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Conserved domains on  [gi|1495939436|ref|XP_026698263|]
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multidrug resistance protein 1 isoform X7 [Athene cunicularia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 166-404 6.56e-167

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: 467.02  E-value: 6.56e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 166 TVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGI 245
Cdd:cd03249     2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEPILFDCTIAENIAYGDNSREVshEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQ 325
Cdd:cd03249    82 VSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 326 ILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 404
Cdd:cd03249   160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_6TM_exporters super family cl38913
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 25-148 1.53e-53

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


The actual alignment was detected with superfamily member cd18578:

Pssm-ID: 365789 [Multi-domain]  Cd Length: 317  Bit Score: 180.73  E-value: 1.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV 104
Cdd:cd18578   194 KIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQF 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1495939436 105 FLVFSAVVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSI 148
Cdd:cd18578   274 FIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 166-404 6.56e-167

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: 467.02  E-value: 6.56e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 166 TVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGI 245
Cdd:cd03249     2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEPILFDCTIAENIAYGDNSREVshEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQ 325
Cdd:cd03249    82 VSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 326 ILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 404
Cdd:cd03249   160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
26-407 2.61e-149

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 435.36  E-value: 2.61e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  26 VATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNVF 105
Cdd:COG1132   202 RLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 106 LVFSAVVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSIDSySEEGEKPETFGGSLTVKDVAFNYPnrPEVKILQG 185
Cdd:COG1132   282 AFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKD 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGD 265
Cdd:COG1132   359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 266 NsrEVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQ 345
Cdd:COG1132   439 P--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQ 516

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 346 EALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQSGS 407
Cdd:COG1132   517 EALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 26-401 3.53e-108

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 334.00  E-value: 3.53e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  26 VATEVIENIRTVASLTRE----RKFELMYGEHLQVPYRNSVKKAhifgFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEY 101
Cdd:TIGR00958 342 VAEEALSGMRTVRSFAAEegeaSRFKEALEETLQLNKRKALAYA----GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSS 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 102 KNV--FLVFSavvfgaMALGQT----SSFAPDYAKAKISAAHLFLLFERVPSIdsySEEGE-KPETFGGSLTVKDVAFNY 174
Cdd:TIGR00958 418 GNLvsFLLYQ------EQLGEAvrvlSYVYSGMMQAVGASEKVFEYLDRKPNI---PLTGTlAPLNLEGLIEFQDVSFSY 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 175 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFD 254
Cdd:TIGR00958 489 PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFS 568

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIAENIAYGDNSREvsHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:TIGR00958 569 GSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 335 ALDTESEKIVQEalDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLV 401
Cdd:TIGR00958 647 ALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
138-406 2.99e-92

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 288.84  E-value: 2.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 138 LFLLFERVPSIDSYSEEGEKPEtfgGSLTVKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFY 217
Cdd:PRK11176  318 LFAILDLEQEKDEGKRVIERAK---GDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 218 DPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSReVSHEEIVKAAKEANIHSFIDSLPDKYNT 297
Cdd:PRK11176  394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQ-YSREQIEEAARMAYAMDFINKMDNGLDT 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 298 RVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQ 377
Cdd:PRK11176  473 VIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVE 552

                         250       260
                  ....*....|....*....|....*....
gi 1495939436 378 NGKVVEQGTHQQLLAEKGIYYSLVNVQSG 406
Cdd:PRK11176  553 DGEIVERGTHAELLAQNGVYAQLHKMQFG 581
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 25-148 1.53e-53

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 180.73  E-value: 1.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV 104
Cdd:cd18578   194 KIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQF 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1495939436 105 FLVFSAVVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSI 148
Cdd:cd18578   274 FIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 183-334 9.37e-46

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: 154.73  E-value: 9.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILF-DCTIAENI 261
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 262 AYGDNSREVSheeivKAAKEANIHSFID--SLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:pfam00005  81 RLGLLLKGLS-----KREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
GguA NF040905
sugar ABC transporter ATP-binding protein;
178-383 2.67e-24

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 104.49  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdP---LDGEMLFDGKNAKTLNI-QWLRAQIGIVSQE---- 249
Cdd:NF040905   12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKDIrDSEALGIVIIHQElali 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 250 PILfdcTIAENIAYGDnsrEVSH------EEIVKAAKE--ANIhsfidSLPDKYNTRVGDKGTqlsgGQKQRIAIARALV 321
Cdd:NF040905   91 PYL---SIAENIFLGN---ERAKrgvidwNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALS 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 322 RQPQILLLDEATSAL-DTESEKIVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVE 383
Cdd:NF040905  156 KDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
174-371 1.40e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 88.83  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 174 YPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlrAQIGIVSQ---EP 250
Cdd:NF040873    2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseVP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 251 ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFidslpdkynTRVGDKG------TQLSGGQKQRIAIARALVRQP 324
Cdd:NF040873   68 DSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEA 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1495939436 325 QILLLDEATSALDTESEKIVQEAL-DKAREGRTCIMIAHRLSTIQNAD 371
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 24-116 5.98e-19

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 86.16  E-value: 5.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  24 FKVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKN 103
Cdd:pfam00664 180 SSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGD 259

                          90
                  ....*....|....*
gi 1495939436 104 --VFLVFSAVVFGAM 116
Cdd:pfam00664 260 lvAFLSLFAQLFGPL 274
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 192-368 3.26e-13

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: 66.63  E-value: 3.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  192 KGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMlfdgknaktlniqwlraqigivsqepILFDCtiaeniaygDNSREVS 271
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDG---------EDILEEV 45

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  272 HEEIVkaakeanihsfidslpdkyNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD-- 349
Cdd:smart00382  46 LDQLL-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106

                          170       180
                   ....*....|....*....|....
gi 1495939436  350 -----KAREGRTCIMIAHRLSTIQ 368
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLG 130
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
187-395 2.41e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.82  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 187 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE-MLFdGK--NAKTLNIqwlRAQIGIVSQEPILF-DCTIAENIA 262
Cdd:NF033858  286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLF-GQpvDAGDIAT---RRRVGYMSQAFSLYgELTVRQNLE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 263 -----YGdnsreVSHEEIVKAAKEAnIHSF-----IDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:NF033858  362 lharlFH-----LPAAEIAARVAEM-LERFdladvADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEP 424

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 333 TSALDTESEKIVQEAL-DKAREGRTCIMIA-HRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKG 395
Cdd:NF033858  425 TSGVDPVARDMFWRLLiELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
300-395 2.36e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 300 GDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESE-KIVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQ 377
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218

                          90
                  ....*....|....*...
gi 1495939436 378 NGKVVEQGTHQQLLAEKG 395
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
GguA NF040905
sugar ABC transporter ATP-binding protein;
165-382 2.28e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 43.24  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKS-TVVQLLERFYDP-LDGEMLFDGKNAKTLNI-QWLRA 241
Cdd:NF040905  258 FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVsDAIDA 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEP-----ILFDcTIAENIAYGdNSREVSHEEIVKAAKEANIhsfIDSLPDKYNTR---VGDKGTQLSGGQKQR 313
Cdd:NF040905  338 GLAYVTEDRkgyglNLID-DIKRNITLA-NLGKVSRRGVIDENEEIKV---AEEYRKKMNIKtpsVFQKVGNLSGGNQQK 412

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 314 IAIARALVRQPQILLLDEATSALDT----ESEKIVQEAldkAREGRTCIMIAHRL-STIQNADKIAVIQNGKVV 382
Cdd:NF040905  413 VVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVISSELpELLGMCDRIYVMNEGRIT 483
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 166-404 6.56e-167

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: 467.02  E-value: 6.56e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 166 TVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGI 245
Cdd:cd03249     2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEPILFDCTIAENIAYGDNSREVshEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQ 325
Cdd:cd03249    82 VSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 326 ILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 404
Cdd:cd03249   160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
26-407 2.61e-149

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 435.36  E-value: 2.61e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  26 VATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNVF 105
Cdd:COG1132   202 RLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 106 LVFSAVVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSIDSySEEGEKPETFGGSLTVKDVAFNYPnrPEVKILQG 185
Cdd:COG1132   282 AFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKD 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGD 265
Cdd:COG1132   359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 266 NsrEVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQ 345
Cdd:COG1132   439 P--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQ 516

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 346 EALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQSGS 407
Cdd:COG1132   517 EALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 29-404 3.82e-128

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: 385.34  E-value: 3.82e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  29 EVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMeykNV--FL 106
Cdd:COG2274   339 ETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQL---TLgqLI 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 107 VFSAVVFGAMA-LGQTSSFAPDYAKAKISAAHLFLLFERVPSIDSYSEEGEKPEtFGGSLTVKDVAFNYPNRpEVKILQG 185
Cdd:COG2274   416 AFNILSGRFLApVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDN 493

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGD 265
Cdd:COG2274   494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD 573

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 266 nsREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQ 345
Cdd:COG2274   574 --PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 346 EALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 404
Cdd:COG2274   652 ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 165-400 4.59e-118

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: 343.06  E-value: 4.59e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:cd03251     1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYGDnsREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 324
Cdd:cd03251    80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 325 QILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSL 400
Cdd:cd03251   158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 137-405 6.51e-114

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: 345.65  E-value: 6.51e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 137 HLFLLFERVPSI-DSyseEGEKPETF-GGSLTVKDVAFNY-PNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL 213
Cdd:COG5265   331 RMFDLLDQPPEVaDA---PDAPPLVVgGGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 214 ERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVKAAKEANIHSFIDSLPD 293
Cdd:COG5265   405 FRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPD 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 294 KYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKI 373
Cdd:COG5265   483 GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEI 562

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1495939436 374 AVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQS 405
Cdd:COG5265   563 LVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 165-404 5.29e-112

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: 327.65  E-value: 5.29e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPnrPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:cd03253     1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYGDNSreVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 324
Cdd:cd03253    79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 325 QILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 404
Cdd:cd03253   157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 26-401 3.53e-108

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 334.00  E-value: 3.53e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  26 VATEVIENIRTVASLTRE----RKFELMYGEHLQVPYRNSVKKAhifgFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEY 101
Cdd:TIGR00958 342 VAEEALSGMRTVRSFAAEegeaSRFKEALEETLQLNKRKALAYA----GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSS 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 102 KNV--FLVFSavvfgaMALGQT----SSFAPDYAKAKISAAHLFLLFERVPSIdsySEEGE-KPETFGGSLTVKDVAFNY 174
Cdd:TIGR00958 418 GNLvsFLLYQ------EQLGEAvrvlSYVYSGMMQAVGASEKVFEYLDRKPNI---PLTGTlAPLNLEGLIEFQDVSFSY 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 175 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFD 254
Cdd:TIGR00958 489 PNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFS 568

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIAENIAYGDNSREvsHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:TIGR00958 569 GSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 335 ALDTESEKIVQEalDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLV 401
Cdd:TIGR00958 647 ALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 27-404 4.16e-108

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 329.74  E-value: 4.16e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  27 ATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV-- 104
Cdd:TIGR02204 200 AGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgq 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 105 FLVFSavVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSIDSYSEEGEKPETFGGSLTVKDVAFNYPNRPEVKILQ 184
Cdd:TIGR02204 280 FVFYA--VMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALD 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 185 GLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYG 264
Cdd:TIGR02204 358 GLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 265 dnSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIV 344
Cdd:TIGR02204 438 --RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLV 515

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 345 QEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 404
Cdd:TIGR02204 516 QQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 163-395 1.91e-105

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: 310.70  E-value: 1.91e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 163 GSLTVKDVAFNYpnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQ 242
Cdd:cd03254     1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 322
Cdd:cd03254    79 IGVVLQDTFLFSGTIMENIRLGRP--NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 323 QPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKG 395
Cdd:cd03254   157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 74-395 2.62e-99

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: 306.68  E-value: 2.62e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  74 LSQAMM-FFTYAG--------CFRFgaylvVNGHMEYKNVFLVF--SAVVFgaMALGQTSSFAPDYAKAKISAAHLFLLF 142
Cdd:COG4988   243 LSSAVLeFFASLSialvavyiGFRL-----LGGSLTLFAALFVLllAPEFF--LPLRDLGSFYHARANGIAAAEKIFALL 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 143 ERvPSIDSYSEEGEKPETFGGSLTVKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDG 222
Cdd:COG4988   316 DA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 223 EMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDnsREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDK 302
Cdd:COG4988   393 SILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEG 470

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 303 GTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVV 382
Cdd:COG4988   471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIV 550

                         330
                  ....*....|...
gi 1495939436 383 EQGTHQQLLAEKG 395
Cdd:COG4988   551 EQGTHEELLAKNG 563
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 134-404 2.06e-98

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: 304.72  E-value: 2.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 134 SAAHLFLLFERVPSIDSYSEEGEKPEtfgGSLTVKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL 213
Cdd:TIGR02203 303 AAESLFTLLDSPPEKDTGTRAIERAR---GDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 214 ERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDnSREVSHEEIVKAAKEANIHSFIDSLPD 293
Cdd:TIGR02203 379 PRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPL 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 294 KYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKI 373
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1495939436 374 AVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 404
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 73-400 2.82e-96

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: 298.99  E-value: 2.82e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  73 ALSQAMMFFTYAGCFRFGAYLVVNGHMEykNVFLVfsAVVFGAMAL----GQTSSFAPDYAKAKISAAHLFLLFERVPSI 148
Cdd:COG4987   244 ALLQLAAGLAVVAVLWLAAPLVAAGALS--GPLLA--LLVLAALALfealAPLPAAAQHLGRVRAAARRLNELLDAPPAV 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 149 DSYSEEGEKPEtfGGSLTVKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG 228
Cdd:COG4987   320 TEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 229 KNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSG 308
Cdd:COG4987   397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSG 474

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQ 388
Cdd:COG4987   475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHE 554

                         330
                  ....*....|..
gi 1495939436 389 QLLAEKGIYYSL 400
Cdd:COG4987   555 ELLAQNGRYRQL 566
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
138-406 2.99e-92

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 288.84  E-value: 2.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 138 LFLLFERVPSIDSYSEEGEKPEtfgGSLTVKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFY 217
Cdd:PRK11176  318 LFAILDLEQEKDEGKRVIERAK---GDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 218 DPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSReVSHEEIVKAAKEANIHSFIDSLPDKYNT 297
Cdd:PRK11176  394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQ-YSREQIEEAARMAYAMDFINKMDNGLDT 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 298 RVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQ 377
Cdd:PRK11176  473 VIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVE 552

                         250       260
                  ....*....|....*....|....*....
gi 1495939436 378 NGKVVEQGTHQQLLAEKGIYYSLVNVQSG 406
Cdd:PRK11176  553 DGEIVERGTHAELLAQNGVYAQLHKMQFG 581
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 165-404 1.76e-90

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: 273.21  E-value: 1.76e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNY-PNRPEvkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 243
Cdd:cd03252     1 ITFEHVRFRYkPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILFDCTIAENIAYGDNSreVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 323
Cdd:cd03252    79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNV 403
Cdd:cd03252   157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236


                  .
gi 1495939436 404 Q 404
Cdd:cd03252   237 Q 237
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 158-381 3.71e-88

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: 266.64  E-value: 3.71e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 158 PETFGGSLTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQ 237
Cdd:cd03248     5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQEPILFDCTIAENIAYGDNSreVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 317
Cdd:cd03248    85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKV 381
Cdd:cd03248   163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 165-380 4.35e-88

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: 264.25  E-value: 4.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:cd03228     1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIaygdnsrevsheeivkaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 324
Cdd:cd03228    80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 325 QILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGK 380
Cdd:cd03228   116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 73-401 6.70e-87

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: 278.37  E-value: 6.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  73 ALSQAMMFFTYAGCFRFGAYLVVNGHME------YKNVFLVFSAVVFGAMALGQT-SSFAPDYAKAK-ISAAHLFLLFER 144
Cdd:TIGR03796 381 VLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDdVLRNPVDPLLEE 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 145 VPSIDSYSEEGEKPEtfgGSLTVKDVAFNYpNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEM 224
Cdd:TIGR03796 461 PEGSAATSEPPRRLS---GYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI 536

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 225 LFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSreVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGT 304
Cdd:TIGR03796 537 LFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGA 614

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALdkAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQ 384
Cdd:TIGR03796 615 NLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQR 692

                         330
                  ....*....|....*..
gi 1495939436 385 GTHQQLLAEKGIYYSLV 401
Cdd:TIGR03796 693 GTHEELWAVGGAYARLI 709
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
87-404 1.27e-86

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 274.53  E-value: 1.27e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  87 FRFGAYLVVNGHMEYKNV--FLVFSAVVFGAmaLGQTSSFAPDYAKAKISAAHLFLLFERVPSIDSySEEGEKPETFGGS 164
Cdd:PRK13657  258 LVLGAALVQKGQLRVGEVvaFVGFATLLIGR--LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRD-PPGAIDLGRVKGA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK13657  335 VEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYGdnsRE-VSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 323
Cdd:PRK13657  413 VVFQDAGLFNRSIEDNIRVG---RPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNV 403
Cdd:PRK13657  490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569


                  .
gi 1495939436 404 Q 404
Cdd:PRK13657  570 Q 570
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 103-406 1.06e-83

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 269.69  E-value: 1.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 103 NVFLVFSAVVFGAMALGQTSSF--------AP---------DYAKAKISaahlfllFERVPSI-DSYSEEGEK-----PE 159
Cdd:TIGR01846 379 LLWFGAHLVIGGALSPGQLVAFnmlagrvtQPvlrlaqlwqDFQQTGIA-------LERLGDIlNSPTEPRSAglaalPE 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 160 tFGGSLTVKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW 238
Cdd:TIGR01846 452 -LRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW 528

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 239 LRAQIGIVSQEPILFDCTIAENIAYGDNSreVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIAR 318
Cdd:TIGR01846 529 LRRQMGVVLQENVLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIAR 606

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYY 398
Cdd:TIGR01846 607 ALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686


                  ....*...
gi 1495939436 399 SLVNVQSG 406
Cdd:TIGR01846 687 RLWQQQSG 694
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 81-404 1.58e-72

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: 239.86  E-value: 1.58e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  81 FTYAGCFRFGAYLVVNGHMEYkNVFLVFSAvvfgamALGQTSSFAPDYAKAKISAAHLFLLFERV-PSIDSYSE-EGEK- 157
Cdd:TIGR03797 371 LTSAALFAAAISLLGGAGLSL-GSFLAFNT------AFGSFSGAVTQLSNTLISILAVIPLWERAkPILEALPEvDEAKt 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 158 -PETFGGSLTVKDVAFNY-PNRPevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN 235
Cdd:TIGR03797 444 dPGKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD 521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWLRAQIGIVSQEPILFDCTIAENIAyGDNSreVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIA 315
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSGSIFENIA-GGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLL 598

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRtcIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKG 395
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREG 676


                  ....*....
gi 1495939436 396 IYYSLVNVQ 404
Cdd:TIGR03797 677 LFAQLARRQ 685
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 163-385 1.91e-72

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: 226.32  E-value: 1.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 163 GSLTVKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQ 242
Cdd:cd03245     1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEPILFDCTIAENIAYGDnsREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 322
Cdd:cd03245    80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 323 QPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQG 385
Cdd:cd03245   158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 90-393 1.18e-69

