEEALELmLEHGIRRL 93
                         90       100
                 ....*....|....*....|
gi 493864995 371 PVVGEEQQYVGIISKRMLLQ 390
Cdd:cd02205   94 PVVDDDGKLVGIVTRRDILR 113
ycf16 CHL00131
sulfate ABC transporter protein; Validated
30-248 1.42e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 52.34  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  30 TKEQILEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIARIsDAELR 101
Cdd:CHL00131   3 KNKPILEIKNLHASVneneilKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDL-EPEER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 102 EvrRKKIAMVFQSFALMPHMTvldNTAFGMELAGTPAQERQEKALDA----------LRQVGL-ENYAHAYPDE-LSGGM 169
Cdd:CHL00131  82 A--HLGIFLAFQYPIEIPGVS---NADFLRLAYNSKRKFQGLPELDPlefleiinekLKLVGMdPSFLSRNVNEgFSGGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHD---LDEAmrIGDRIAIMQNGEVVQV 246
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYqrlLDYI--KPDYVHVMQNGKIIKT 233

                 ..
gi 493864995 247 GT 248
Cdd:CHL00131 234 GD 235
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
44-216 1.94e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 51.10  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARIsdaelREVRRKKIAMVFQSFALMPHMTV 123
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD-----LCTYQKQLCFVGHRSGINPYLTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 LDNTAFGMELAGTPAQerqekaLDAL-RQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL---- 198
Cdd:PRK13540  92 RENCLYDIHFSPGAVG------ITELcRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELsllt 165
                        170       180
                 ....*....|....*....|..
gi 493864995 199 IRTEMQDELVK----LQAKHQR 216
Cdd:PRK13540 166 IITKIQEHRAKggavLLTSHQD 187
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
46-223 3.31e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 50.26  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIARISdaelrevrRKKIAMVFQSFALMPHMTVLD 125
Cdd:PRK13541  18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--------KPYCTYIGHNLGLKLEMTVFE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 126 NTAFGMELAGTpaqerQEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEMQD 205
Cdd:PRK13541  90 NLKFWSEIYNS-----AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLN 163
                        170
                 ....*....|....*...
gi 493864995 206 ELVKLQAKHQRTIVFISH 223
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSH 181
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
51-239 4.00e-07

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: 49.88  E-value: 4.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIArisdaelreVRRKKIamvfqsfalmphmtvldntafg 130
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV---------YKPQYI---------------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 131 melagtpaqerqekaldalrqvglenyahaypdELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKL 210
Cdd:cd03222   71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
                        170       180
                 ....*....|....*....|....*....
gi 493864995 211 QAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
Cdd:cd03222  118 SEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
45-224 4.32e-07

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: 51.86  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNrlieptrgqvlidGVDIARISDAELREVRrkKIAMVFQSFALMPHMTVL 124
Cdd:TIGR03719  22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFNGEARPQPGI--KVGYLPQEPQLDPTKTVR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  125 DNTAFG---------------MELAGTPAQ-----ERQEKALDALRQVG-------LENYAHAY--PD------ELSGGM 169
Cdd:TIGR03719  87 ENVEEGvaeikdaldrfneisAKYAEPDADfdklaAEQAELQEIIDAADawdldsqLEIAMDALrcPPwdadvtKLSGGE 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 493864995  170 RQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
18-253 1.91e-06

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 50.11  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    18 PQRAFKYIEKGLTKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE----PTRGQVLIDGvdia 93
Cdd:TIGR00956   51 PNALLKILTRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDG---- 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    94 rISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAgTPA--------QERQEKALD-ALRQVGLenyAHAYP-- 162
Cdd:TIGR00956  127 -ITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCK-TPQnrpdgvsrEEYAKHIADvYMATYGL---SHTRNtk 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   163 --DEL----SGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvKLQAKHQRTIVFIS--HDLDEAMRIGDR 234
Cdd:TIGR00956  202 vgNDFvrgvSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL-KTSANILDTTPLVAiyQCSQDAYELFDK 280
                          250
                   ....*....|....*....
gi 493864995   235 IAIMQNGEVVQVGTPDEIL 253
Cdd:TIGR00956  281 VIVLYEGYQIYFGPADKAK 299
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
54-241 2.85e-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: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995    54 GEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGVdiaRISDA-ELREVRRKKIAMVFQSFALMPHMTV---LDNTAF 129
Cdd:TIGR00956  789 GTLTALMGASGAGKTT---LLNVLAERVTTGVITGGD---RLVNGrPLDSSFQRSIGYVQQQDLHLPTSTVresLRFSAY 862
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   130 GMELAGTPAQERQEKALDALRQVGLENYAHAY---PDE-LSGGMRQRVGLARALAINPDILL-MDEAFSALDPliRTE-- 202
Cdd:TIGR00956  863 LRQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS--QTAws 940
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 493864995   203 -MQdeLVKLQAKHQRTIVFISH----DLDEAMrigDRIAIMQNG 241
Cdd:TIGR00956  941 iCK--LMRKLADHGQAILCTIHqpsaILFEEF---DRLLLLQKG 979
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
52-225 9.99e-06