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: 229.63  E-value: 1.18e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  90 GAYLVVNGHMeyknvflvfSAvvfGAM----------------ALGQTSSFApdyaKAKISAAHLFLLFERVPsidsysE 153
Cdd:COG4618   260 GAYLVIQGEI---------TP---GAMiaasilmgralapieqAIGGWKQFV----SARQAYRRLNELLAAVP------A 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 154 EGE-----KPEtfgGSLTVKDVAFNYPNRPEVkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG 228
Cdd:COG4618   318 EPErmplpRPK---GRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 229 KNAKtlniQWLRAQ----IGIVSQEPILFDCTIAENIAygdnsR--EVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDK 302
Cdd:COG4618   394 ADLS----QWDREElgrhIGYLPQDVELFDGTIAENIA-----RfgDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEG 464

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 303 GTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIAVIQNGKV 381
Cdd:COG4618   465 GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRV 544

                         330
                  ....*....|..
gi 1495939436 382 VEQGTHQQLLAE 393
Cdd:COG4618   545 QAFGPRDEVLAR 556
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 29-409 3.13e-69

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 237.62  E-value: 3.13e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436   29 EVIENIRTVASLTRE----RKFELmyGEHLQVPY---RNSVKKAHIfgfcfALSQAMMFFTYAGCFRFGAYLVVNG-HME 100
Cdd:PTZ00265   241 EALVGIRTVVSYCGEktilKKFNL--SEKLYSKYilkANFMESLHI-----GMINGFILASYAFGFWYGTRIIISDlSNQ 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  101 YKN-------VFLVFSAVVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSIDSySEEGEKPETFGgSLTVKDVAFN 173
Cdd:PTZ00265   314 QPNndfhggsVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFH 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  174 YPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLF-DGKNAKTLNIQWLRAQIGIVSQEPIL 252
Cdd:PTZ00265   392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLL 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  253 FDCTIAENIAY------------------------GDNSRE-------------------------------VSHEEIVK 277
Cdd:PTZ00265   472 FSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNscrakcagdlndmsnttdsneliemrknyqtIKDSEVVD 551

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  278 AAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD--KAREGR 355
Cdd:PTZ00265   552 VSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENR 631

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  356 TCIMIAHRLSTIQNADKIAVIQNGK-----------------------------------------------VVEQGTHQ 388
Cdd:PTZ00265   632 ITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHD 711

                          490       500
                   ....*....|....*....|..
gi 1495939436  389 QLLAEK-GIYYSLVNVQSGSCN 409
Cdd:PTZ00265   712 ALMKNKnGIYYTMINNQKVSSK 733
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 163-386 6.68e-69

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: 216.98  E-value: 6.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 163 GSLTVKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 241
Cdd:cd03244     1 GDIEFKNVSLRYrPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 321
Cdd:cd03244    79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 322 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGT 386
Cdd:cd03244   156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 18-403 1.89e-68

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 235.31  E-value: 1.89e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436   18 FPDIAFfkVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNG 97
Cdd:PTZ00265  1018 FKDPSF--LIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRG 1095

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436   98 HMEYKNVFLVFSAVVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSIDSYSEEG---EKPETFGGSLTVKDVAFNY 174
Cdd:PTZ00265  1096 TILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRY 1175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  175 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLD--------------------------------- 221
Cdd:PTZ00265  1176 ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknv 1255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  222 ---------------------GEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGdnSREVSHEEIVKAAK 280
Cdd:PTZ00265  1256 nefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACK 1333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  281 EANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEAL----DKAreGRT 356
Cdd:PTZ00265  1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKT 1411

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1495939436  357 CIMIAHRLSTIQNADKIAVIQN----GKVVE-QGTHQQLL-AEKGIYYSLVNV 403
Cdd:PTZ00265  1412 IITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQDGVYKKYVKL 1464
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
111-397 1.95e-68

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 226.52  E-value: 1.95e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 111 VVFGAMALGQTSSFA--------PDYAKA-------KISAAH--LFLLFERVPSIDsyseEGEKPETFG-GSLTVKDVAF 172
Cdd:PRK10789  246 VVNGSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAAYsrIRAMLAEAPVVK----DGSEPVPEGrGELDVNIRQF 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 173 NYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPIL 252
Cdd:PRK10789  322 TYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 253 FDCTIAENIAYGdnSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK10789  401 FSDTVANNIALG--RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 333 TSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIY 397
Cdd:PRK10789  479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
162-404 7.95e-67

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 222.67  E-value: 7.95e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 162 GGSLTVKDVAFNYpnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 241
Cdd:PRK10790  338 SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPILFDCTIAENIAYGdnsREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 321
Cdd:PRK10790  416 GVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 322 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLV 401
Cdd:PRK10790  493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572


                  ...
gi 1495939436 402 NVQ 404
Cdd:PRK10790  573 QLQ 575
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 73-400 1.12e-66

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 222.01  E-value: 1.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  73 ALSQAMMFF----TYAGCFRFGAYLVvnGHMEYKNVFLVFsaVVFGAMA--------------LGQTSSfapdyakakiS 134
Cdd:PRK11160  245 GLSQALMILanglTVVLMLWLAAGGV--GGNAQPGALIAL--FVFAALAafealmpvagafqhLGQVIA----------S 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 135 AAHLFLLFERVPSIDSYSEEGEKPETfgGSLTVKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLE 214
Cdd:PRK11160  311 ARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 215 RFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVKAAKEANIHSFIDSlPDK 294
Cdd:PRK11160  388 RAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP--NASDEALIEVLQQVGLEKLLED-DKG 464

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 295 YNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIA 374
Cdd:PRK11160  465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544

                         330       340
                  ....*....|....*....|....*.
gi 1495939436 375 VIQNGKVVEQGTHQQLLAEKGIYYSL 400
Cdd:PRK11160  545 VMDNGQIIEQGTHQELLAQQGRYYQL 570
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 94-376 2.02e-66

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: 220.24  E-value: 2.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  94 VVNGHMEYKNVFLVFSAV--VFgaMALGQTSSFAPDYAKAKISAAHLFLLFERVPSIdsYSEEGEKPETFGGSLTVKDVA 171
Cdd:TIGR02857 253 LLAGDLDLATGLFVLLLApeFY--LPLRQLGAQYHARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVS 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 172 FNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPI 251
Cdd:TIGR02857 329 VAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPF 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 252 LFDCTIAENIAYGDnsREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDE 331
Cdd:TIGR02857 407 LFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1495939436 332 ATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVI 376
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 89-403 4.98e-62

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 212.29  E-value: 4.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  89 FGAYLVVNGHMEYKNVfLVFSAVV-FGAMALGQTSSFAPDYAKAKISAAHLFLLFeRVPSIDSYSEEGEKPETFGGSLTV 167
Cdd:TIGR01193 399 TGAYLVMRGKLTLGQL-ITFNALLsYFLTPLENIINLQPKLQAARVANNRLNEVY-LVDSEFINKKKRTELNNLNGDIVI 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 168 KDVAFNYP-NRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 246
Cdd:TIGR01193 477 NDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQEPILFDCTIAENIAYGdNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQI 326
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 327 LLLDEATSALDTESEKIVQEALDKAREgRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNV 403
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 178-408 8.67e-61

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 206.62  E-value: 8.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQG-LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCT 256
Cdd:PRK11174  360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENIAYGDNsrEVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 336
Cdd:PRK11174  439 LRDNVLLGNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 337 DTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQSGSC 408
Cdd:PRK11174  517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 90-393 1.93e-56

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 194.10  E-value: 1.93e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  90 GAYLVVNGHMEYKNVflVFSAVVFGAmALG---QTSSFAPDYAKAKISAAHLFLLFERVPSIDSYSEEGEkPEtfgGSLT 166
Cdd:TIGR01842 246 GAYLAIDGEITPGMM--IAGSILVGR-ALApidGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPE-PE---GHLS 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNrPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 246
Cdd:TIGR01842 319 VENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQEPILFDCTIAENIA-YGDNsreVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQ 325
Cdd:TIGR01842 398 PQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 326 ILLLDEATSALDTESEKIVQEALDKAR-EGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 165-390 3.40e-56

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: 184.69  E-value: 3.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKNAKTLNIQ-- 237
Cdd:cd03260     1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQEPILFDCTIAENIAYGDN-----SREVSHEEIVKAAKEANihsfidsLPDKYNTRVgdKGTQLSGGQKQ 312
Cdd:cd03260    78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKAA-------LWDEVKDRL--HALGLSGGQQQ 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQL 390
Cdd:cd03260   149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 143-392 2.02e-55

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: 190.88  E-value: 2.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 143 ERVPSIDSYSEEGEKPETFGGS-LTVKDVAFNYPNRP--EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDP 219
Cdd:COG1123   238 AAVPRLGAARGRAAPAAAAAEPlLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 220 LDGEMLFDGKNAKTLN---IQWLRAQIGIVSQEPIL-FDC--TIAENIAYG-DNSREVSHEEIVKAAKEAnIH------S 286
Cdd:COG1123   318 TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LErvglppD 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 287 FIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD--KAREGRTCIMIAHRL 364
Cdd:COG1123   397 LADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDL 465

                         250       260
                  ....*....|....*....|....*....
gi 1495939436 365 STIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:COG1123   466 AVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 165-394 3.07e-55

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: 182.15  E-value: 3.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:COG1122     1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPI--LFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 318
Cdd:COG1122    79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGTHQQLLAEK 394
Cdd:COG1122   148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
165-381 6.73e-55

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 180.40  E-value: 6.73e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:COG4619     1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYGDNSRE--VSHEEIVKAAKEANihsfidsLPDKY-NTRVgdkgTQLSGGQKQRIAIARALV 321
Cdd:COG4619    78 YVPQEPALWGGTVRDNLPFPFQLRErkFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRALL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 322 RQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKV 381
Cdd:COG4619   147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 25-148 1.53e-53

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 180.73  E-value: 1.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV 104
Cdd:cd18578   194 KIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQF 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1495939436 105 FLVFSAVVFGAMALGQTSSFAPDYAKAKISAAHLFLLFERVPSI 148
Cdd:cd18578   274 FIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 165-385 5.56e-53

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: 176.16  E-value: 5.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL---R 240
Cdd:cd03257     2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 241 AQIGIVSQEPI-----LFdcTIAENIA-----YGDNSREvshEEIVKAAKEANIH-----SFIDSLPDkyntrvgdkgtQ 305
Cdd:cd03257    82 KEIQMVFQDPMsslnpRM--TIGEQIAeplriHGKLSKK---EARKEAVLLLLVGvglpeEVLNRYPH-----------E 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 306 LSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVV 382
Cdd:cd03257   146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225


                  ...
gi 1495939436 383 EQG 385
Cdd:cd03257   226 EEG 228
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 112-364 5.71e-53

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: 184.49  E-value: 5.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 112 VFGAMALGQTSSFAP------DYAKAKISAAHLFLLFERVPSIDSYSEEGEKPETFGG-SLTVKDVAFNYPNRPEVkiLQ 184
Cdd:TIGR02868 275 VLVLLPLAAFEAFAAlpaaaqQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LD 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 185 GLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYG 264
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 265 dnSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIV 344
Cdd:TIGR02868 433 --RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510

                         250       260
                  ....*....|....*....|
gi 1495939436 345 QEALDKAREGRTCIMIAHRL 364
Cdd:TIGR02868 511 LEDLLAALSGRTVVLITHHL 530
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 165-385 1.29e-52

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: 173.65  E-value: 1.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIG 244
Cdd:cd03247     1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIaygdnsrevsheeivkaakeanihsfidslpdkyntrvgdkGTQLSGGQKQRIAIARALVRQP 324
Cdd:cd03247    79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 325 QILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQG 385
Cdd:cd03247   118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 167-380 1.50e-52

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: 174.58  E-value: 1.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 246
Cdd:cd03225     2 LKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARAL 320
Cdd:cd03225    81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 321 VRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGK 380
Cdd:cd03225   150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 165-381 2.87e-51

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: 169.70  E-value: 2.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:cd03246     1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIaygdnsrevsheeivkaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 324
Cdd:cd03246    80 YLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNP 115

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 325 QILLLDEATSALDTESEKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIAVIQNGKV 381
Cdd:cd03246   116 RILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 165-392 1.31e-49

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: 175.09  E-value: 1.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDP---LDGEMLFDGKNAKTLNIQWLRA 241
Cdd:COG1123     5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPI--LFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIA 315
Cdd:COG1123    84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQRQRVA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:COG1123   153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 165-392 3.57e-49

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: 166.90  E-value: 3.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPE-VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 243
Cdd:COG1124     2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPIL-------FDCTIAE--NIAYGDNSREvsheEIVKAAKEANIH-SFIDSLPDkyntrvgdkgtQLSGGQKQR 313
Cdd:COG1124    82 QMVFQDPYAslhprhtVDRILAEplRIHGLPDREE----RIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 314 IAIARALVRQPQILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGT 386
Cdd:COG1124   147 VAIARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222


                  ....*.
gi 1495939436 387 HQQLLA 392
Cdd:COG1124   223 VADLLA 228
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 158-386 8.61e-49

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: 164.51  E-value: 8.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 158 PETfgGSLTVKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI 236
Cdd:cd03369     2 PEH--GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 237 QWLRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAakeanihsfidslpdkynTRVGDKGTQLSGGQKQRIAI 316
Cdd:cd03369    78 EDLRSSLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCL 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGT 386
Cdd:cd03369   137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 165-385 3.08e-48

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: 163.46  E-value: 3.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIG 244
Cdd:cd03259     1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFD-CTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 319
Cdd:cd03259    76 MVFQDYALFPhLTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARA 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 320 LVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQG 385
Cdd:cd03259   145 LAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
165-384 5.29e-48

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 163.29  E-value: 5.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPN-RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERfydPLDGEMLFDGKNAKTLN---IQ 237
Cdd:COG1136     5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSereLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQ-IGIVSQEPILFDC-TIAENIA----YGDNSREVSHEEIVKAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQK 311
Cdd:COG1136    82 RLRRRhIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 312 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQ 384
Cdd:COG1136   151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 165-384 7.41e-48

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: 162.64  E-value: 7.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNR-PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQI 243
Cdd:cd03293     1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILFD-CTIAENIAYGDNSREVSHEEIVKAAKEAnIH-----SFIDSLPDkyntrvgdkgtQLSGGQKQRIAIA 317
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-LElvglsGFENAYPH-----------QLSGGMRQRVALA 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQN--GKVVEQ 384
Cdd:cd03293   144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 165-391 3.84e-47

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: 161.75  E-value: 3.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:COG1120     2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPIL-FDCTIAENIAYG--------DNSREVSHEEIVKAAKEANIHSFIDslpdkynTRVgdkgTQLSGGQKQRIA 315
Cdd:COG1120    79 YVPQEPPApFGLTVRELVALGryphlglfGRPSAEDREAVEEALERTGLEHLAD-------RPV----DELSGGERQRVL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:COG1120   148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 164-386 8.72e-47

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 163.73  E-value: 8.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQI 243
Cdd:COG3842     5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILF-DCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 318
Cdd:COG3842    80 GMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRVALAR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS---TIqnADKIAVIQNGKVVEQGT 386
Cdd:COG3842   149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 165-392 2.36e-46

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: 159.28  E-value: 2.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQ---LLERfydPLDGEMLFDGKNAKTLN---IQ 237
Cdd:cd03258     2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQEPILFDC-TIAENIAYgdnSREVSHEEivKAAKEANIHSFID--SLPDKYNTRVGdkgtQLSGGQKQRI 314
Cdd:cd03258    79 KARRRIGMIFQHFNLLSSrTVFENVAL---PLEIAGVP--KAEIEERVLELLElvGLEDKADAYPA----QLSGGQKQRV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 315 AIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLL 391
Cdd:cd03258   150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229


                  .
gi 1495939436 392 A 392
Cdd:cd03258   230 A 230
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
165-393 2.74e-46

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 159.07  E-value: 2.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWlRAQIG 244
Cdd:COG1131     1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILF-DCTIAENIAYGDNSREVSHEEIVKAAKEAnIHSFidSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQ 323
Cdd:COG1131    77 YVPQEPALYpDLTVRENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHD 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:COG1131   150 PELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
165-386 4.21e-46

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 161.78  E-value: 4.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQ---LLERfydPLDGEMLFDGKNAKTLNIQWLR 240
Cdd:COG1135     2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 241 A---QIGIVSQEPILFD-CTIAENIAY-----GdnsreVSHEEIVKAAKEanihsfidsLPDkyntRVG--DKG----TQ 305
Cdd:COG1135    79 AarrKIGMIFQHFNLLSsRTVAENVALpleiaG-----VPKAEIRKRVAE---------LLE----LVGlsDKAdaypSQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 306 LSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVV 382
Cdd:COG1135   141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220


                  ....
gi 1495939436 383 EQGT 386
Cdd:COG1135   221 EQGP 224
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 153-400 8.28e-46

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: 169.36  E-value: 8.28e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  153 EEGEKPETF--GGSLTVKDVAFNYpnRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK 229
Cdd:TIGR00957 1271 QETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL 1348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  230 NAKTLNIQWLRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGG 309
Cdd:TIGR00957 1349 NIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVG 1425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  310 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQ 389
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSN 1505

                          250
                   ....*....|.
gi 1495939436  390 LLAEKGIYYSL 400
Cdd:TIGR00957 1506 LLQQRGIFYSM 1516
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 183-334 9.37e-46

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: 154.73  E-value: 9.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILF-DCTIAENI 261
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 262 AYGDNSREVSheeivKAAKEANIHSFID--SLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:pfam00005  81 RLGLLLKGLS-----KREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 167-394 1.63e-45

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 157.98  E-value: 1.63e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL-NIQWLRAQIGI 245
Cdd:TIGR04520   3 VENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEPilfD-----CTIAENIAYGDNSREVSHEEIVK----AAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAI 316
Cdd:TIGR04520  82 VFQNP---DnqfvgATVEDDVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRVAI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAR--EGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEK 394
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 167-392 2.65e-45

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: 156.51  E-value: 2.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRAQI 243
Cdd:cd03261     3 LRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILFDC-TIAENIAYG--DNSREvSHEEIVKAAKE----ANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAI 316
Cdd:cd03261    80 GMLFQSGALFDSlTVFENVAFPlrEHTRL-SEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRVAL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 317 ARALVRQPQILLLDEATSALD-TESEKIVQEALD-KAREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:cd03261   148 ARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 165-390 5.29e-45

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 156.35  E-value: 5.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD--P---LDGEMLFDGKN--AKTLNIQ 237
Cdd:COG1117    12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQEPILFDCTIAENIAYG-----DNSREVsHEEIVKAA-KEANihsfidsLPDKYNTRVGDKGTQLSGGQK 311
Cdd:COG1117    89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 312 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAH------RLStiqnaDKIAVIQNGKVVEQG 385
Cdd:COG1117   161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFG 235


                  ....*
gi 1495939436 386 THQQL 390
Cdd:COG1117   236 PTEQI 240
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 179-392 5.38e-45

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 155.54  E-value: 5.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTV---VQLLERfydPLDGEMLFDGKN--AKTLNIQWLRAQIGIVSQEPILF 253
Cdd:COG1126    13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 -DCTIAENIAYGD-NSREVSHEEIVKAAKEAnihsfidsLpdkynTRVG--DKG----TQLSGGQKQRIAIARALVRQPQ 325
Cdd:COG1126    90 pHLTVLENVTLAPiKVKKMSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 326 ILLLDEATSALDTEsekIVQEALD--K--AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:COG1126   157 VMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 166-380 1.69e-44