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: 46.59  E-value: 9.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  52 EEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL----IDGVdIARISDAELREVRRK------KIAMVFQSFALMPHm 121
Cdd:cd03236   24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdWDEI-LDEFRGSELQNYFTKllegdvKVIVKPQYVDLIPK- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TVLDNTafGMELAGTPAQERQEKALDALrqvGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
Cdd:cd03236  102 AVKGKV--GELLKKKDERGKLDELVDQL---ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
                        170       180
                 ....*....|....*....|....
gi 493864995 202 EMQdELVKLQAKHQRTIVFISHDL 225
Cdd:cd03236  177 NAA-RLIRELAEDDNYVLVVEHDL 199
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
44-223 1.19e-05

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: 47.44  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIdgvdiarisdaelrEVRRKKIAMVFQSfalmPHMT- 122
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--------------KPAKGKLFYVPQR----PYMTl 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  123 -------VLDNTAFGMELAGTPAQERqEKALDAL-------RQVGLENYAHaYPDELSGGMRQRVGLARALAINPDILLM 188
Cdd:TIGR00954 529 gtlrdqiIYPDSSEDMKRRGLSDKDL-EQILDNVqlthileREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAIL 606
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 493864995  189 DEAFSALDPlirtEMQDELVKLQAKHQRTIVFISH 223
Cdd:TIGR00954 607 DECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
PLN03073 PLN03073
ABC transporter F family; Provisional
35-223 1.19e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.55  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  35 LEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN-RLIE--PTRGQVL-----IDGVDIARI-----SD 97
Cdd:PLN03073 180 MENFSISVGgrdlIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDgiPKNCQILhveqeVVGDDTTALqcvlnTD 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  98 AELREVRRKKIAMVFQSFAL-MPHMTVLDNTAFGMELAGTPAQERQE---KALDALRQVGLENYAHAY-------PD--- 163
Cdd:PLN03073 260 IERTQLLEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVSQRLEeiyKRLELIDAYTAEARAASIlaglsftPEmqv 339
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864995 164 ----ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqakhQRTIVFISH 223
Cdd:PLN03073 340 katkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW----PKTFIVVSH 399
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
50-225 1.64e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 46.73  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVdIARISDAEL----REVRRKKIAMVF--QSFALMP 119
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWDEV-LKRFRGTELqnyfKKLYNGEIKVVHkpQYVDLIP 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 HmtVLDNTAfGMELAGTpaQERqeKALDALR-QVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
Cdd:PRK13409 174 K--VFKGKV-RELLKKV--DER--GKLDEVVeRLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
                        170       180
                 ....*....|....*....|....*..
gi 493864995 199 IRTEMQDELVKLQAKhqRTIVFISHDL 225
Cdd:PRK13409 247 QRLNVARLIRELAEG--KYVLVVEHDL 271
PLN03140 PLN03140
ABC transporter G family member; Provisional
31-248 1.67e-05

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 47.15  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   31 KEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-----NRLIEptrGQVLIDGV-----DIARIS---- 96
Cdd:PLN03140  884 KEQGVTEDRLQL-LREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrktGGYIE---GDIRISGFpkkqeTFARISgyce 959
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   97 --DAELREVRRKKiAMVFQSFALMP-------HMTVLDNTafgMELAgtpaqerqekALDALRQ--VGLENYAHaypdeL 165
Cdd:PLN03140  960 qnDIHSPQVTVRE-SLIYSAFLRLPkevskeeKMMFVDEV---MELV----------ELDNLKDaiVGLPGVTG-----L 1020
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  166 SGGMRQRVGLARALAINPDILLMDEAFSALDP-----LIRTemqdelVKLQAKHQRTIVFISH----DLDEAMrigDRIA 236
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDAraaaiVMRT------VRNTVDTGRTVVCTIHqpsiDIFEAF---DELL 1091
                         250
                  ....*....|...
gi 493864995  237 IMQ-NGEVVQVGT 248
Cdd:PLN03140 1092 LMKrGGQVIYSGP 1104
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
297-392 1.67e-05

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 45.26  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 297 RSALKLLQDEdREYGYLVERGNKFVGVVSIDSLKTALSENQGIDAALIDA-----PLAVDAETPLSELL-----SHVGqa 366
Cdd:COG2524  106 EEALELMLEK-GISGLPVVDDGKLVGIITERDLLKALAEGRDLLDAPVSDimtrdVVTVSEDDSLEEALrlmleHGIG-- 182
                         90       100
                 ....*....|....*....|....*.
gi 493864995 367 pcAVPVVGEEQQYVGIISKRMLLQAL 392
Cdd:COG2524  183 --RLPVVDDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
260-392 6.25e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 42.59  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 260 YVRTFFRGVDISHVFSAKDIARRTPNGIIRKtpgfgprsALKLLqdEDREYGYL--VERGNKFVGVVSIDSLKTALsENQ 337
Cdd:COG4109    8 SYDTFKEILLVEDIMTLEDVATLSEDDTVED--------ALELL--EKTGHSRFpvVDENGRLVGIVTSKDILGKD-DDT 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 338 GIDAALIDAPLAVDAETPL---SELLSHVGQApcAVPVVGEEQQYVGIISKRMLLQAL 392
Cdd:COG4109   77 PIEDVMTKNPITVTPDTSLasaAHKMIWEGIE--LLPVVDDDGRLLGIISRQDVLKAL 132
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
50-225 8.70e-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: 8.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL----IDGVdIARISDAEL----REVRRKKI--AMVFQSFALMP 119
Cdd:COG1245   95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepsWDEV-LKRFRGTELqdyfKKLANGEIkvAHKPQYVDLIP 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 120 HmtVLDNTAfgMELAGTpAQERqEKALDALRQVGLENYAHAYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
Cdd:COG1245  174 K--VFKGTV--RELLEK-VDER-GKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
                        170       180
                 ....*....|....*....|....*.
gi 493864995 200 RTEMQdELVKLQAKHQRTIVFISHDL 225
Cdd:COG1245  248 RLNVA-RLIRELAEEGKYVLVVEHDL 272
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
165-238 1.62e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 41.96  E-value: 1.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 165 LSGGMRQRVGLARALA---INPDIL-LMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIM 238
Cdd:cd03227   78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPR-DGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLIHI 153
CBS COG0517
CBS domain [Signal transduction mechanisms];
343-398 1.88e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 41.00  E-value: 1.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493864995 343 LIDAPLAVDAETPLSELLSHVGQAPC-AVPVVGEEQQYVGIISKRMLLQALDREGTN 398
Cdd:COG0517    7 MTTDVVTVSPDATVREALELMSEKRIgGLPVVDEDGKLVGIVTDRDLRRALAAEGKD 63
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
314-395 2.93e-04

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.62  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 314 VERGNKFVGVVSIDSLKTALSENQGIDAALIDA-----------PLAVDAETPLSELL-----SHVGqapcAVPVVGEEQ 377
Cdd:COG3448   39 VDEDGRLVGIVTERDLLRALLPDRLDELEERLLdlpvedvmtrpVVTVTPDTPLEEAAelmleHGIH----RLPVVDDDG 114
                         90
                 ....*....|....*...
gi 493864995 378 QYVGIISKRMLLQALDRE 395
Cdd:COG3448  115 RLVGIVTRTDLLRALARL 132
CBS_pair_chlorobiales cd09837
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
317-389 4.03e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in chlorobiales; 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: 341406 [Multi-domain]  Cd Length: 111  Bit Score: 39.66  E-value: 4.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493864995 317 GNKFVGVVSIDSLKTALSENQGIDAALIDAPL----AVDAETPLSELLSHVGQAPCA-VPVVGEEQQYVGIISKRMLL 389
Cdd:cd09837   33 DGRYVAMVTLADLLPARQGTPTAGLKLGELSLeevgSIGPHEHLFDLFSRLALFPCSiIPVSDEDGRYIGVVSKKRVL 110
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
85-256 5.23e-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: 42.31  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995   85 VLIDGVDIARISDAELREvrrkkiAMVFQSFalmphmtvLDNTAFGMELAGTPAQERQEKaLDALRQVGLE--NYAHAyP 162
Cdd:TIGR00630 423 VTVGGKSIADVSELSIRE------AHEFFNQ--------LTLTPEEKKIAEEVLKEIRER-LGFLIDVGLDylSLSRA-A 486
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  163 DELSGGMRQRVGLARAL--AINPDILLMDEAFSALDP-----LIRTemqdeLVKLQAKHQRTIVfISHDlDEAMRIGDRI 235
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQrdnrrLINT-----LKRLRDLGNTLIV-VEHD-EDTIRAADYV 559
                         170       180
                  ....*....|....*....|....*..
gi 493864995  236 ------AIMQNGEVVQVGTPDEILNNP 256
Cdd:TIGR00630 560 idigpgAGEHGGEVVASGTPEEILANP 586
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
44-247 6.65e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 40.38  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGvdiarisdaeLREVRRKKIAMVFQsfalmphmtv 123
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKST---LVNEGLYASGKARLISF----------LPKFSRNKLIFIDQ---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 124 ldntafgmelagtpaqerqekaLDALRQVGLENYAHAYP-DELSGGMRQRVGLARALAINPD--ILLMDEAFSALDPLIR 200
Cdd:cd03238   68 ----------------------LQFLIDVGLGYLTLGQKlSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864995 201 TEMQDELVKL-QAKHqrTIVFISHDLDeAMRIGDRIAIM------QNGEVVQVG 247
Cdd:cd03238  126 NQLLEVIKGLiDLGN--TVILIEHNLD-VLSSADWIIDFgpgsgkSGGKVVFSG 176
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
140-226 6.77e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 41.64  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 140 ERQ-EKALDALR------QVGlenyahaypdELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQA 212
Cdd:PRK11819 142 DSQlEIAMDALRcppwdaKVT----------KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLH 207
                         90
                 ....*....|....*..
gi 493864995 213 KHQRTIVFISHD---LD 226
Cdd:PRK11819 208 DYPGTVVAVTHDryfLD 224
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
165-241 8.08e-04