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: 151.63  E-value: 1.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 166 TVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGI 245
Cdd:cd00267     1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQepilfdctiaeniaygdnsrevsheeivkaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPQ 325
Cdd:cd00267    78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 326 ILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQNA-DKIAVIQNGK 380
Cdd:cd00267   101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 165-395 1.84e-44

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: 154.63  E-value: 1.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIqWLRAQIG 244
Cdd:COG4555     2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFD-CTIAENIAYGDNSREVSHEEIVKAAKEAnIHSFIdsLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQ 323
Cdd:COG4555    78 VLPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHD 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAEKG 395
Cdd:COG4555   151 PKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 165-383 4.98e-44

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 153.71  E-value: 4.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQI 243
Cdd:COG1116     8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILFD-CTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 318
Cdd:COG1116    83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAH------RLstiqnADKIAVIQN--GKVVE 383
Cdd:COG1116   152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 165-392 5.17e-44

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: 153.21  E-value: 5.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRA 241
Cdd:COG1127     6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPILFDC-TIAENIAYG-DNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIA 315
Cdd:COG1127    83 RIGMLFQGGALFDSlTVFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:COG1127   152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 165-380 1.13e-43

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: 150.42  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW--LRAQ 242
Cdd:cd03229     1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEPILF-DCTIAENIAYGdnsrevsheeivkaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALV 321
Cdd:cd03229    78 IGMVFQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 322 RQPQILLLDEATSALDTESEKIVQEALD--KAREGRTCIMIAHRLSTIQN-ADKIAVIQNGK 380
Cdd:cd03229   117 MDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 165-392 1.40e-43

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: 152.07  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:cd03295     1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILF-DCTIAENIAYGDNSREVSHEEIVKAAKEanIHSFIDSLPDKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 323
Cdd:cd03295    79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADE--LLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRL-STIQNADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:cd03295   154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 165-380 1.95e-42

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: 148.00  E-value: 1.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEV--KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ErfYDPLDGEMLFDGKnaktlniqwlr 240
Cdd:cd03250     1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 241 aqIGIVSQEPILFDCTIAENIAYGDNSREVSHEEIVKA-AKEANIhsfiDSLPDKYNTRVGDKGTQLSGGQKQRIAIARA 319
Cdd:cd03250    68 --IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKAcALEPDL----EILPDGDLTEIGEKGINLSGGQKQRISLARA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 320 LVRQPQILLLDEATSALDTE-SEKIVQEALDKA-REGRTCIMIAHRLSTIQNADKIAVIQNGK 380
Cdd:cd03250   142 VYSDADIYLLDDPLSAVDAHvGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 165-381 3.03e-42

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: 147.64  E-value: 3.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPE-VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN----IQWL 239
Cdd:cd03255     1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 RAQIGIVSQE----PILfdcTIAENIAYGDNSREVSHEEIVKAAKEAnihsfIDS--LPDKYNTRVGdkgtQLSGGQKQR 313
Cdd:cd03255    81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 314 IAIARALVRQPQILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIMIAHRLSTIQNADKIAVIQNGKV 381
Cdd:cd03255   149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 165-393 1.04e-41

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: 149.43  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKD--VAFNYPNRPeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPL---DGEMLFDGKNAKTLN---I 236
Cdd:COG0444     2 LEVRNlkVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 237 QWLR-AQIGIVSQEPI-----LFdcTIAENIA-----YGDNSREVSHEEIVKAAKEANIH---SFIDSLPdkyntrvgdk 302
Cdd:COG0444    81 RKIRgREIQMIFQDPMtslnpVM--TVGDQIAeplriHGGLSKAEARERAIELLERVGLPdpeRRLDRYP---------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 303 gTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIMIAHRLSTI-QNADKIAV 375
Cdd:COG0444   149 -HELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAV 223

                         250
                  ....*....|....*...
gi 1495939436 376 IQNGKVVEQGTHQQLLAE 393
Cdd:COG0444   224 MYAGRIVEEGPVEELFEN 241
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 164-391 3.47e-41

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 148.76  E-value: 3.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERfydPLDGEMLFDGKNAKTlniqWLR 240
Cdd:COG1118     2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFT----NLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 241 AQ---IGIVSQEPILF-DCTIAENIAYGDNSREVSHEEIVKAAKE----ANIHSFIDSLPdkyntrvgdkgTQLSGGQKQ 312
Cdd:COG1118    72 PRerrVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALDT----ESEKIVQEALDkaREGRTCIMIAH------RLstiqnADKIAVIQNGKVV 382
Cdd:COG1118   141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIE 213


                  ....*....
gi 1495939436 383 EQGTHQQLL 391
Cdd:COG1118   214 QVGTPDEVY 222
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 163-390 4.97e-41

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 148.68  E-value: 4.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 163 GSLTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQ 242
Cdd:COG3839     2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLPPK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 ---IGIVSQEPILFD-CTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRI 314
Cdd:COG3839    74 drnIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKPK-----------QLSGGQRQRV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 315 AIARALVRQPQILLLDEATSALD------TESE-KIVQEALdkareGRTCIMIAHRLS---TIqnADKIAVIQNGKVVEQ 384
Cdd:COG3839   143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215


                  ....*.
gi 1495939436 385 GTHQQL 390
Cdd:COG3839   216 GTPEEL 221
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 167-396 7.12e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 145.90  E-value: 7.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 246
Cdd:PRK13632   10 VENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQEPilfD-----CTIAENIAYGDNSREVSHEE----IVKAAKEANIHSFIDSLPDKyntrvgdkgtqLSGGQKQRIAIA 317
Cdd:PRK13632   89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKG 395
Cdd:PRK13632  155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234


                  .
gi 1495939436 396 I 396
Cdd:PRK13632  235 I 235
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
165-392 1.12e-40

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 145.54  E-value: 1.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnakTLNIQ--W-LRA 241
Cdd:PRK13635    6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEEtvWdVRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPilfD-----CTIAENIAYGDNSREVSHEEIVK----AAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQ 312
Cdd:PRK13635   82 QVGMVFQNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALDTESEkivQEALD-----KAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTH 387
Cdd:PRK13635  148 RVAIAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224


                  ....*
gi 1495939436 388 QQLLA 392
Cdd:PRK13635  225 EEIFK 229
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
168-383 4.08e-40

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 142.50  E-value: 4.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 168 KDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRAQIG 244
Cdd:COG2884     5 ENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQE-PILFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 319
Cdd:COG2884    83 VVFQDfRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVAIARA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 320 LVRQPQILLLDEATSALDTE-SEKIVqEALDKA-REGRTCIMIAHRLSTIQNADK-IAVIQNGKVVE 383
Cdd:COG2884   152 LVNRPELLLADEPTGNLDPEtSWEIM-ELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 161-401 4.99e-40

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: 143.13  E-value: 4.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 161 FGGSLTVKDVAFNYPN--RPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW 238
Cdd:cd03288    16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 239 LRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIAR 318
Cdd:cd03288    93 LRSRLSIILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEK-GIY 397
Cdd:cd03288   170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249


                  ....
gi 1495939436 398 YSLV 401
Cdd:cd03288   250 ASLV 253
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 183-391 6.94e-40

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: 142.09  E-value: 6.94e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPILF-DCTIAENI 261
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 262 AYGDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTESE 341
Cdd:cd03299    93 AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 342 KIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLL 391
Cdd:cd03299   166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 166-385 1.06e-39

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: 139.88  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 166 TVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGI 245
Cdd:cd03214     1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQepilfdctiaeniaygdnsrevsheeivkAAKEANIHSFIDSLpdkYNTrvgdkgtqLSGGQKQRIAIARALVRQPQ 325
Cdd:cd03214    78 VPQ-----------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPP 117

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 326 ILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQG 385
Cdd:cd03214   118 ILLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 165-393 1.53e-39

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 141.38  E-value: 1.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLniqwlRAQIG 244
Cdd:COG1121     7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQE-------PIlfdcTIAENIAYG--------DNSREVSHEEIVKAAKEANIHSFIDslpdkynTRVGdkgtQLSGG 309
Cdd:COG1121    79 YVPQRaevdwdfPI----TVRDVVLMGrygrrglfRRPSRADREAVDEALERVGLEDLAD-------RPIG----ELSGG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 310 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTI-QNADKIAVIqNGKVVEQGTH 387
Cdd:COG1121   144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222


                  ....*.
gi 1495939436 388 QQLLAE 393
Cdd:COG1121   223 EEVLTP 228
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 165-390 2.01e-39

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 141.35  E-value: 2.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRA 241
Cdd:COG3638     3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPILFD-CTIAENI---AYGDNS------REVSHEEIVKAakeaniHSFIDS--LPDKYNTRVGdkgtQLSGG 309
Cdd:COG3638    81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 310 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGT 386
Cdd:COG3638   151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGP 230


                  ....
gi 1495939436 387 HQQL 390
Cdd:COG3638   231 PAEL 234
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 187-393 2.64e-39

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: 141.63  E-value: 2.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 187 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA----QIGIVSQEPILF-DCTIAENI 261
Cdd:cd03294    44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 262 AYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALD 337
Cdd:cd03294   124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 338 TESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:cd03294   193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 165-392 2.07e-38

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: 144.83  E-value: 2.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNR--------PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFyDPLDGEMLFDGKNAKTLN- 235
Cdd:COG4172   276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 --IQWLRAQIGIVSQEPilFDC-----TIAENIAYGdnsREVSHEEIVKAAKEANIhsfIDSLpdkynTRVG-DKGT--- 304
Cdd:COG4172   355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhr 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 ---QLSGGQKQRIAIARALVRQPQILLLDEATSALDteseKIVQ-EALD-----KAREGRTCIMIAHRLSTIQN-ADKIA 374
Cdd:COG4172   422 yphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVM 497

                         250
                  ....*....|....*...
gi 1495939436 375 VIQNGKVVEQGTHQQLLA 392
Cdd:COG4172   498 VMKDGKVVEQGPTEQVFD 515
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 165-394 4.31e-38

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: 137.70  E-value: 4.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK---NAKTLNIQWLRA 241
Cdd:cd03256     1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPILFD-CTIAENI---AYGDNS------REVSHEEIVKAAkeanihSFIDS--LPDKYNTRVGdkgtQLSGG 309
Cdd:cd03256    79 QIGMIFQQFNLIErLSVLENVlsgRLGRRStwrslfGLFPKEEKQRAL------AALERvgLLDKAYQRAD----QLSGG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 310 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGT 386
Cdd:cd03256   149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGP 228


                  ....*...
gi 1495939436 387 HQQLLAEK 394
Cdd:cd03256   229 PAELTDEV 236
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 165-381 8.77e-38

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: 134.45  E-value: 8.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIG 244
Cdd:cd03230     1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILF-DCTIAENIaygdnsrevsheeivkaakeanihsfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQ 323
Cdd:cd03230    77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKV 381
Cdd:cd03230   114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
PLN03232 PLN03232
ABC transporter C family member; Provisional
 143-409 1.09e-37

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 145.50  E-value: 1.09e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  143 ERVPS-IDSYSE-----EGEKPET---FGGSLTVKDVAFNYpnRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQL 212
Cdd:PLN03232  1204 ERVGNyIDLPSEataiiENNRPVSgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  213 LERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLP 292
Cdd:PLN03232  1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNP 1358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  293 DKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKarEGRTCIM--IAHRLSTIQNA 370
Cdd:PLN03232  1359 FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMlvIAHRLNTIIDC 1436

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1495939436  371 DKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVQSGSCN 409
Cdd:PLN03232  1437 DKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
165-392 1.66e-37

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 135.65  E-value: 1.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkiLQgLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIqwlrAQ-- 242
Cdd:COG3840     2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErp 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEPILFD-CTIAENIAYGDNSR----EVSHEEIVKAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIA 317
Cdd:COG3840    73 VSMLFQENNLFPhLTVAQNIGLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 318 RALVRQPQILLLDEATSALD----TESEKIVQEALDkaREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:COG3840   142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 167-385 1.67e-37

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 134.97  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLniqwlRAQIGIV 246
Cdd:cd03235     2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQEPIL---FDCTIAENIAYGDNSREVSHEEIVKAAKEAnihsfIDSLPDkyntRVGDKG------TQLSGGQKQRIAIA 317
Cdd:cd03235    74 PQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK-----VDEALE----RVGLSEladrqiGELSGGQQQRVLLA 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIqNGKVVEQG 385
Cdd:cd03235   145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
PLN03130 PLN03130
ABC transporter C family member; Provisional
 163-409 3.28e-37

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 144.11  E-value: 3.28e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  163 GSLTVKDVAFNYpnRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 241
Cdd:PLN03130  1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  242 QIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 321
Cdd:PLN03130  1314 VLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  322 RQPQILLLDEATSALDTESEKIVQEALDKarEGRTCIM--IAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYS 399
Cdd:PLN03130  1391 RRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMliIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468

                          250
                   ....*....|.
gi 1495939436  400 LVnVQS-GSCN 409
Cdd:PLN03130  1469 KM-VQStGAAN 1478
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 182-390 3.80e-37

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: 134.67  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNakTLNIQWLRAQIGIVSQEPILF-DCTIAEN 260
Cdd:cd03300    15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD--ITNLPPHKRPVNTVFQNYALFpHLTVFEN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 261 IAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSAL 336
Cdd:cd03300    93 IAFGLRLKKLPKAEIKERVAEAldlvQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 337 DTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQL 390
Cdd:cd03300   162 DLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 176-386 8.02e-37

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 136.85  E-value: 8.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 176 NRPEVKILQGLNLKVEKGQTLALVGSSGCGKST---VVQLLERfydPLDGEMLFDGKNAKTLNIQWLRA---QIGIVSQE 249
Cdd:PRK11153   14 GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 250 pilFDC----TIAENIAYGdnsrevshEEIVKAAKeANIHSFIDSLPDkyntRVG--DKG----TQLSGGQKQRIAIARA 319
Cdd:PRK11153   91 ---FNLlssrTVFDNVALP--------LELAGTPK-AEIKARVTELLE----LVGlsDKAdrypAQLSGGQKQRVAIARA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 320 LVRQPQILLLDEATSALDTESEKIVQEALDKA-RE-GRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGT 386
Cdd:PRK11153  155 LASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 165-393 3.94e-36

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 134.86  E-value: 3.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYP--------NRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN- 235
Cdd:COG4608     8 LEVRDLKKHFPvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 --IQWLRAQIGIVSQEPilFDC-----TIAENIAYG-DNSREVSheeivKAAKEANIHSFIDslpdkyntRVGDKGT--- 304
Cdd:COG4608    88 reLRPLRRRMQMVFQDP--YASlnprmTVGDIIAEPlRIHGLAS-----KAERRERVAELLE--------LVGLRPEhad 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 ----QLSGGQKQRIAIARALVRQPQILLLDEATSALDteseKIVQ-------EALdKAREGRTCIMIAHRLSTIQN-ADK 372
Cdd:COG4608   153 ryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALD----VSIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDR 227

                         250       260
                  ....*....|....*....|.
gi 1495939436 373 IAVIQNGKVVEQGTHQQLLAE 393
Cdd:COG4608   228 VAVMYLGKIVEIAPRDELYAR 248
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
178-385 4.81e-36

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 137.84  E-value: 4.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI-QWLRAQIGIVSQEPILF-DC 255
Cdd:COG1129    15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAYGdnsRE------VSHEEIVKAAKEA----NIHsfIDslPDkynTRVGDkgtqLSGGQKQRIAIARALVRQPQ 325
Cdd:COG1129    95 SVAENIFLG---REprrgglIDWRAMRRRARELlarlGLD--ID--PD---TPVGD----LSVAQQQLVEIARALSRDAR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 326 ILLLDEATSAL-DTESE---KIVQEaLdkAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:COG1129   161 VLILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTG 222
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
 25-138 6.47e-36

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 133.94  E-value: 6.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHME-YKN 103
Cdd:cd18558   199 AVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEV 278

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1495939436 104 VFLVFSAVVFGAMALGQTSSFAPdYAKAKISAAHL 138
Cdd:cd18558   279 LTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 166-382 9.21e-36

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: 130.45  E-value: 9.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 166 TVKDVAFNYPNRPEvkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlniQWLRAQ-IG 244
Cdd:cd03226     1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKsIG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVR 322
Cdd:cd03226    75 YVMQDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLS 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 323 QPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVV 382
Cdd:cd03226   144 GKDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 181-381 3.07e-35

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: 129.19  E-value: 3.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 181 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQIGIVSQEPILF-DCTI 257
Cdd:cd03262    14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNLFpHLTV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 258 AENIAYGD-NSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:cd03262    94 LENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEP 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 333 TSALDTEsekIVQEALDK----AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKV 381
Cdd:cd03262   163 TSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
cbiO PRK13650
energy-coupling factor transporter ATPase;
165-392 1.30e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 129.47  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK13650    5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 318
Cdd:PRK13650   85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 165-390 2.49e-34

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 127.97  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKN---AKTLNI 236
Cdd:PRK14239    6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiysPRTDTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 237 QwLRAQIGIVSQEPILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSfiDSLPDKYNTRVGDKGTQLSGGQKQRIAI 316
Cdd:PRK14239   83 D-LRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRL---STIqnADKIAVIQNGKVVEQGTHQQL 390
Cdd:PRK14239  160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 165-393 2.82e-34

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: 126.78  E-value: 2.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiQWLRAQIG 244
Cdd:cd03224     1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERARAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 I--VSQEPILF-DCTIAENIAYGDNSREvsheeivKAAKEANIHSFIDSLPDKYnTRVGDKGTQLSGGQKQRIAIARALV 321
Cdd:cd03224    77 IgyVPEGRRIFpELTVEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALM 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 322 RQPQILLLDEATSALdteSEKIVQE---ALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:cd03224   149 SRPKLLLLDEPSEGL---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 165-394 2.83e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 128.27  E-value: 2.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL--RAQ 242
Cdd:PRK13639    2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANihsfidslpdkynTRVGDKGTQ------LSGGQKQRI 314
Cdd:PRK13639   80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEAL-------------KAVGMEGFEnkpphhLSGGQKKRV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 315 AIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTIQ-NADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK13639  147 AIAGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226


                  ..
gi 1495939436 393 EK 394
Cdd:PRK13639  227 DI 228
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 165-385 4.24e-34

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: 126.22  E-value: 4.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKN-----AKTLNIqwl 239
Cdd:cd03301     1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlpPKDRDI--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 raqiGIVSQEPILF-DCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLPDKyntrvgdKGTQLSGGQKQRIAIAR 318
Cdd:cd03301    75 ----AMVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDR-------KPKQLSGGQRQRVALGR 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAH-RLSTIQNADKIAVIQNGKVVEQG 385
Cdd:cd03301   144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
182-386 6.68e-34

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 129.68  E-value: 6.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPILF-DCTIAEN 260
Cdd:PRK09452   29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFEN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 261 IAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 336
Cdd:PRK09452  107 VAFGLRMQKTPAAEITPRVMEAlrmvQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 337 DTESEKIVQEALdKA--RE-GRTCIMIAH-RLSTIQNADKIAVIQNGKVVEQGT 386
Cdd:PRK09452  176 DYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 165-392 2.19e-33