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 40.33  E-value: 8.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 165 LSGGMRQRVGLARALA----------INPDILLMDEAFSALDPLIRtEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDR 234
Cdd:cd03279  124 LSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEAL-EAVATALELIRTENRMVGVISHVEELKERIPQR 202

                 ....*..
gi 493864995 235 IAIMQNG 241
Cdd:cd03279  203 LEVIKTP 209
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
166-235 1.21e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 40.92  E-value: 1.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493864995 166 SGGMRQRVGLARALAINPDILLMDEAFSA--LDPLIRTEmqdelvKLQAKHQRTIVFISHDLDEAMRIGDRI 235
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHldLDAVIWLE------KWLKSYQGTLILISHDRDFLDPIVDKI 216
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
347-392 1.61e-03

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.42  E-value: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 493864995  347 PLAVDAETPLSELLSHVGQAPC-AVPVVGEEQQYVGIISKRMLLQAL 392
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGIsRLPVVDEDGKLVGIVTLKDLLRAL 55
CBS COG0517
CBS domain [Signal transduction mechanisms];
297-395 1.95e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 37.92  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 297 RSALKLLQDEDREYGYLVERGNKFVGVVSI-DSLKTALSENQGIDAALIDA-----PLAVDAETPLSELLS-----HVGQ 365
Cdd:COG0517   21 REALELMSEKRIGGLPVVDEDGKLVGIVTDrDLRRALAAEGKDLLDTPVSEvmtrpPVTVSPDTSLEEAAElmeehKIRR 100
                         90       100       110
                 ....*....|....*....|....*....|
gi 493864995 366 apcaVPVVGEEQQYVGIISKRMLLQALDRE 395
Cdd:COG0517  101 ----LPVVDDDGRLVGIITIKDLLKALLEP 126
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
44-196 1.99e-03

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 39.39  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGVDIARISDAELREvrrKKIAMVFQSFALMPHM 121
Cdd:PRK09580  17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAG---EGIFMAFQYPVEIPGV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 122 TvldNTAFGMELAGTPAQERQEKALDALR-QVGLENYAH--AYPDEL---------SGGMRQRVGLARALAINPDILLMD 189
Cdd:PRK09580  94 S---NQFFLQTALNAVRSYRGQEPLDRFDfQDLMEEKIAllKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170

                 ....*..
gi 493864995 190 EAFSALD 196
Cdd:PRK09580 171 ESDSGLD 177
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
312-392 9.52e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. 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: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 36.01  E-value: 9.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864995 312 YLVERGNKFVGVVSIDSLKTALSEnQGIDAAL------IDAPLAVDAETPLSELLSHVGQAPC-AVPVVGEEQQYVGIIS 384
Cdd:cd04639   34 LVTDEAGRLVGLITVDDLRAIPTS-QWPDTPVrelmkpLEEIPTVAADQSLLEVVKLLEEQQLpALAVVSENGTLVGLIE 112

                 ....*...
gi 493864995 385 KRMLLQAL 392
Cdd:cd04639  113 KEDIIELL 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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