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: 130.96  E-value: 2.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKD--VAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKS----TVVQLLERFYDPLDGEMLFDGKNAKTLNIQW 238
Cdd:COG4172     7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 239 LRA----QIGIVSQEPI-----LFdcTIAENIAygdnsrEV--SHEEIVKAAKEANIHSFIDS--LPDKyNTRVGDKGTQ 305
Cdd:COG4172    86 LRRirgnRIAMIFQEPMtslnpLH--TIGKQIA------EVlrLHRGLSGAAARARALELLERvgIPDP-ERRLDAYPHQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 306 LSGGQKQRIAIARALVRQPQILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIMIAHRLSTIQN-ADKIAVIQN 378
Cdd:COG4172   157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232

                         250
                  ....*....|....
gi 1495939436 379 GKVVEQGTHQQLLA 392
Cdd:COG4172   233 GEIVEQGPTAELFA 246
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 165-375 2.77e-33

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: 123.74  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWlRAQIG 244
Cdd:COG4133     3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILF-DCTIAENIA-----YGdnsREVSHEEIVKAAKEANIHSFIDslpdkynTRVGdkgtQLSGGQKQRIAIAR 318
Cdd:COG4133    79 YLGHADGLKpELTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALAR 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEAL-DKAREGRTCIMIAHRLSTIQNADKIAV 375
Cdd:COG4133   145 LLLSPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVLDL 202
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 164-378 3.29e-33

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 123.75  E-value: 3.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDP---LDGEMLFDGKNAKTLNIQwlR 240
Cdd:COG4136     1 MLSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--Q 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 241 AQIGIVSQEPILFD-CTIAENIAYG---DNSREVSHEEIVKAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAI 316
Cdd:COG4136    76 RRIGILFQDDLLFPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVAL 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 317 ARALVRQPQILLLDEATSALDTE-SEKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIAVIQN 378
Cdd:COG4136   145 LRALLAEPRALLLDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 164-390 4.85e-33

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 123.99  E-value: 4.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRPEvkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQI 243
Cdd:cd03296     2 SIEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILF-DCTIAENIAYGDNSREVShEEIVKAAKEANIHSFI-----DSLPDKYNTrvgdkgtQLSGGQKQRIAIA 317
Cdd:cd03296    77 GFVFQHYALFrHMTVFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQL 390
Cdd:cd03296   149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 181-385 7.56e-33

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: 122.79  E-value: 7.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 181 KILQGLNLKVE---KGQTLALVGSSGCGKSTVVQLLERFYDP------LDGEMLFDGKnaKTLNIQWLRAQIGIVSQEPI 251
Cdd:cd03297     8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPdggtivLNGTVLFDSR--KKINLPPQQRKIGLVFQQYA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 252 LF-DCTIAENIAYG-----DNSREVSHEEIVKAAKeanihsfIDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPQ 325
Cdd:cd03297    86 LFpHLNVRENLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYPA-------QLSGGEKQRVALARALAAQPE 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 326 ILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:cd03297   152 LLLLDEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
cbiO PRK13640
energy-coupling factor transporter ATPase;
165-386 9.22e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 124.53  E-value: 9.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE---MLFDGKNAKTLNIQWLRA 241
Cdd:PRK13640    6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVK----AAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIA 315
Cdd:PRK13640   85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESE----KIVQEALDKarEGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGT 386
Cdd:PRK13640  154 IAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 162-379 1.24e-32

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 129.16  E-value: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 162 GGSLTVKDVAFNYPN-RPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-----------ERfydPLDGEMLFdgk 229
Cdd:COG4178   360 DGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriAR---PAGARVLF--- 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 230 naktlniqwlraqigiVSQEPILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLpdkynTRVGDKGTQLSGG 309
Cdd:COG4178   431 ----------------LPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLG 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 310 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNG 379
Cdd:COG4178   490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 163-397 1.24e-32

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: 124.20  E-value: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 163 GSLTVKDVAFNYPNRPEVkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDpLDGEMLFDGKNAKTLNIQWLRAQ 242
Cdd:cd03289     1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 322
Cdd:cd03289    79 FGVIPQKVFIFSGTFRKNL---DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 323 QPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIY 397
Cdd:cd03289   156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 167-401 1.41e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 123.69  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 246
Cdd:PRK13647    7 VEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARAL 320
Cdd:PRK13647   85 FQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPP-----------YHLSYGQKKRVAIAGVL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 321 VRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQG-----THQQLLAE 393
Cdd:PRK13647  154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQ 233


                  ....*...
gi 1495939436 394 KGIYYSLV 401
Cdd:PRK13647  234 AGLRLPLV 241
cbiO PRK13637
energy-coupling factor transporter ATPase;
164-393 1.73e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 124.00  E-value: 1.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKN--AKTLNIQWL 239
Cdd:PRK13637    2 SIKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 RAQIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEAnihsfIDSLPDKYNTrVGDKGT-QLSGGQKQRIAI 316
Cdd:PRK13637   82 RKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTeseKIVQEALDKARE-----GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQL 390
Cdd:PRK13637  156 AGVVAMEPKILILDEPTAGLDP---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232


                  ...
gi 1495939436 391 LAE 393
Cdd:PRK13637  233 FKE 235
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 165-394 2.12e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 123.80  E-value: 2.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQ 242
Cdd:PRK13636    6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARAL 320
Cdd:PRK13636   84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 321 VRQPQILLLDEATSALD----TESEKIVQEALDKAreGRTCIMIAHRLSTIQ-NADKIAVIQNGKVVEQGTHQQLLAEK 394
Cdd:PRK13636  157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 165-382 2.54e-32

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: 119.84  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-IQWLRAQI 243
Cdd:cd03216     1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQepilfdctiaeniaygdnsrevsheeivkaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQ 323
Cdd:cd03216    78 AMVYQ---------------------------------------------------------LSVGERQMVEIARALARN 100

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 324 PQILLLDEATSAL-DTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVV 382
Cdd:cd03216   101 ARLLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
cbiO PRK13642
energy-coupling factor transporter ATPase;
165-392 3.73e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 122.89  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK13642    5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIH-SFIDslpdkYNTRvgdKGTQLSGGQKQRIAIARALV 321
Cdd:PRK13642   85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAvNMLD-----FKTR---EPARLSGGQKQRVAVAGIIA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 322 RQPQILLLDEATSALD----TESEKIVQEALDKARegRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK13642  157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 168-381 6.45e-32

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: 120.21  E-value: 6.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 168 KDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRAQIG 244
Cdd:cd03292     4 INVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQE-PILFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARA 319
Cdd:cd03292    82 VVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALP-----------AELSGGEQQRVAIARA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 320 LVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADK--IAVIQNGKV 381
Cdd:cd03292   151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 183-393 7.10e-32

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 121.81  E-value: 7.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPL-----DGEMLFDGKN--AKTLNIQWLRAQIGIVSQEPILFDC 255
Cdd:PRK14243   26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAYGD--NSREVSHEEIV-KAAKEAnihSFIDSLPDKYNtrvgDKGTQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK14243  106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA---ALWDEVKDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 333 TSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK14243  179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 165-396 2.07e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 120.63  E-value: 2.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYpNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK13648    8 IVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIV----KAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 318
Cdd:PRK13648   87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHrrvsEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIMIAHRLSTIQNADKIAVIQNGKVVEQGT------HQQL 390
Cdd:PRK13648  156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteifdHAEE 235


                  ....*.
gi 1495939436 391 LAEKGI 396
Cdd:PRK13648  236 LTRIGL 241
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 165-390 2.38e-31

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: 118.76  E-value: 2.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIG 244
Cdd:cd03263     1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFD-CTIAENIAYGDNSREVSHEEIvKAAKEANIHSFidSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQ 323
Cdd:cd03263    79 YCPQFDALFDeLTVREHLRFYARLKGLPKSEI-KEEVELLLRVL--GLTDKANKRART----LSGGMKRKLSLAIALIGG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQL 390
Cdd:cd03263   152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 162-397 7.28e-31

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: 125.41  E-value: 7.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  162 GGSLTVKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPlDGEMLFDGKNAKTLNIQWLRA 241
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRK 1292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  242 QIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 321
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436  322 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIY 397
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
179-391 9.57e-31

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 117.89  E-value: 9.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQIGIVSQEPILF-DC 255
Cdd:PRK09493   13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvNDPKVDERLIRQEAGMVFQQFYLFpHL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAYGD-NSREVSHEEIVKAAKEanihsfidsLPDKYN--TRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK09493   93 TALENVMFGPlRVRGASKEEAEKQARE---------LLAKVGlaERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 333 TSALDTEsekIVQEAL----DKAREGRTCIMIAHRlstIQNADKIA----VIQNGKVVEQGTHQQLL 391
Cdd:PRK09493  164 TSALDPE---LRHEVLkvmqDLAEEGMTMVIVTHE---IGFAEKVAsrliFIDKGRIAEDGDPQVLI 224
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 165-394 9.38e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 116.66  E-value: 9.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDG------EMLFDGKNAKtlNI 236
Cdd:PRK13634    3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKKNK--KL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 237 QWLRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVKAAKEAnihsfID--SLPDKYNTRvgdKGTQLSGGQKQ 312
Cdd:PRK13634   81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALDTESEKIVQE---ALDKaREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQ 388
Cdd:PRK13634  153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231


                  ....*.
gi 1495939436 389 QLLAEK 394
Cdd:PRK13634  232 EIFADP 237
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 162-397 1.61e-29

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: 121.59  E-value: 1.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  162 GGSLTVKDVAFNYPnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGknaktlniqwlra 241
Cdd:TIGR00957  634 GNSITVHNATFTWA-RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------- 699

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  242 QIGIVSQEPILFDCTIAENIAYGDNSREVSHEEIVKAAKeanIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 321
Cdd:TIGR00957  700 SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA---LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVY 776

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436  322 RQPQILLLDEATSALDTESEKIVQEAL---DKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIY 397
Cdd:TIGR00957  777 SNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 186-385 2.25e-29

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: 113.36  E-value: 2.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPILF-DCTIAENIAYG 264
Cdd:cd03298    17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 265 DNSR----EVSHEEIVKAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALD-TE 339
Cdd:cd03298    95 LSPGlkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDpAL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1495939436 340 SEKIVQEALDKARE-GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:cd03298   164 RAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 165-391 2.33e-29

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: 114.41  E-value: 2.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE--MLFDGKNAKTlNIQWLRAQ 242
Cdd:COG1119     4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGERRGGE-DVWELRKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVS---QEPILFDCTIAENIAYGDNS-----REVSHEEIVKAakEANIHSF-IDSLPDK-YNTrvgdkgtqLSGGQKQ 312
Cdd:COG1119    80 IGLVSpalQLRFPRDETVLDVVLSGFFDsiglyREPTDEQRERA--RELLELLgLAHLADRpFGT--------LSQGEQR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTC-IMIAHRLSTIQNA-DKIAVIQNGKVVEQGTHQQ 389
Cdd:COG1119   150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTlVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEE 229


                  ..
gi 1495939436 390 LL 391
Cdd:COG1119   230 VL 231
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
182-390 3.20e-29

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 116.36  E-value: 3.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPILF-DCTIAEN 260
Cdd:PRK11432   21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 261 IAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSAL 336
Cdd:PRK11432   99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLSNL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 337 DTESEKIVQEaldKARE-----GRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQL 390
Cdd:PRK11432  168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 164-391 3.73e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 114.36  E-value: 3.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDpLDGEMLFDGK--------NAKTLN 235
Cdd:PRK14258    7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWLRAQIGIVSQEPILFDCTIAENIAYGDN----SREVSHEEIVKAAKEANihsfidSLPDKYNTRVGDKGTQLSGGQK 311
Cdd:PRK14258   83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 312 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD--KAREGRTCIMIAHRLSTIQN-ADKIAVIQN-----GKVVE 383
Cdd:PRK14258  157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVE 236


                  ....*...
gi 1495939436 384 QGTHQQLL 391
Cdd:PRK14258  237 FGLTKKIF 244
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 180-386 3.83e-29

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: 113.30  E-value: 3.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 180 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIGIVS--QEPILF-DCT 256
Cdd:cd03219    13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENI----------AYGDNSREVSHEEIVKAAKEAnihsfIDS--LPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 324
Cdd:cd03219    92 VLENVmvaaqartgsGLLLARARREEREARERAEEL-----LERvgLADLADRPAGE----LSYGQQRRLEIARALATDP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 325 QILLLDEATSAL-DTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGT 386
Cdd:cd03219   163 KLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
cbiO PRK13644
energy-coupling factor transporter ATPase;
167-398 4.28e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 114.31  E-value: 4.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-IQWLRAQIGI 245
Cdd:PRK13644    4 LENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEAnihsFIDSLPDKYNTRvgdKGTQLSGGQKQRIAIARALVRQ 323
Cdd:PRK13644   82 VFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTME 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDKA-REGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYY 398
Cdd:PRK13644  155 PECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 182-393 4.72e-29

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 113.69  E-value: 4.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDG-----EMLFDGknAKTLN-----IQWLRAQIGIVSQEPI 251
Cdd:PRK11264   18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDT--ARSLSqqkglIRQLRQHVGFVFQNFN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 252 LFDC-TIAENIAYGDN-SREVSHEEIVKAAKEANIHSFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPQILLL 329
Cdd:PRK11264   96 LFPHrTVLENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILF 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 330 DEATSALDTEsekIVQEALDK----AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK11264  169 DEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 178-382 7.53e-29

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 117.82  E-value: 7.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnakTLNI----QWLRAQIGIVSQEPILF 253
Cdd:COG3845    16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIrsprDAIALGIGMVHQHFMLV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 DC-TIAENIAYGDNSREVSHEEIVKAAKEanihsfIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPQI 326
Cdd:COG3845    93 PNlTVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 327 LLLDEATSALdTESEkiVQE---ALDK-AREGRTCIMIAHRLSTI-QNADKIAVIQNGKVV 382
Cdd:COG3845   163 LILDEPTAVL-TPQE--ADElfeILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
187-392 8.98e-29

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 112.37  E-value: 8.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 187 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPILFD-CTIAENIAYGD 265
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 266 NS----REVSHEEIVKAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPQILLLDEATSALD---- 337
Cdd:PRK10771   97 NPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 338 TESEKIVQEALDkaREGRTCIMIAHRLstiQNADKIA----VIQNGKVVEQGTHQQLLA 392
Cdd:PRK10771  166 QEMLTLVSQVCQ--ERQLTLLMVSHSL---EDAARIAprslVVADGRIAWDGPTDELLS 219
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 162-385 9.59e-29

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: 111.10  E-value: 9.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 162 GGSLTVKDVAFNYPNRP---EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLDGEMLFDGKNaktLNI 236
Cdd:cd03213     1 GVTLSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 237 QWLRAQIGIVSQEPILFDC-TIAENIAYgdnsrevsheeivkAAKeanihsfidsLpdkyntrvgdKGtqLSGGQKQRIA 315
Cdd:cd03213    78 RSFRKIIGYVPQDDILHPTlTVRETLMF--------------AAK----------L----------RG--LSGGERKRVS 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLST--IQNADKIAVIQNGKVVEQG 385
Cdd:cd03213   122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 165-392 1.10e-28

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 112.00  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQ-- 242
Cdd:COG0410     4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHri 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 ----IGIVSQEPILF-DCTIAENI---AYGDNSREVSHEEIVKAA------KEanihsfidslpdkyntRVGDKGTQLSG 308
Cdd:COG0410    76 arlgIGYVPEGRRIFpSLTVEENLllgAYARRDRAEVRADLERVYelfprlKE----------------RRRQRAGTLSG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALdteSEKIVQEALDK----AREGRTCIMI---AHRLSTIqnADKIAVIQNGKV 381
Cdd:COG0410   140 GEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRI 214

                         250
                  ....*....|.
gi 1495939436 382 VEQGTHQQLLA 392
Cdd:COG0410   215 VLEGTAAELLA 225
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 164-388 1.10e-28

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 112.41  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEM-----LFD-GKNAKTLNIQ 237
Cdd:PRK11124    2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDfSKTPSDKAIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQE----PILfdcTIAEN-IAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSG 308
Cdd:PRK11124   79 ELRRNVGMVFQQynlwPHL---TVQQNlIEAPCRVLGLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGT 386
Cdd:PRK11124  145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224


                  ..
gi 1495939436 387 HQ 388
Cdd:PRK11124  225 AS 226
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
186-410 1.16e-28

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 115.32  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlNIQWLRAQIGIVSQEPILF-DCTIAENIAYG 264
Cdd:PRK11607   38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQNIAFG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 265 DNSREVSHEEIVKAAKE--ANIHSfidslpDKYNTRvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTE-SE 341
Cdd:PRK11607  116 LKQDKLPKAEIASRVNEmlGLVHM------QEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRD 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 342 KIVQEALD-KAREGRTCIMIAH-RLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLVNVqsGSCNM 410
Cdd:PRK11607  187 RMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI--GSVNV 255
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 178-380 1.24e-28

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 117.34  E-value: 1.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdP---LDGEMLFDGKNAKTLNIQWL-RAQIGIVSQEPILF 253
Cdd:PRK13549   16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 -DCTIAENIAYGdnsREVSH------EEIVKAAKE--ANIHSFIDSlpdkyNTRVGDkgtqLSGGQKQRIAIARALVRQP 324
Cdd:PRK13549   95 kELSVLENIFLG---NEITPggimdyDAMYLRAQKllAQLKLDINP-----ATPVGN----LGLGQQQLVEIAKALNKQA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 325 QILLLDEATSALdTESE-----KIVQealDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGK 380
Cdd:PRK13549  163 RLLILDEPTASL-TESEtavllDIIR---DLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 165-385 1.33e-28

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: 111.15  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWlrAQIG 244
Cdd:cd03268     1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFD-CTIAENIAYGDNSREVSHEEIVKAAKEANIHsfidslpdkynTRVGDKGTQLSGGQKQRIAIARALVRQ 323
Cdd:cd03268    76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGN 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEAL-DKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:cd03268   145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 179-385 1.46e-28

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 111.22  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlraQIGIVSQEPILF-DCTI 257
Cdd:cd03269    12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLPEERGLYpKMKV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 258 AENIAYGDNSREVSHEEIVKAAKEAnIHSFidSLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPQILLLDEATSALD 337
Cdd:cd03269    88 IDQLVYLAQLKGLKKEEARRRIDEW-LERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1495939436 338 TESEKIVQEAL-DKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:cd03269   161 PVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 178-379 2.01e-28

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: 111.27  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQ----IGIVSQEPILF 253
Cdd:cd03290    12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 DCTIAENIAYGDNSREVSHEEIVKAAkeaNIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEAT 333
Cdd:cd03290    92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1495939436 334 SALDTE-SEKIVQEALDK--AREGRTCIMIAHRLSTIQNADKIAVIQNG 379
Cdd:cd03290   169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 177-385 2.42e-28

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: 111.21  E-value: 2.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 177 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLD---GEMLFDGKnakTLNIQWLRAQIGIVSQEPILF 253
Cdd:cd03234    17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDQFQKCVAYVRQDDILL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 DC-TIAENIAYGDNSRevSHEEIVKAAKEANIHSFidSLPDKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPQILLLDE 331
Cdd:cd03234    94 PGlTVRETLTYTAILR--LPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 332 ATSALDTESE-KIVQEALDKAREGRTCIMIAH--RLSTIQNADKIAVIQNGKVVEQG 385
Cdd:cd03234   170 PTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 182-391 2.87e-28

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 111.68  E-value: 2.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF---YDP---LDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILF-D 254
Cdd:PRK14246   25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIAENIAYGDNSREVSHEEIVKAAKEANIHSFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:PRK14246  105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 335 ALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLL 391
Cdd:PRK14246  183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
cbiO PRK13649
energy-coupling factor transporter ATPase;
164-393 3.16e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 112.15  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK----NAKTLNIQ 237
Cdd:PRK13649    2 GINLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVKAAKEA-NIHSFIDSLPDKyntrvgdKGTQLSGGQKQRI 314
Cdd:PRK13649   82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 315 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK13649  155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234


                  .
gi 1495939436 393 E 393
Cdd:PRK13649  235 D 235
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
168-393 4.82e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 111.72  E-value: 4.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 168 KDVAFNYPNRPEVK---ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW-LRAQI 243
Cdd:PRK13633    8 KNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVK----AAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIA 317
Cdd:PRK13633   88 GMVFQNPdnQIVATIVEEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK13633  157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 182-394 4.95e-28

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 111.44  E-value: 4.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA---QIGIVSQepilfDCTIA 258
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ-----DSPSA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 259 EN--IAYGDNSRE-VSH-EEIVKAAKEANIHSFID--SLPDKYNTRVGdkgTQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:TIGR02769 101 VNprMTVRQIIGEpLRHlTSLDESEQKARIAELLDmvGLRSEDADKLP---RQLSGGQLQRINIARALAVKPKLIVLDEA 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 333 TSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAEK 394
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
PTZ00243 PTZ00243
ABC transporter; Provisional
 163-402 5.63e-28

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 116.80  E-value: 5.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  163 GSLTVKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 241
Cdd:PTZ00243  1307 GSLVFEGVQMRYrEGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  242 QIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 321
Cdd:PTZ00243  1385 QFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  322 -RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQL-LAEKGIYYS 399
Cdd:PTZ00243  1462 kKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHS 1541


                   ...
gi 1495939436  400 LVN 402
Cdd:PTZ00243  1542 MVE 1544
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 165-385 5.90e-28

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 109.59  E-value: 5.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTlALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIG 244
Cdd:cd03264     1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFD-CTIAENIAY-----GDNSREVsHEEIVKAAKEANihsfidsLPDKYNTRVGdkgtQLSGGQKQRIAIAR 318
Cdd:cd03264    76 YLPQEFGVYPnFTVREFLDYiawlkGIPSKEV-KARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQ 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:cd03264   144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 197-392 6.83e-28

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: 112.89  E-value: 6.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 197 ALVGSSGCGKSTVVQL---LERfydP------LDGEMLFDGKNAktlniQWL---RAQIGIVSQEPILFD-CTIAENIAY 263
Cdd:COG4148    29 ALFGPSGSGKTTLLRAiagLER---PdsgrirLGGEVLQDSARG-----IFLpphRRRIGYVFQEARLFPhLSVRGNLLY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 264 G-----DNSREVSHEEIVKAAkeaNIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALDT 338
Cdd:COG4148   101 GrkrapRAERRISFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 339 ES--------EKIVQE----------ALDKARegrtcimiahRLstiqnADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:COG4148   167 ARkaeilpylERLRDEldipilyvshSLDEVA----------RL-----ADHVVLLEQGRVVASGPLAEVLS 223
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 182-401 8.93e-28

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: 116.16  E-value: 8.93e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlraqIGIVSQEPILFDCTIAENI 261
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  262 AYGDNSREVSHEEIVKAAKeanIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESE 341
Cdd:TIGR01271  508 IFGLSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436  342 K-IVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLV 401
Cdd:TIGR01271  585 KeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 180-392 1.23e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 111.59  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 180 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRAQIGIVSQEPilfdct 256
Cdd:PRK11308   28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP------ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 iaeniaYGD-NSRE----------VSHEEIVKAAKEANIHSFIdslpdkynTRVGDKGTQ-------LSGGQKQRIAIAR 318
Cdd:PRK11308  102 ------YGSlNPRKkvgqileeplLINTSLSAAERREKALAMM--------AKVGLRPEHydryphmFSGGQRQRIAIAR 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK11308  168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQElGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 165-377 1.49e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 109.03  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK10247    8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYgdnSREVSHEEIVKAAKEANIHSFidSLPDKyntrVGDKG-TQLSGGQKQRIAIARALVRQ 323
Cdd:PRK10247   85 YCAQTPTLFGDTVYDNLIF---PWQIRNQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFM 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDK-AREGRTCIM-IAHRLSTIQNADKIAVIQ 377
Cdd:PRK10247  156 PKVLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
164-387 1.92e-27

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 108.95  E-value: 1.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEML-----FD---GKNAKTln 235
Cdd:COG4161     2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDfsqKPSEKA-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWLRAQIGIVSQE----PILfdcTIAENIAYG-----DNSREVSHEEIVKAAKEANIHSFIDSLPdkyntrvgdkgTQL 306
Cdd:COG4161    77 IRLLRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 307 SGGQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQ 384
Cdd:COG4161   143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQ 222


                  ...
gi 1495939436 385 GTH 387
Cdd:COG4161   223 GDA 225
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 165-385 2.17e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 109.23  E-value: 2.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKNAKTLNIQWL 239
Cdd:PRK14247    4 IEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 RAQIGIVSQEP-ILFDCTIAENIAYG-------DNSREVshEEIVKAAKEANihsfidSLPDKYNTRVGDKGTQLSGGQK 311
Cdd:PRK14247   81 RRRVQMVFQIPnPIPNLSIFENVALGlklnrlvKSKKEL--QERVRWALEKA------QLWDEVKDRLDAPAGKLSGGQQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 312 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAH------RLStiqnaDKIAVIQNGKVVEQG 385
Cdd:PRK14247  153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 186-394 2.59e-27

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: 111.36  E-value: 2.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVEKGQTLALVGSSGCGKSTVVQL---LERFYDP---LDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPILF-DCTIA 258
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRPDEGeivLNGRTLFDSRKGIFLPPE--KRRIGYVFQEARLFpHLSVR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 259 ENIAYG-----DNSREVSHEEIVKAAkeaNIHSFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEAT 333
Cdd:TIGR02142  94 GNLRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 334 SALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAEK 394
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 182-385 3.55e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 108.78  E-value: 3.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKNAKTLNIQWL--RAQIGIVSQEPILF- 253
Cdd:PRK14267   19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 DCTIAENIAYG------DNSREVSHEEIVKAAKEAnihsfidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQIL 327
Cdd:PRK14267   99 HLTIYDNVAIGvklnglVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 328 LLDEATSALDTESEKIVQEALDKAREGRTCIMIAHrlSTIQNA---DKIAVIQNGKVVEQG 385
Cdd:PRK14267  172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
132-391 9.91e-27

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 110.51  E-value: 9.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 132 KISAAHLFLLFERVPSID-SYSEEGEKPETF----GGSLTVKDVAfnypnrpevkilqglnLKVEKGQTLALVGSSGCGK 206
Cdd:PRK10070    4 KLEIKNLYKIFGEHPQRAfKYIEQGLSKEQIlektGLSLGVKDAS----------------LAIEEGEIFVIMGLSGSGK 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 207 STVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLR----AQIGIVSQE-PILFDCTIAENIAYGDN----SREVSHEEIVK 277
Cdd:PRK10070   68 STMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTVLDNTAFGMElagiNAEERREKALD 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 278 AAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGR 355
Cdd:PRK10070  148 ALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKlqAKHQR 216

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1495939436 356 TCIMIAHRL-STIQNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:PRK10070  217 TIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 25-138 1.22e-26

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 108.33  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV 104
Cdd:cd18577   187 SIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDV 266

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1495939436 105 FLVFSAVVFGAMALGQTSSFAPDYAKAKISAAHL 138
Cdd:cd18577   267 LTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 182-401 1.24e-26

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: 108.02  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlraqIGIVSQEPILFDCTIAENI 261
Cdd:cd03291    52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 262 AYGDNSREVSHEEIVKAAK-EANIHSFidslPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTES 340
Cdd:cd03291   119 IFGVSYDEYRYKSVVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 341 EK-IVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLV 401
Cdd:cd03291   195 EKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
165-362 1.39e-26

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 107.26  E-value: 1.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPN-RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQI 243
Cdd:COG4525     4 LTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILFD-CTIAENIAYGDNSREVSHEEIVKAAKEanihsfidslpdkYNTRVGDKGT------QLSGGQKQRIAI 316
Cdd:COG4525    79 GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGI 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAH 362
Cdd:COG4525   146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 175-385 1.58e-26

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 105.91  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 175 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQEPILFD 254
Cdd:cd03266    13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 -CTIAENIAY-----GDNSREVsHEEIVKAAKEANIHSFIDSlpdkyntRVGDkgtqLSGGQKQRIAIARALVRQPQILL 328
Cdd:cd03266    92 rLTARENLEYfaglyGLKGDEL-TARLEELADRLGMEELLDR-------RVGG----FSTGMRQKVAIARALVHDPPVLL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 329 LDEATSALDTESEKIVQEALDKAREGRTCIMIA-HRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:cd03266   160 LDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
cbiO PRK13641
energy-coupling factor transporter ATPase;
164-394 1.66e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 107.61  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK----NAKTLNIQ 237
Cdd:PRK13641    2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEivkaAKEANIhsfidslpdKYNTRVG------DKGT-QLSG 308
Cdd:PRK13641   82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALDTESEK-IVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGT 386
Cdd:PRK13641  149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHAS 228


                  ....*...
gi 1495939436 387 HQQLLAEK 394
Cdd:PRK13641  229 PKEIFSDK 236
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 165-394 3.01e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 107.48  E-value: 3.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL-------- 234
Cdd:PRK13651    3 IKVKNIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 235 ----------------NIQWLRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVKAAKEanihsFID--SLPDK 294
Cdd:PRK13651   83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIElvGLDES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 295 YNTRvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKA-REGRTCIMIAHRL-STIQNADK 372
Cdd:PRK13651  158 YLQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKR 234

                         250       260
                  ....*....|....*....|...
gi 1495939436 373 IAVIQNGKVVEQG-THQQLLAEK 394
Cdd:PRK13651  235 TIFFKDGKIIKDGdTYDILSDNK 257
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 172-397 4.03e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 107.24  E-value: 4.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 172 FNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQ----LL---------ERFY--DPLDGEMLFDGKNAKTL-N 235
Cdd:PRK13631   31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIkskygtiqvGDIYigDKKNNHELITNPYSKKIkN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWLRAQIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEivkAAKEANIHSFIDSLPDKYNTRvgdKGTQLSGGQKQR 313
Cdd:PRK13631  111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSYLER---SPFGLSGGQKRR 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 314 IAIARALVRQPQILLLDEATSALDTESEK-IVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:PRK13631  185 VAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIF 264


                  ....*.
gi 1495939436 392 AEKGIY 397
Cdd:PRK13631  265 TDQHII 270
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 180-386 4.21e-26

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: 105.51  E-value: 4.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 180 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiQWLRAQIGIVS--QEPILF-DCT 256
Cdd:COG0411    17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFpELT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENIA---------------YGDNSREVSHEEIVKAAKEAnIHSFidSLPDKYNTRVGDkgtqLSGGQKQRIAIARALV 321
Cdd:COG0411    96 VLENVLvaaharlgrgllaalLRLPRARREEREARERAEEL-LERV--GLADRADEPAGN----LSYGQQRRLEIARALA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 322 RQPQILLLDEATSAL-DTESEKIVqEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGT 386
Cdd:COG0411   169 TEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 165-392 5.09e-26

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 109.79  E-value: 5.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKS-TVVQLLERFYDP----LDGEMLFDGKNAKTLNIQW 238
Cdd:PRK15134    6 LAIENLSVAFRQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 239 LRA----QIGIVSQEPIL-------FDCTIAENIA-YGDNSREVSHEEIVKAAKEANIHsfidslpdKYNTRVGDKGTQL 306
Cdd:PRK15134   86 LRGvrgnKIAMIFQEPMVslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 307 SGGQKQRIAIARALVRQPQILLLDEATSALD-TESEKIVQEALDKARE-GRTCIMIAHRLSTI-QNADKIAVIQNGKVVE 383
Cdd:PRK15134  158 SGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQLLRELQQElNMGLLFITHNLSIVrKLADRVAVMQNGRCVE 237


                  ....*....
gi 1495939436 384 QGTHQQLLA 392
Cdd:PRK15134  238 QNRAATLFS 246
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
164-394 6.76e-26

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 105.10  E-value: 6.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 243
Cdd:PRK11231    2 TLRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPIL-FDCTIAENIAYGdNSREVSH--------EEIVKAAKEAnihSFIDSLPDKyntRVgdkgTQLSGGQKQRI 314
Cdd:PRK11231   79 ALLPQHHLTpEGITVRELVAYG-RSPWLSLwgrlsaedNARVNQAMEQ---TRINHLADR---RL----TDLSGGQRQRA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 315 AIARALVRQPQILLLDEATSALD----TESEKIVQEAldkAREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQ 389
Cdd:PRK11231  148 FLAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEE 224


                  ....*
gi 1495939436 390 LLAEK 394
Cdd:PRK11231  225 VMTPG 229
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 165-382 7.06e-26

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 105.17  E-value: 7.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDV--AFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiQWLRAQ 242
Cdd:COG1101     2 LELKNLskTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 -IGIVSQEPILFDC---TIAENIAYGDN---SREVSheeivKAAKEANIHSFIDS-------LPDKYNTRVGdkgtQLSG 308
Cdd:COG1101    81 yIGRVFQDPMMGTApsmTIEENLALAYRrgkRRGLR-----RGLTKKRRELFRELlatlglgLENRLDTKVG----LLSG 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVV 382
Cdd:COG1101   152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 165-395 3.43e-25

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 102.84  E-value: 3.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL---ERfYDPLDGEMLFDGKNAKTLNIQwLRA 241
Cdd:COG0396     1 LEIKNLHVSVEGKE---ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGI-VS-QEPI--------LFDCTIAENIAYGDNSREVSHEEIVKAAKEANihsfidsLPDKYNTR---VGdkgtqLSG 308
Cdd:COG0396    76 RAGIfLAfQYPVeipgvsvsNFLRTALNARRGEELSAREFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIMIAH--RLSTIQNADKIAVIQNGKVVEQG 385
Cdd:COG0396   144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223

                         250
                  ....*....|..
gi 1495939436 386 THQ--QLLAEKG 395
Cdd:COG0396   224 GKElaLELEEEG 235
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 183-379 3.81e-25

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: 102.54  E-value: 3.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQIGIVSQEPILFD-CTIAENI 261
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-----ITEPGPDRMVVFQNYSLLPwLTVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 262 AYGDNS--REVSHEEivkaaKEANIHSFIDSLPdkyNTRVGDKG-TQLSGGQKQRIAIARALVRQPQILLLDEATSALDT 338
Cdd:TIGR01184  76 ALAVDRvlPDLSKSE-----RRAIVEEHIALVG---LTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1495939436 339 ESEKIVQEALDKARE--GRTCIMIAHRL-STIQNADKIAVIQNG 379
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
181-390 5.88e-25

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 104.78  E-value: 5.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 181 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPILF-DCTIAE 259
Cdd:PRK10851   16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 260 NIAYGDN---SREVSHEEIVKAaKEANIHSFI--DSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:PRK10851   94 NIAFGLTvlpRRERPNAAAIKA-KVTQLLEMVqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFG 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 335 ALDTESEKIVQEALDKARE--GRTCIMIAH-RLSTIQNADKIAVIQNGKVVEQGTHQQL 390
Cdd:PRK10851  166 ALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 180-382 1.01e-24

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: 105.68  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 180 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFY--DPLDGEMLFDGKNAKTLNIQWL-RAQIGIVSQEPILF-DC 255
Cdd:TIGR02633  14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAYGD----NSREVSHEEIVKAAKEANIHSFIDSLPdkyNTR-VGDKGtqlsGGQKQRIAIARALVRQPQILLLD 330
Cdd:TIGR02633  94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 331 EATSAL-DTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVV 382
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 179-383 1.02e-24

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: 101.36  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERfydPLDGEMLFDGKNAKTLN----IQWLRAQIGIVSQE-- 249
Cdd:COG4181    24 ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfq 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 250 --PILfdcTIAEN------IAYGDNSREVSHEEIvkaakeanihsfidslpdkynTRVGDKG------TQLSGGQKQRIA 315
Cdd:COG4181   101 llPTL---TALENvmlpleLAGRRDARARARALL---------------------ERVGLGHrldhypAQLSGGEQQRVA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 316 IARALVRQPQILLLDEATSALDTE-SEKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIAVIQNGKVVE 383
Cdd:COG4181   157 LARAFATEPAILFADEPTGNLDAAtGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
164-386 1.62e-24

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 103.38  E-value: 1.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERFydpLDGEMLFDGKNAKTLniqwlr 240
Cdd:PRK11650    3 GLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 241 aqigivsqEPILFDC-------------TIAENIAYGDNSREVSHEEI----VKAAKEANIHSFIDSLPdkyntrvgdkg 303
Cdd:PRK11650   72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIeervAEAARILELEPLLDRKP----------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 304 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTeseKI-VQEALD----KAREGRTCIMIAH-RLSTIQNADKIAVIq 377
Cdd:PRK11650  133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA---KLrVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVM- 208

                         250
                  ....*....|
gi 1495939436 378 NGKVVEQ-GT 386
Cdd:PRK11650  209 NGGVAEQiGT 218
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
165-392 1.67e-24

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 101.45  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNR------PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW 238
Cdd:COG4167     5 LEVRNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 239 L-----------------RAQIGIVSQEPILFdctiaeNIAYGDNSREvshEEIVKAAKEANIhsfidsLPDKYNtrvgD 301
Cdd:COG4167    85 RckhirmifqdpntslnpRLNIGQILEEPLRL------NTDLTAEERE---ERIFATLRLVGL------LPEHAN----F 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 302 KGTQLSGGQKQRIAIARALVRQPQILLLDEATSALD-TESEKIVQEALD-KAREGRTCIMIAHRLSTIQN-ADKIAVIQN 378
Cdd:COG4167   146 YPHMLSSGQKQRVALARALILQPKIIIADEALAALDmSVRSQIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQ 225

                         250
                  ....*....|....
gi 1495939436 379 GKVVEQGTHQQLLA 392
Cdd:COG4167   226 GEVVEYGKTAEVFA 239
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 182-392 1.71e-24

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 105.17  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdPLDGEMLFDGKNAKTLNIQWL---RAQIGIVSQEP---ILFDC 255
Cdd:PRK15134  301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAYGdnsREVSHEEIVKAAKEANIHSFIDSLPDKYNTRvGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSA 335
Cdd:PRK15134  380 NVLQIIEEG---LRVHQPTLSAAQREQQVIAVMEEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 336 LDteseKIVQE---ALDKAREGR---TCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK15134  456 LD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
165-386 2.13e-24

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 101.30  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPN------RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN--- 235
Cdd:PRK10419    4 LNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWLRAQIGIVSQEPI-LFDC--TIAENIA--------YGDNSREVSHEEIVKAAKEANihSFIDSLPdkyntrvgdkgT 304
Cdd:PRK10419   84 RKAFRRDIQMVFQDSIsAVNPrkTVREIIReplrhllsLDKAERLARASEMLRAVDLDD--SVLDKRP-----------P 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKV 381
Cdd:PRK10419  151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQI 230


                  ....*
gi 1495939436 382 VEQGT 386
Cdd:PRK10419  231 VETQP 235
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
165-406 2.15e-24

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 105.58  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPE-VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL---- 239
Cdd:PRK10535    5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 RAQIGIVSQE-PILFDCTIAENIaygdnsrEVS--HEEIVKAAKEANIHSFIDSLpdKYNTRVGDKGTQLSGGQKQRIAI 316
Cdd:PRK10535   85 REHFGFIFQRyHLLSHLTAAQNV-------EVPavYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKG 395
Cdd:PRK10535  156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAG 235

                         250
                  ....*....|.
gi 1495939436 396 IYYSLVNVQSG 406
Cdd:PRK10535  236 GTEPVVNTASG 246
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 165-386 2.39e-24

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 100.29  E-value: 2.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL-RAQI 243
Cdd:TIGR03410   1 LEVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILF-DCTIAENIAYGDNSREVSHEEIVkaakeANIHSFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVR 322
Cdd:TIGR03410  78 AYVPQGREIFpRLTVEENLLTGLAALPRRSRKIP-----DEIYELFPVLKEMLGRRGGD----LSGGQQQQLAIARALVT 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 323 QPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGT 386
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
GguA NF040905
sugar ABC transporter ATP-binding protein;
178-383 2.67e-24

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 104.49  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdP---LDGEMLFDGKNAKTLNI-QWLRAQIGIVSQE---- 249
Cdd:NF040905   12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKDIrDSEALGIVIIHQElali 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 250 PILfdcTIAENIAYGDnsrEVSH------EEIVKAAKE--ANIhsfidSLPDKYNTRVGDKGTqlsgGQKQRIAIARALV 321
Cdd:NF040905   91 PYL---SIAENIFLGN---ERAKrgvidwNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALS 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 322 RQPQILLLDEATSAL-DTESEKIVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVE 383
Cdd:NF040905  156 KDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
165-392 3.75e-24

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 100.85  E-value: 3.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQ 242
Cdd:PRK13638    2 LATSDLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANihsfidSLPDKYNTRvgDKGTQ-LSGGQKQRIAIARA 319
Cdd:PRK13638   79 VATVFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL------TLVDAQHFR--HQPIQcLSHGQKKRVAIAGA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 320 LVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK13638  151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 162-381 4.15e-24

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 100.14  E-value: 4.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 162 GGSLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLfdgknAKTLNIQWLRA 241
Cdd:PRK11247   10 GTPLLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEARE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPILFDC-TIAENIAYG--DNSREVSHEeivkaAKEANihsfidSLPDkyntRVGDKGTQLSGGQKQRIAIAR 318
Cdd:PRK11247   82 DTRLMFQDARLLPWkKVIDNVGLGlkGQWRDAALQ-----ALAAV------GLAD----RANEWPAALSGGQKQRVALAR 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKV 381
Cdd:PRK11247  147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 164-391 4.98e-24

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 99.85  E-value: 4.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 243
Cdd:PRK13548    2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPIL-FDCTIAENIAYG--DNSREVSH-EEIVKAA-KEANIHSFIDSLpdkYntrvgdkgTQLSGGQKQRIAIAR 318
Cdd:PRK13548   79 AVLPQHSSLsFPFTVEEVVAMGraPHGLSRAEdDALVAAAlAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 319 ALVR------QPQILLLDEATSALD-TESEKIVQEALDKARE-GRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQ 389
Cdd:PRK13548  148 VLAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227


                  ..
gi 1495939436 390 LL 391
Cdd:PRK13548  228 VL 229
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 165-383 9.79e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 102.84  E-value: 9.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFdGKNAKtlniqwlraqIG 244
Cdd:COG0488   316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDC--TIAENIAygdnsrevsheEIVKAAKEANIHSFIDSL---PDKYNTRVGDkgtqLSGGQKQRIAIARA 319
Cdd:COG0488   382 YFDQHQEELDPdkTVLDELR-----------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 320 LVRQPQILLLDEATSALDTESEKIVQEALDkAREGrTCIMIAH-R--LSTIqnADKIAVIQNGKVVE 383
Cdd:COG0488   447 LLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
cbiO PRK13645
energy-coupling factor transporter ATPase;
160-393 1.42e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 99.70  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 160 TFGGSLTVKDVAFNYPNRP--EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL-----LERFYDPLDGEMLFDGKNAK 232
Cdd:PRK13645    2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 233 TLNIQWLRAQIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEanihsFID--SLPDKYNTRvgdKGTQLSG 308
Cdd:PRK13645   82 IKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPE-----LLKlvQLPEDYVKR---SPFELSG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQ---EALDKaREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQ 384
Cdd:PRK13645  154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFInlfERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISI 232

                         250
                  ....*....|....*
gi 1495939436 385 G------THQQLLAE 393
Cdd:PRK13645  233 GspfeifSNQELLTK 247
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
165-362 1.74e-23

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 98.62  E-value: 1.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQIG 244
Cdd:PRK11248    2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQ-EPILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIhsfidslpdkyntRVGDKGT------QLSGGQKQRIAIA 317
Cdd:PRK11248   74 VVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIA 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAH 362
Cdd:PRK11248  141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
PLN03232 PLN03232
ABC transporter C family member; Provisional
 89-401 2.78e-23

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 102.75  E-value: 2.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436   89 FGAYLVVNGHMEYKNVFLVFSAVVFGAMALGQTSSFAPDYAKAKIS---AAHLFLLFERVPSIDSYSEEGEKpetfggSL 165
Cdd:PLN03232   542 FGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSlqrIEELLLSEERILAQNPPLQPGAP------AI 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  166 TVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQllerfydpldgEMLFDGKNAKTLNIQwLRAQIGI 245
Cdd:PLN03232   616 SIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS-----------AMLGELSHAETSSVV-IRGSVAY 683

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  246 VSQEPILFDCTIAENIAYGDnsrEVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQ 325
Cdd:PLN03232   684 VPQVSWIFNATVRENILFGS---DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436  326 ILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKGIYYSLV 401
Cdd:PLN03232   761 IYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 165-393 2.81e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 98.34  E-value: 2.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYpnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK13652    4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVKAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 318
Cdd:PRK13652   82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSAlhmlGLEELRDRVPH-----------HLSGGEKKRVAIAG 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK13652  151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 179-384 3.38e-23

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 97.16  E-value: 3.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW---LRAQ-IGIVSQEPILFD 254
Cdd:PRK10584   22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIA-ENIAY-----GDNSREvSHEEIVKAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPQILL 328
Cdd:PRK10584  102 TLNAlENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 329 LDEATSALDTES-EKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIAVIQNGKVVEQ 384
Cdd:PRK10584  170 ADEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
164-385 3.39e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 99.72  E-value: 3.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlNIQWLRAQI 243
Cdd:PRK11000    3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILF-DCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVR 322
Cdd:PRK11000   78 GMVFQSYALYpHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDR-------KPKALSGGQRQRVAIGRTLVA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 323 QPQILLLDEATSALDTE---SEKIVQEALDKaREGRTCIMIAH-RLSTIQNADKIAVIQNGKVVEQG 385
Cdd:PRK11000  151 EPSVFLLDEPLSNLDAAlrvQMRIEISRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 181-390 7.28e-23

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 98.24  E-value: 7.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 181 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-IQWL--RAQIGIVSQEPILF---D 254
Cdd:PRK15079   35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIAENIA------YGDNSREVSHEEiVKA--AKEANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPQI 326
Cdd:PRK15079  115 MTIGEIIAeplrtyHPKLSRQEVKDR-VKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKL 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 327 LLLDEATSALDTESEKIVQEALDK-ARE-GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQL 390
Cdd:PRK15079  183 IICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
cbiO PRK13643
energy-coupling factor transporter ATPase;
168-393 9.61e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 97.11  E-value: 9.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 168 KDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEM----LFDGKNAKTLNIQWLRA 241
Cdd:PRK13643    5 EKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVK-AAKEANIHSFIDSLPDKyntrvgdKGTQLSGGQKQRIAIAR 318
Cdd:PRK13643   85 KVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEK-------SPFELSGGQMRRVAIAG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK13643  158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 165-392 1.21e-22

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: 95.69  E-value: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIqWLRAQIG 244
Cdd:cd03218     1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 I--VSQEPILF-DCTIAENIAYGDNSREVSHEEIVKAAkEANIHSF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARAL 320
Cdd:cd03218    77 IgyLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARAL 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 321 VRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIA-HRLS-TIQNADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:cd03218   149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 167-381 1.27e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 99.75  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGknaktlniqwlRAQIGIV 246
Cdd:COG0488     1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQEPILFD-CTIAENIAYGDNSR--------------EVSHEEIVKAAK-------------EANIHSFIDSL---PDKY 295
Cdd:COG0488    67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleaklAEPDEDLERLAElqeefealggweaEARAEEILSGLgfpEEDL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 296 NTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTESekiVQ--EALDKAREGrTCIMIAH-R--LSTIqnA 370
Cdd:COG0488   147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--A 216

                         250
                  ....*....|.
gi 1495939436 371 DKIAVIQNGKV 381
Cdd:COG0488   217 TRILELDRGKL 227
PTZ00243 PTZ00243
ABC transporter; Provisional
 153-385 1.46e-22

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 100.62  E-value: 1.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  153 EEGEKPETFGGSLTVKDVAFnYPNRPEVkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMlfdgknak 232
Cdd:PTZ00243   648 EATPTSERSAKTPKMKTDDF-FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------- 717

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  233 tlniqWLRAQIGIVSQEPILFDCTIAENIAYGDNSREVSHEEIVKAAK-EANIHSfidsLPDKYNTRVGDKGTQLSGGQK 311
Cdd:PTZ00243   718 -----WAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQlEADLAQ----LGGGLETEIGEKGVNLSGGQK 788

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436  312 QRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQG 385
Cdd:PTZ00243   789 ARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 183-390 1.91e-22

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: 94.74  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG----KNAKTLniqwlRAQIGIVSQEPILFD-CTI 257
Cdd:cd03265    16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREV-----RRRIGIVFQDLSVDDeLTG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 258 AENIA-----YGdNSREVSHEEIVKAAKEANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:cd03265    91 WENLYiharlYG-VPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 333 TSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGTHQQL 390
Cdd:cd03265   159 TIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
183-367 1.93e-22

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 94.94  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNA---KTLNIQWLRAQIGIVSQEP-ILFDCTIA 258
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRTVY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 259 ENIAYgdnsrevshEEIVKAAKEANIHSFIDSLPDKyntrVG--DKG----TQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK10908   98 DNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1495939436 333 TSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTI 367
Cdd:PRK10908  165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 179-385 2.02e-22

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: 94.13  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLDGEMLFDGKNAKTLNIQwLRAQIGI--VSQEPILFd 254
Cdd:cd03217    12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEI- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 ctiaENIAYGDNSREVsheeivkaakeanihsfidslpdkyntrvgDKGtqLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:cd03217    90 ----PGVKNADFLRYV------------------------------NEG--FSGGEKKRNEILQLLLLEPDLAILDEPDS 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 335 ALDTESEKIVQEALDKAR-EGRTCIMIAH--RLSTIQNADKIAVIQNGKVVEQG 385
Cdd:cd03217   134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
cbiO PRK13646
energy-coupling factor transporter ATPase;
164-394 2.77e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 96.00  E-value: 2.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPN-RP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG----KNAKTLNIQ 237
Cdd:PRK13646    2 TIRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRAQIGIVSQ--EPILFDCTIAENIAYG--------DNSREVSHEEIVKAAKEANIHSfidSLPdkyntrvgdkgTQLS 307
Cdd:PRK13646   82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpknfkmnlDEVKNYAHRLLMDLGFSRDVMS---QSP-----------FQMS 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 308 GGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAR--EGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQ 384
Cdd:PRK13646  148 GGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQ 227

                         250
                  ....*....|
gi 1495939436 385 GTHQQLLAEK 394
Cdd:PRK13646  228 TSPKELFKDK 237
PLN03130 PLN03130
ABC transporter C family member; Provisional
 138-392 4.13e-22

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 99.04  E-value: 4.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  138 LFLLFERV----PSIDSyseegEKPetfggSLTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL 213
Cdd:PLN03130   594 LLLAEERVllpnPPLEP-----GLP-----AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  214 ErfydpldGEMlfdgkNAKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSREVSHEeivKAAKEANIHSFIDSLPD 293
Cdd:PLN03130   664 L-------GEL-----PPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYE---RAIDVTALQHDLDLLPG 728

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  294 KYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTIQNADK 372
Cdd:PLN03130   729 GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDR 808

                          250       260
                   ....*....|....*....|
gi 1495939436  373 IAVIQNGKVVEQGTHQQLLA 392
Cdd:PLN03130   809 IILVHEGMIKEEGTYEELSN 828
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 179-386 6.28e-22

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 95.18  E-value: 6.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTlniqwlRAQIGIVSQEPILF-DC 255
Cdd:COG4152    13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEplDPED------RRRIGYLPEERGLYpKM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAY-----GdnsreVSHEEIVKAAKEanihsFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILL 328
Cdd:COG4152    87 KVGEQLVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 329 LDEATSALDTES-EKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGT 386
Cdd:COG4152   153 LDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
179-392 6.81e-22

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 94.27  E-value: 6.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL-------------NIQWLRAQIGI 245
Cdd:PRK10619   17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEPILFD-CTIAENIAYGDN-----SREVSHEEIVKAAKEANIHsfiDSLPDKYNTrvgdkgtQLSGGQKQRIAIARA 319
Cdd:PRK10619   97 VFQHFNLWShMTVLENVMEAPIqvlglSKQEARERAVKYLAKVGID---ERAQGKYPV-------HLSGGQQQRVSIARA 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 320 LVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK10619  167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 161-392 7.18e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 94.39  E-value: 7.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 161 FGGSLTVKDVAFNYPNRPevkilqglnlkvekgqTLALVGSSGCGKSTVVQLLERFYDPLDG-----EMLFDGKNA-KTL 234
Cdd:PRK14271   31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 235 NIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFidSLPDKYNTRVGDKGTQLSGGQKQRI 314
Cdd:PRK14271   95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 315 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK14271  173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 165-379 8.25e-22

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: 93.27  E-value: 8.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVA--FNYPNRPEVKI--LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKN-----AKTLN 235
Cdd:COG4778     5 LEVENLSktFTLHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWL---RAQIGIVSQ---------------EPILfdctiaeniaygdnSREVSHEEIVKAAKEA----NIHSFIDSLPD 293
Cdd:COG4778    85 REILalrRRTIGYVSQflrviprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 294 kyNTrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKA-REGRTCIMIAHRLSTIQN-AD 371
Cdd:COG4778   151 --AT--------FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvAD 220


                  ....*...
gi 1495939436 372 KIAVIQNG 379
Cdd:COG4778   221 RVVDVTPF 228
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
169-394 1.46e-21

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 94.90  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 169 DVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQ 248
Cdd:PRK13536   46 GVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 249 epilFD-----CTIAENIA-----YGDNSREVsheeivkaakEANIHSFID--SLPDKYNTRVGDkgtqLSGGQKQRIAI 316
Cdd:PRK13536  122 ----FDnldleFTVRENLLvfgryFGMSTREI----------EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDK--AReGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK13536  184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262


                  .
gi 1495939436 394 K 394
Cdd:PRK13536  263 H 263
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 165-391 3.12e-21

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 94.52  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNypnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK09536    4 IDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPIL-FDCTIAENIAYGDN---SREVSHEEIVKAAKE-----ANIHSFIDSlpdkyntrvgdKGTQLSGGQKQRIA 315
Cdd:PRK09536   81 SVPQDTSLsFEFDVRQVVEMGRTphrSRFDTWTETDRAAVEramerTGVAQFADR-----------PVTSLSGGERQRVL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESE-KIVQEALDKAREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:PRK09536  150 LARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 142-405 3.51e-21

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: 96.24  E-value: 3.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  142 FERVPSIDSYSEEGEKPETFGGS------------LTVKDVA--FNYPNRPEVkilQGLNLKVEKGQTLALVGSSGCGKS 207
Cdd:TIGR01257  894 LEKTEPLTEEMEDPEHPEGINDSfferelpglvpgVCVKNLVkiFEPSGRPAV---DRLNITFYENQITAFLGHNGAGKT 970

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  208 TVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQEPILFD-CTIAENIAYGDNSREVSHEEiVKAAKEANIHS 286
Cdd:TIGR01257  971 TTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEE-AQLEMEAMLED 1048

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  287 fiDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLST 366
Cdd:TIGR01257 1049 --TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1495939436  367 IQN-ADKIAVIQNGKVVEQGTHQQL--LAEKGIYYSLV----NVQS 405
Cdd:TIGR01257 1123 ADLlGDRIAIISQGRLYCSGTPLFLknCFGTGFYLTLVrkmkNIQS 1168
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 165-378 8.46e-21

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: 88.36  E-value: 8.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPN-RPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--------ERFYDPLDGEMLFdgknaktln 235
Cdd:cd03223     1 IELENLSLATPDgRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMPEGEDLLF--------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 iqwlraqigiVSQEPILFDCTIAENIAYgdnsrevsheeivkaakeanihsfidslPdkyntrvgdKGTQLSGGQKQRIA 315
Cdd:cd03223    69 ----------LPQRPYLPLGTLREQLIY----------------------------P---------WDDVLSGGEQQRLA 101

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 316 IARALVRQPQILLLDEATSALDTESEKIVQEALDKarEGRTCIMIAHRLSTIQNADKIAVIQN 378
Cdd:cd03223   102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
174-371 1.40e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 88.83  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 174 YPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlrAQIGIVSQ---EP 250
Cdd:NF040873    2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseVP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 251 ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFidslpdkynTRVGDKG------TQLSGGQKQRIAIARALVRQP 324
Cdd:NF040873   68 DSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEA 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1495939436 325 QILLLDEATSALDTESEKIVQEAL-DKAREGRTCIMIAHRLSTIQNAD 371
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
167-390 1.44e-20

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 90.59  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL---RAQI 243
Cdd:PRK11831   10 MRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEPILF-DCTIAENIAYgdNSREVSH--EEIVKAAKEANIHSfidslpdkyntrVGDKG------TQLSGGQKQRI 314
Cdd:PRK11831   87 SMLFQSGALFtDMNVFDNVAY--PLREHTQlpAPLLHSTVMMKLEA------------VGLRGaaklmpSELSGGMARRA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 315 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQL 390
Cdd:PRK11831  153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
178-393 1.61e-20

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 93.44  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQ-WLRAQIGIVSQEPILF-DC 255
Cdd:PRK11288   15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEM 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAYGD--NSREVSHEEIVKA-AKEANIHSFIDSLPDkynTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK11288   95 TVAENLYLGQlpHKGGIVNRRLLNYeAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 333 TSALDT-ESE---KIVQEALDkarEGRTCIMIAHRLSTI-QNADKIAVIQNGKVVE------QGTHQQLLAE 393
Cdd:PRK11288  168 TSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLVQA 236
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 165-385 3.16e-20

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 93.00  E-value: 3.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRP--------EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN- 235
Cdd:PRK10261  314 LQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 --IQWLRAQIGIVSQEPilfdctiaeniaYGD-NSREVSHEEIVKAAKeanIHSFIDSLPDKYNT-----RVGDKGT--- 304
Cdd:PRK10261  394 gkLQALRRDIQFIFQDP------------YASlDPRQTVGDSIMEPLR---VHGLLPGKAAAARVawlleRVGLLPEhaw 458

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 ----QLSGGQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKARE-GRTCIMIAHRLSTIQN-ADKIAVIQ 377
Cdd:PRK10261  459 ryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMY 538


                  ....*...
gi 1495939436 378 NGKVVEQG 385
Cdd:PRK10261  539 LGQIVEIG 546
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
177-392 5.65e-20

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 88.69  E-value: 5.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 177 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPI----- 251
Cdd:PRK15112   23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnp 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 252 ------LFDCTIAENIAYGDNSREvshEEIVKAAKEANIhsfidsLPDKYNTRvgdkGTQLSGGQKQRIAIARALVRQPQ 325
Cdd:PRK15112  103 rqrisqILDFPLRLNTDLEPEQRE---KQIIETLRQVGL------LPDHASYY----PHMLAPGQKQRLGLARALILRPK 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 326 ILLLDEATSALD-TESEKIVQEALD-KAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK15112  170 VIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
165-396 5.75e-20

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 88.01  E-value: 5.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlniQW-----L 239
Cdd:PRK11614    6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWqtakiM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 RAQIGIVSQEPILFD-CTIAENIAYGD--NSREVSHEEIVKAakeanihsfIDSLPDKYNTRVGDKGTqLSGGQKQRIAI 316
Cdd:PRK11614   79 REAVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALdteSEKIVQEALDKAR----EGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:PRK11614  149 GRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225


                  ....*
gi 1495939436 392 AEKGI 396
Cdd:PRK11614  226 ANEAV 230
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 165-392 1.43e-19

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: 90.63  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLDGEML----------------F 226
Cdd:TIGR03269   1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 227 DGKNAK----TLNIQ----W---------LRAQIGIVSQEPILF--DCTIAENIAYGDNSREVSHEEIVKAAKEanihsF 287
Cdd:TIGR03269  78 VGEPCPvcggTLEPEevdfWnlsdklrrrIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVD-----L 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 288 IDSLpdKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKA--REGRTCIMIAHRLS 365
Cdd:TIGR03269 153 IEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPE 230

                         250       260
                  ....*....|....*....|....*...
gi 1495939436 366 TIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:TIGR03269 231 VIEDlSDKAIWLENGEIKEEGTPDEVVA 258
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
181-407 1.74e-19

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 87.38  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 181 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL----------ERFYDPLDGEMLFDGKNAKtlNIQWLRAQIGIVSQEP 250
Cdd:PRK09984   18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 251 ILFD-CTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLpdkynTRVG------DKGTQLSGGQKQRIAIARALVRQ 323
Cdd:PRK09984   96 NLVNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALD--KAREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQLLAEK--GIYY 398
Cdd:PRK09984  171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfdHLYR 250


                  ....*....
gi 1495939436 399 SLVNVQSGS 407
Cdd:PRK09984  251 SINRVEENA 259
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 158-385 1.74e-19

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: 86.43  E-value: 1.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 158 PETFGGSLTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlnIQ 237
Cdd:cd03220    13 YKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 W-LRAQIGIVSQ----EPILFDCTIaeniaYGdnsreVSHEEIvkAAKEANIHSFIDsLPDKYNTRVGdkgtQLSGGQKQ 312
Cdd:cd03220    87 SlLGLGGGFNPEltgrENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQG 385
Cdd:cd03220   150 RLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 165-380 2.15e-19

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: 84.04  E-value: 2.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLerfydpldgemlfdgknaktlniqwlraqig 244
Cdd:cd03221     1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 ivsqepilfdctiaeniaygdNSREVSHEEIVKAAKEANIHSFidslpdkyntrvgdkgTQLSGGQKQRIAIARALVRQP 324
Cdd:cd03221    47 ---------------------AGELEPDEGIVTWGSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 325 QILLLDEATSALDTESEKIVQEALdKAREGrTCIMIAHRLSTIQN-ADKIAVIQNGK 380
Cdd:cd03221    90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 162-386 2.39e-19

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 86.67  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 162 GGSLTVKDVAFN--YPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlnIQWL 239
Cdd:COG1134    19 EPSRSLKELLLRrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 raqIGI-VSQEPILfdcTIAENI-----AYGdnsreVSHEEIVKAAKE----ANIHSFIDsLPDKYntrvgdkgtqLSGG 309
Cdd:COG1134    93 ---LELgAGFHPEL---TGRENIylngrLLG-----LSRKEIDEKFDEivefAELGDFID-QPVKT----------YSSG 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 310 QKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGT 386
Cdd:COG1134   151 MRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 165-393 2.87e-19

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: 89.48  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNY--PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLF-------DGKNAKTLN 235
Cdd:TIGR03269 280 IKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKPGPDG 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWLRAQIGIVSQEPILF-DCTIAENIaygdnSREVSHEEIVKAAKEANIHSF-IDSLPDKYNTRVGDKGT-QLSGGQKQ 312
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELSEGERH 434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQ 389
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEE 514


                  ....
gi 1495939436 390 LLAE 393
Cdd:TIGR03269 515 IVEE 518
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 183-381 3.28e-19

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: 84.41  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI-QWLRAQIGIVSQEP----ILFDCTI 257
Cdd:cd03215    16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLSV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 258 AENIAygdnsrevsheeivkaakeanihsfidsLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALD 337
Cdd:cd03215    96 AENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1495939436 338 TES-EKIVQEALDKAREGRTCIMIahrlST-----IQNADKIAVIQNGKV 381
Cdd:cd03215   137 VGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 24-116 5.98e-19

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 86.16  E-value: 5.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  24 FKVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKN 103
Cdd:pfam00664 180 SSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGD 259

                          90
                  ....*....|....*
gi 1495939436 104 --VFLVFSAVVFGAM 116
Cdd:pfam00664 260 lvAFLSLFAQLFGPL 274
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
182-391 7.76e-19

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 85.81  E-value: 7.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPIL-FDCTIAEN 260
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 261 IAYG--------DNSREVSHEEIVKAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK10253  102 VARGryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLLDEP 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 333 TSALDTESEKIVQEALDK--AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:PRK10253  171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 178-380 1.00e-18

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 87.75  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAkTLN--IQWLRAQIGIVSQEPILFD- 254
Cdd:PRK10762   15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNgpKSSQEAGIGIIHQELNLIPq 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIAENIAYGdnsREVSHeeIVKAAKEANIHSFIDSLPDKYN------TRVGDkgtqLSGGQKQRIAIARALVRQPQILL 328
Cdd:PRK10762   94 LTIAENIFLG---REFVN--RFGRIDWKKMYAEADKLLARLNlrfssdKLVGE----LSIGEQQMVEIAKVLSFESKVII 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 329 LDEATSAL-DTESE---KIVQEALDkarEGRTCIMIAHRLSTI-QNADKIAVIQNGK 380
Cdd:PRK10762  165 MDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 179-402 1.62e-18

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 84.31  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 179 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLDGEMLFDGKNAKTLNIQwLRAQIGI----------- 245
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 -VSQEPILfdctiaeNIAYgdNSREVSHEEivkaaKEANIHSFIDSLPDKYNTrVGDKGTQL--------SGGQKQRIAI 316
Cdd:CHL00131   98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAH--RLSTIQNADKIAVIQNGKVVEQGTHQ--QLL 391
Cdd:CHL00131  163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKEL 242

                         250
                  ....*....|.
gi 1495939436 392 AEKGiyYSLVN 402
Cdd:CHL00131  243 EKKG--YDWLK 251
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 151-383 2.49e-18

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 86.95  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 151 YSEEGEKPETFGG--SLTVKDVAFNYPNRP-EVKilqGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFD 227
Cdd:PRK10522  307 YKAEFPRPQAFPDwqTLELRNVTFAYQDNGfSVG---PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 228 GKNAKTLNIQWLRAQIGIVSQEPILFDCTIaeniayGDNSrevsheeivKAAKEANIHSFIDSLPDKYNTRVGD---KGT 304
Cdd:PRK10522  384 GKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEG---------KPANPALVEKWLERLKMAHKLELEDgriSNL 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIV-QEALDKARE-GRTCIMIAHRLSTIQNADKIAVIQNGKVV 382
Cdd:PRK10522  449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLS 528


                  .
gi 1495939436 383 E 383
Cdd:PRK10522  529 E 529
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
182-365 2.71e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 83.33  E-value: 2.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW---LRAQ-IGIVSQ-EPILFDCT 256
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENIAY----GDNSREVSHE---EIVKAAKEANihsfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPQILLL 329
Cdd:PRK11629  104 ALENVAMplliGKKKPAEINSralEMLAAVGLEH--------------RANHRPSELSGGERQRVAIARALVNNPRLVLA 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1495939436 330 DEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLS 365
Cdd:PRK11629  170 DEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 180-385 3.81e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 86.26  E-value: 3.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 180 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIGI--VSQEPILF-DCT 256
Cdd:PRK15439   24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 336
Cdd:PRK15439  103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 337 D-TESEKI---VQEALDKareGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQG 385
Cdd:PRK15439  172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 177-391 6.41e-18

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 85.87  E-value: 6.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 177 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLErFYDPldGEMLFDGK---NAKTLNIQWLRAQIGIVSQEPILF 253
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSP--KGVKGSGSvllNGMPIDAKEMRAISAYVQQDDLFI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 -DCTIAENIAYGDNSRevSHEEIVKAAKEANIHSFID--SLPDKYNTRVGDKGTQ--LSGGQKQRIAIARALVRQPQILL 328
Cdd:TIGR00955 112 pTLTVREHLMFQAHLR--MPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 329 LDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLST--IQNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
165-382 1.92e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 83.91  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVafnypNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLerF-YDPLD-GEMLFDGKNAKTLNI-QWLRA 241
Cdd:COG1129   257 LEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgADPADsGEIRLDGKPVRIRSPrDAIRA 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVS----QEPILFDCTIAENIAYGdNSREVSHEEIVKAAKEANI-HSFIDSLpdkyNTRVGDKGT---QLSGGQKQR 313
Cdd:COG1129   328 GIAYVPedrkGEGLVLDLSIRENITLA-SLDRLSRGGLLDRRRERALaEEYIKRL----RIKTPSPEQpvgNLSGGNQQK 402

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 314 IAIARALVRQPQILLLDEATSALD--TESE--KIVQEAldkAREGRTCIMIahrlST-----IQNADKIAVIQNGKVV 382
Cdd:COG1129   403 VVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRIV 473
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
156-391 2.51e-17

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 81.37  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 156 EKPETFGGSLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN 235
Cdd:PRK10575    3 EYTNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQWLRAQIGIVSQE-PILFDCTIAENIA------------YGDNSREVSHEEIVKAAKEANIHSFIDSLpdkyntrvgdk 302
Cdd:PRK10575   80 SKAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDSL----------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 303 gtqlSGGQKQRIAIARALVRQPQILLLDEATSALD----TESEKIVQEaLDKAReGRTCIMIAHRLS-TIQNADKIAVIQ 377
Cdd:PRK10575  149 ----SGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHR-LSQER-GLTVIAVLHDINmAARYCDYLVALR 222

                         250
                  ....*....|....
gi 1495939436 378 NGKVVEQGTHQQLL 391
Cdd:PRK10575  223 GGEMIAQGTPAELM 236
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 161-390 3.72e-17

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 80.42  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 161 FGGSLTVKDVAFNypnrpevkilqglnlkVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLr 240
Cdd:PRK11300   15 FGGLLAVNNVNLE----------------VREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 241 AQIGIVS--QEPILF-DCTIAENI--------------------AYgdnsREVSHEEIVKAAkeanihSFID--SLPDKY 295
Cdd:PRK11300   78 ARMGVVRtfQHVRLFrEMTVIENLlvaqhqqlktglfsgllktpAF----RRAESEALDRAA------TWLErvGLLEHA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 296 NTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADK 372
Cdd:PRK11300  148 NRQAGN----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDR 223

                         250
                  ....*....|....*...
gi 1495939436 373 IAVIQNGKVVEQGTHQQL 390
Cdd:PRK11300  224 IYVVNQGTPLANGTPEEI 241
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 169-390 4.94e-17

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 82.98  E-value: 4.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 169 DVAFNYpNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE-----MLFDGKNAKTLNI------- 236
Cdd:PRK10261   19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkMLLRRRSRQVIELseqsaaq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 237 -QWLR-AQIGIVSQEPI-----LFdcTIAENIAYGDNSRE-VSHEEIVKAAKEanihsFIDS--LPDKyNTRVGDKGTQL 306
Cdd:PRK10261   98 mRHVRgADMAMIFQEPMtslnpVF--TVGEQIAESIRLHQgASREEAMVEAKR-----MLDQvrIPEA-QTILSRYPHQL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 307 SGGQKQRIAIARALVRQPQILLLDEATSALDTESE-------KIVQEALDKAregrtCIMIAHRLSTIQN-ADKIAVIQN 378
Cdd:PRK10261  170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQ 244

                         250
                  ....*....|..
gi 1495939436 379 GKVVEQGTHQQL 390
Cdd:PRK10261  245 GEAVETGSVEQI 256
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
182-392 6.32e-17

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 80.62  E-value: 6.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQ----EPilfDCTI 257
Cdd:PRK13537   22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQfdnlDP---DFTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 258 AENIA-----YGDNSREVshEEIVKAAKEanihsfIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK13537   98 RENLLvfgryFGLSAAAA--RALVPPLLE------FAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 333 TSALDTESEKIVQEALDK--AReGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLA 392
Cdd:PRK13537  166 TTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 156-385 6.79e-17

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: 79.30  E-value: 6.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 156 EKPETFGGSLTvkdvAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGknaktlN 235
Cdd:cd03267    14 SKEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------L 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 236 IQW-----LRAQIGIV--SQEPILFDCTIAENIA-----YGdnsrevsheeIVKAAKEANIHSFIDSLPdkyNTRVGDKG 303
Cdd:cd03267    84 VPWkrrkkFLRRIGVVfgQKTQLWWDLPVIDSFYllaaiYD----------LPPARFKKRLDELSELLD---LEELLDTP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 304 T-QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIMIAHRLSTIQN-ADKIAVIQNG 379
Cdd:cd03267   151 VrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKG 230


                  ....*.
gi 1495939436 380 KVVEQG 385
Cdd:cd03267   231 RLLYDG 236
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 163-392 6.89e-17

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 79.30  E-value: 6.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 163 GSLTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVvqllerFY------DPLDGEMLFDGKNAKTLNI 236
Cdd:COG1137     2 MTLEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 237 qWLRAQIGI--VSQEPILF-DCTIAENIA----YGDNSREVSHEEIVKAAKEANIHSFIDSlpdkyntrvgdKGTQLSGG 309
Cdd:COG1137    73 -HKRARLGIgyLPQEASIFrKLTVEDNILavleLRKLSKKEREERLEELLEEFGITHLRKS-----------KAYSLSGG 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 310 QKQRIAIARALVRQPQILLLDEATSALD----TESEKIVQEALDK----------AREgrtcimiahrlsTIQNADKIAV 375
Cdd:COG1137   141 ERRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKERgigvlitdhnVRE------------TLGICDRAYI 208

                         250
                  ....*....|....*..
gi 1495939436 376 IQNGKVVEQGTHQQLLA 392
Cdd:COG1137   209 ISEGKVLAEGTPEEILN 225
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 165-390 9.32e-17

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 80.54  E-value: 9.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKD--VAFNYPNrPEVKILQGLNLKVEKGQTLALVGSSGCGKS-TVVQLLERFYDP--LDGEMLFDGKN-----AKTL 234
Cdd:PRK09473   13 LDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 235 NIqwLRA-QIGIVSQEPIlfdCTIAENIAYGDNSREV--SHEEIVKA-AKEANIHsFIDS--LPDKyNTRVGDKGTQLSG 308
Cdd:PRK09473   92 NK--LRAeQISMIFQDPM---TSLNPYMRVGEQLMEVlmLHKGMSKAeAFEESVR-MLDAvkMPEA-RKRMKMYPHEFSG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALD-TESEKIVQEALDKAREGRTC-IMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:PRK09473  165 GMRQRVMIAMALLCRPKLLIADEPTTALDvTVQAQIMTLLNELKREFNTAiIMITHDLGVVAGiCDKVLVMYAGRTMEYG 244


                  ....*
gi 1495939436 386 THQQL 390
Cdd:PRK09473  245 NARDV 249
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 166-397 2.57e-16

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 78.20  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 166 TVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGI 245
Cdd:COG4604     3 EIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEP-ILFDCTIAENIAYG------------DnsrevshEEIVKAAkeanIHSF-IDSLPDKYNTrvgdkgtQLSGGQK 311
Cdd:COG4604    80 LRQENhINSRLTVRELVAFGrfpyskgrltaeD-------REIIDEA----IAYLdLEDLADRYLD-------ELSGGQR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 312 QRIAIARALVRQPQILLLDEATSALD----TESEKIVQEAldkARE-GRTCIMIAHRLstiqN-----ADKIAVIQNGKV 381
Cdd:COG4604   142 QRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRV 214

                         250
                  ....*....|....*....
gi 1495939436 382 VEQGTHQQLLAE---KGIY 397
Cdd:COG4604   215 VAQGTPEEIITPevlSDIY 233
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 12-331 3.41e-16

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: 80.23  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  12 EQLFHHFpdiaffkvaTEVIENIRTVAsLTRERKFELmYGEHLQVP---YRNSVKKAH-IFGFCFALSQAMMFFTYAGCF 87
Cdd:COG4615   183 DRLFKHF---------RALLEGFKELK-LNRRRRRAF-FDEDLQPTaerYRDLRIRADtIFALANNWGNLLFFALIGLIL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  88 rfgaYLVVNGHMEYKNVFLVFSAVV-FGAMALGQTSSFAPDYAKAKISA---AHLFLLFERVPSIDSYSEEGEKPETFGg 163
Cdd:COG4615   252 ----FLLPALGWADPAVLSGFVLVLlFLRGPLSQLVGALPTLSRANVALrkiEELELALAAAEPAAADAAAPPAPADFQ- 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRPEVK--ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 241
Cdd:COG4615   327 TLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEPILFDCTIAENiayGDNSREVSHEEIVKAAkeanihsfidsLPDKynTRVGDKG---TQLSGGQKQRIAIAR 318
Cdd:COG4615   407 LFSAVFSDFHLFDRLLGLD---GEADPARARELLERLE-----------LDHK--VSVEDGRfstTDLSQGQRKRLALLV 470

                         330
                  ....*....|...
gi 1495939436 319 ALVRQPQILLLDE 331
Cdd:COG4615   471 ALLEDRPILVFDE 483
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 165-391 3.64e-16

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 77.66  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL----- 239
Cdd:PRK11701    7 LSVRGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaer 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 ----RAQIGIVSQEP---ILFDCTIAENI-----AYGDNSrevsHEEIVKAAKEANIHSFIDSlpdkynTRVGDKGTQLS 307
Cdd:PRK11701   84 rrllRTEWGFVHQHPrdgLRMQVSAGGNIgerlmAVGARH----YGDIRATAGDWLERVEIDA------ARIDDLPTTFS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 308 GGQKQRIAIARALVRQPQILLLDEATSALDTEsekiVQ-EALDKARE-----GRTCIMIAHRLSTIQN-ADKIAVIQNGK 380
Cdd:PRK11701  154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGR 229

                         250
                  ....*....|.
gi 1495939436 381 VVEQGTHQQLL 391
Cdd:PRK11701  230 VVESGLTDQVL 240
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
178-385 5.65e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 79.44  E-value: 5.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQ--IGIVSQEPILFD- 254
Cdd:PRK09700   16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQELSVIDe 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIAENIAYGDN-SREVSHEEIV---KAAKEANIHSFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLD 330
Cdd:PRK09700   95 LTVLENLYIGRHlTKKVCGVNIIdwrEMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMD 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 331 EATSAL-DTESEKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:PRK09700  171 EPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 178-382 2.09e-15

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 77.85  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNiQWLRAQIGIVSQE-PILFD 254
Cdd:PRK10982    9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSK-EALENGISMVHQElNLVLQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 CTIAENIAYGDNSRE---VSHEEIVKAAKeanihSFIDSLPDKYNTRvgDKGTQLSGGQKQRIAIARALVRQPQILLLDE 331
Cdd:PRK10982   88 RSVMDNMWLGRYPTKgmfVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 332 ATSALdTESE-----KIVQEALDKareGRTCIMIAHRLSTI-QNADKIAVIQNGKVV 382
Cdd:PRK10982  161 PTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQWI 213
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 177-376 2.14e-15

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: 74.45  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 177 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPILFDCT 256
Cdd:cd03231    10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENIAY--GDNSREvsheEIVKAAKEANIHSFIDsLPdkyntrvgdkGTQLSGGQKQRIAIARALVRQPQILLLDEATS 334
Cdd:cd03231    90 VLENLRFwhADHSDE----QVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1495939436 335 ALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKIAVI 376
Cdd:cd03231   155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
186-385 3.40e-15

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 76.07  E-value: 3.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVE-----KGQTlALVGSSGCGKSTVVQLLERFYDP------LDGEMLFDgkNAKTLNIQWLRAQIGIVSQEPILF- 253
Cdd:PRK11144   13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPqkgrivLNGRVLFD--AEKGICLPPEKRRIGYVFQDARLFp 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 254 DCTIAENIAYG-DNSREVSHEEIVKAAKeanihsfIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK11144   90 HYKVRGNLRYGmAKSMVAQFDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEP 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 333 TSALDTESEKIVQEALDK-AREGRTCIM-IAHRLSTI-QNADKIAVIQNGKVVEQG 385
Cdd:PRK11144  156 LASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 165-346 9.03e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 72.60  E-value: 9.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAfnyPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiqwLRAQIG 244
Cdd:PRK13539    3 LEGEDLA---CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQ----EPILfdcTIAENIA-----YGDnsrevsHEEIVKAAKEA-NIHSFIDsLPDKYntrvgdkgtqLSGGQKQRI 314
Cdd:PRK13539   77 YLGHrnamKPAL---TVAENLEfwaafLGG------EELDIAAALEAvGLAPLAH-LPFGY----------LSAGQKRRV 136

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1495939436 315 AIARALVRQPQILLLDEATSALDTESEKIVQE 346
Cdd:PRK13539  137 ALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 162-382 1.16e-14

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 71.89  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 162 GGSLTVKDVAFNYP-NRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-ERFYDPL-DGEMLFDGK-NAKTLNIQ 237
Cdd:cd03232     1 GSVLTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRpLDKNFQRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 wlraqIGIVSQEPILFDC-TIAENIAYGDNSREVSHEeivkaakeanihsfidslpdkyntrvgdkgtqlsggQKQRIAI 316
Cdd:cd03232    81 -----TGYVEQQDVHSPNlTVREALRFSALLRGLSVE------------------------------------QRKRLTI 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLS--TIQNADKIAVIQ-NGKVV 382
Cdd:cd03232   120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKrGGKTV 189
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 144-365 1.90e-14

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: 75.17  E-value: 1.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 144 RVPSIDSYSEEGEKPETFGGSLTVKDVaFN---YPNRPEV-----KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLE- 214
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVEYQ-DNgikFENIPLVtpngdVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGe 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 215 -------RFYDPLDGEMLFdgknaktlniqwlraqigiVSQEPILFDCTIAENIAYGDNS-----REVSHEEIVKAAKEA 282
Cdd:TIGR00954 501 lwpvyggRLTKPAKGKLFY-------------------VPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLEQILDNV 561

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 283 NIHSFIdslpdkynTR------VGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAreGRT 356
Cdd:TIGR00954 562 QLTHIL--------EReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GIT 631


                  ....*....
gi 1495939436 357 CIMIAHRLS 365
Cdd:TIGR00954 632 LFSVSHRKS 640
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 165-382 2.02e-14

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 74.68  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVafNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERfyDPLDGEMLFDGKNAKTLNI-QWLRA 241
Cdd:COG3845   258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRL 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEP-----ILfDCTIAENIAYGDNSRE-------VSHEEIVKAAKEanihsfidsLPDKYNTRVGDKGT---QL 306
Cdd:COG3845   334 GVAYIPEDRlgrglVP-DMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEE---------LIEEFDVRTPGPDTparSL 403

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 307 SGGQKQRIAIARALVRQPQILLLDEATSALDTES-EKIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVV 382
Cdd:COG3845   404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 165-373 2.73e-14

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: 71.24  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNypnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:TIGR01189   1 LAARNLACS---RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYgdnsrevsheeivkaakEANIHSFIDSLPDKYNTRVGDKG------TQLSGGQKQRIAIAR 318
Cdd:TIGR01189  78 LGHLPGLKPELSALENLHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALAR 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTcIMIAHRLSTIQNADKI 373
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAhlARGGIV-LLTTHQDLGLVEAREL 196
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 164-396 5.15e-14

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 71.08  E-value: 5.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI-QWLRAQ 242
Cdd:PRK10895    3 TLTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEPILFD-CTIAENIA-----YGDNSREVSHEEIVKAAKEANIHSFIDSLpdkyntrvgdkGTQLSGGQKQRIAI 316
Cdd:PRK10895   80 IGYLPQEASIFRrLSVYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 317 ARALVRQPQILLLDEATSALDTES----EKIVQEALDKareGRTCIMIAHRL-STIQNADKIAVIQNGKVVEQGTHQQLL 391
Cdd:PRK10895  149 ARALAANPKFILLDEPFAGVDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225


                  ....*
gi 1495939436 392 AEKGI 396
Cdd:PRK10895  226 QDEHV 230
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 176-363 1.19e-13

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 69.60  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 176 NRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDgknaktlniqwlraqigiVSQEPILFDC 255
Cdd:COG2401    39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENIAYGDNsrevsheeiVKAAKEAnIHSFidSLPDKYNTRVgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSA 335
Cdd:COG2401   101 SLIDAIGRKGD---------FKDAVEL-LNAV--GLSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 1495939436 336 LDTESEKIVQEALDKA--REGRTCIMIAHR 363
Cdd:COG2401   167 LDRQTAKRVARNLQKLarRAGITLVVATHH 196
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 165-393 1.65e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 69.96  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFnyPNRpevkiLQGLNLKVEKGQTLALVGSSGCGKSTvvqLLERFYDPLD--GEMLFDGKNAKTLNIQWLRAQ 242
Cdd:PRK03695    1 MQLNDVAV--STR-----LGPLSAEVRAGEILHLVGPNGAGKST---LLARMAGLLPgsGSIQFAGQPLEAWSAAELARH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQE---PILFDCtiaenIAYGDNSRevsHEEIVKAAKEANIHSFIDS--LPDKYNTRVGdkgtQLSGGQKQRIAIA 317
Cdd:PRK03695   71 RAYLSQQqtpPFAMPV-----FQYLTLHQ---PDKTRTEAVASALNEVAEAlgLDDKLGRSVN----QLSGGEWQRVRLA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 318 RALVR-------QPQILLLDEATSALDtesekIVQE-ALDK-----AREGRTCIMIAHRLS-TIQNADKIAVIQNGKVVE 383
Cdd:PRK03695  139 AVVLQvwpdinpAGQLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLA 213

                         250
                  ....*....|
gi 1495939436 384 QGTHQQLLAE 393
Cdd:PRK03695  214 SGRRDEVLTP 223
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 189-386 1.94e-13

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 70.54  E-value: 1.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 189 KVEKGQTLALVGSSGCGKST---VVQLLERFYDPLDGEML-FDGKNAKTLNIQWLR----AQIGIVSQEPI--LFDC--- 255
Cdd:PRK11022   29 SVKQGEVVGIVGESGSGKSVsslAIMGLIDYPGRVMAEKLeFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPCytv 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 --TIAENI-AYGDNSREVSHEEIVKAAKEANIhsfidslPDKyNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:PRK11022  109 gfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGI-------PDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 333 TSALD-TESEKIVQEALD-KAREGRTCIMIAHRLSTI-QNADKIAVIQNGKVVEQGT 386
Cdd:PRK11022  181 TTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 165-395 2.08e-13

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 69.43  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLDGEMLFDGKNAKTLNIQwLRAQ 242
Cdd:PRK09580    2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGI--VSQEPI-------LFDCTIAENIAygdnsREVSHEEivkAAKEANIHSFID------SLPDKYNTRVGDKGtqLS 307
Cdd:PRK09580   78 EGIfmAFQYPVeipgvsnQFFLQTALNAV-----RSYRGQE---PLDRFDFQDLMEekiallKMPEDLLTRSVNVG--FS 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 308 GGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREG-RTCIMIAH--RLSTIQNADKIAVIQNGKVVEQ 384
Cdd:PRK09580  148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKS 227

                         250
                  ....*....|...
gi 1495939436 385 GTHQ--QLLAEKG 395
Cdd:PRK09580  228 GDFTlvKQLEEQG 240
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 165-364 2.48e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 69.37  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwLRaqIG 244
Cdd:PRK09544    5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEpILFDCTIAENIAYGDNSRE-VSHEEIVKAAKEANIHSFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQ 323
Cdd:PRK09544   71 YVPQK-LYLDTTLPLTVNRFLRLRPgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNR 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1495939436 324 PQILLLDEATSALDTESEKIVQEALDKAREGRTC--IMIAHRL 364
Cdd:PRK09544  139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCavLMVSHDL 181
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 192-368 3.26e-13

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: 66.63  E-value: 3.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  192 KGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMlfdgknaktlniqwlraqigivsqepILFDCtiaeniaygDNSREVS 271
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDG---------EDILEEV 45

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  272 HEEIVkaakeanihsfidslpdkyNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD-- 349
Cdd:smart00382  46 LDQLL-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106

                          170       180
                   ....*....|....*....|....
gi 1495939436  350 -----KAREGRTCIMIAHRLSTIQ 368
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLG 130
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 156-392 1.10e-12

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 68.19  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 156 EKPETFGGSLTvkdvAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG----KNA 231
Cdd:COG4586    15 EKEPGLKGALK----GLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 232 KTLniqwlRAQIGIV----SQepILFDCTIAEniaygdnSREVSHE--EIVKAAKEANIHSFID--SLPDKYNTRVgdkg 303
Cdd:COG4586    91 KEF-----ARRIGVVfgqrSQ--LWWDLPAID-------SFRLLKAiyRIPDAEYKKRLDELVEllDLGELLDTPV---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 304 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQN-ADKIAVIQNGK 380
Cdd:COG4586   153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGR 232

                         250
                  ....*....|..
gi 1495939436 381 VVEQGTHQQLLA 392
Cdd:COG4586   233 IIYDGSLEELKE 244
PLN03211 PLN03211
ABC transporter G-25; Provisional
 161-392 1.54e-12

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 69.14  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 161 FGGSLTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTvvqLLERFYDPLDGEMlFDGK---NAKTLNIQ 237
Cdd:PLN03211   65 LGHKPKISDETRQIQER---TILNGVTGMASPGEILAVLGPSGSGKST---LLNALAGRIQGNN-FTGTilaNNRKPTKQ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 238 WLRaQIGIVSQEPILF-DCTIAENIAYGDNSR---EVSHEEIVKAAkEANIHSFidSLPDKYNTRVGDKGTQ-LSGGQKQ 312
Cdd:PLN03211  138 ILK-RTGFVTQDDILYpHLTVRETLVFCSLLRlpkSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERK 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 313 RIAIARALVRQPQILLLDEATSALD-TESEKIVQEALDKAREGRTCIMIAHRLST--IQNADKIAVIQNGKVVEQGTHQQ 389
Cdd:PLN03211  214 RVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSD 293


                  ...
gi 1495939436 390 LLA 392
Cdd:PLN03211  294 AMA 296
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 165-381 2.33e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 68.42  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdP--LDGEMLFDGKNAKTLN-IQWLRA 241
Cdd:PRK13549  260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKPVKIRNpQQAIAQ 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEP----ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNT---RVGdkgtQLSGGQKQRI 314
Cdd:PRK13549  339 GIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKA 414

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 315 AIARALVRQPQILLLDEATSALDT----ESEKIVQEAldkAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKV 381
Cdd:PRK13549  415 VLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 165-392 2.48e-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: 68.31  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-PLDGEMLFDGKNAKTLN-IQWLRAQ 242
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAG 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 243 IGIVSQEP----ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLpdKYNTRVGDKG-TQLSGGQKQRIAIA 317
Cdd:TIGR02633 338 IAMVPEDRkrhgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLA 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 318 RALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKV----VEQG-THQQL 390
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLkgdfVNHAlTQEQV 495


                  ..
gi 1495939436 391 LA 392
Cdd:TIGR02633 496 LA 497
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 176-381 3.92e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 67.45  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 176 NRPEVkilQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-----------IQWLRAQIG 244
Cdd:PRK10982  260 RQPSI---RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYGDNSREVSHEEIvkaakEANIHSFIDSLPDK---YNTRVGdkgtQLSGGQKQRIAIARALV 321
Cdd:PRK10982  337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 322 RQPQILLLDEATSALDTESE-KIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKV 381
Cdd:PRK10982  408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 174-385 4.59e-12

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 65.49  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 174 YPNRPEVKilqGLNLKVEKGQTLALVGSSGCGKS----TVVQLLERFYDPLDGEMLFDGKnakTLNIQWLRAQ-IGIVSQ 248
Cdd:PRK10418   13 QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRGRkIATIMQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 249 EP--------ILFDCTIAENIAYGDNSREVSHEEIVKAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARAL 320
Cdd:PRK10418   87 NPrsafnplhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALAL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 321 VRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:PRK10418  156 LCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 182-394 1.42e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 66.13  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLerfydplDGEMLFD-GKnaktLNIqwlrAQIGIVS---QEP------I 251
Cdd:PRK11147   18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGR----IIY----EQDLIVArlqQDPprnvegT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 252 LFDcTIAENIA--------YGDNSREVSHEE----IVKAAK-------------EANIHSFIDSL---PDKyntrvgdKG 303
Cdd:PRK11147   83 VYD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------AL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 304 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALdKAREGrTCIMIAHRLSTIQN-ADKIAVIQNGKVV 382
Cdd:PRK11147  155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232

                         250
                  ....*....|...
gi 1495939436 383 E-QGTHQQLLAEK 394
Cdd:PRK11147  233 SyPGNYDQYLLEK 245
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 165-371 1.73e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 63.05  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 244
Cdd:PRK13540    2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDCTIAENIAYG--DNSREVSHEEIVKAAKEANIHSFIDSLpdkyntrvgdkgtqLSGGQKQRIAIARALVR 322
Cdd:PRK13540   79 VGHRSGINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1495939436 323 QPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIMIAHRLSTIQNAD 371
Cdd:PRK13540  145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 187-393 2.34e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 65.04  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 187 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE----------MLFDgKNAKTLNIQWLRAQIGIVSQEPILFDCT 256
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFE-QLQKLVSDEWQRNNTDMLSPGEDDTGRT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENIAYGDNSREVSHEeivkAAKEANIHSFIDSlPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEATSAL 336
Cdd:PRK10938  102 TAEIIQDEVKDPARCEQ----LAQQFGITALLDR-RFKY----------LSTGETRKTLLCQALMSEPDLLILDEPFDGL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 337 DTESEKIVQEALDK-AREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK10938  167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 165-396 2.39e-11

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 65.30  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEmlfdgknaktlnIQWL-RAQI 243
Cdd:PRK15064  320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT------------VKWSeNANI 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GIVSQEP--------ILFDCtIAENIAYGDNSREV---------SHEEIVKAAKeanihsfidslpdkyntrvgdkgtQL 306
Cdd:PRK15064  385 GYYAQDHaydfendlTLFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VL 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 307 SGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKArEGrTCIMIAH-R--LSTIqnADKIAVIQNGKVVE 383
Cdd:PRK15064  440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSL--ATRIIEITPDGVVD 515

                         250
                  ....*....|....
gi 1495939436 384 -QGTHQQLLAEKGI 396
Cdd:PRK15064  516 fSGTYEEYLRSQGI 529
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
164-385 4.84e-11

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 62.98  E-value: 4.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 164 SLTVKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 243
Cdd:PRK15056    6 GIVVNDVTVTWRNGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 GiVSQE-----PILFDCTIAENiAYGDNS---REVSHE-EIVKAAKEAnihsfIDSLPDKYNtRVGdkgtQLSGGQKQRI 314
Cdd:PRK15056   84 P-QSEEvdwsfPVLVEDVVMMG-RYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRV 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 315 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIMIAHRLSTIQNADKIAVIQNGKVVEQG 385
Cdd:PRK15056  152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 25-145 4.89e-11

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 62.96  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV 104
Cdd:cd18557   176 QVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGEL 255

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1495939436 105 --FLVFSAVVfgAMALGQTSSFAPDYAKAkISAAhlfllfERV 145
Cdd:cd18557   256 tsFILYTIMV--ASSVGGLSSLLADIMKA-LGAS------ERV 289
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 175-340 7.84e-11

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 63.80  E-value: 7.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 175 PNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTvvqlLERFYDPLDGEmlFDGKNAKTLNIQwlraqIGIVSQEPILFD 254
Cdd:TIGR03719  16 PKK---EILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDKD--FNGEARPQPGIK-----VGYLPQEPQLDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 C-TIAENI-------------------AYGDNSREVSH--------EEIVKAAKEANIHSFIDSLPDKYNTRVGD-KGTQ 305
Cdd:TIGR03719  82 TkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKlaaeqaelQEIIDAADAWDLDSQLEIAMDALRCPPWDaDVTK 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1495939436 306 LSGGQKQRIAIARALVRQPQILLLDEATSALDTES 340
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
hmuV PRK13547
heme ABC transporter ATP-binding protein;
182-386 3.11e-10

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 60.61  E-value: 3.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 182 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLE-RFYDP-------LDGEMLFDGKNAKTLNIQWL---RAQIGIVSQEP 250
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 251 ILFdcTIAENIAYG-----DNSREVSHE--EIVKAAKEanihsfidsLPDKyNTRVGDKGTQLSGGQKQRIAIARAL--- 320
Cdd:PRK13547   96 FAF--SAREIVLLGryphaRRAGALTHRdgEIAWQALA---------LAGA-TALVGRDVTTLSGGELARVQFARVLaql 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 321 ------VRQPQILLLDEATSALD-TESEKIVQEALDKAREGRTCIM-IAHRLS-TIQNADKIAVIQNGKVVEQGT 386
Cdd:PRK13547  164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLGVLaIVHDPNlAARHADRIAMLADGAIVAHGA 238
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
177-362 7.24e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 58.28  E-value: 7.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 177 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL------NIQWLRAQIGIVSqep 250
Cdd:PRK13538   11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKT--- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 251 ilfDCTIAENIA-YGDNSREVSHEEIVKAAKEANIHSFIDsLPDKyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLL 329
Cdd:PRK13538   88 ---ELTALENLRfYQRLHGPGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1495939436 330 DEATSALDTESEKIVQEALDK-AREGRTCIMIAH 362
Cdd:PRK13538  154 DEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 186-398 7.86e-10

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: 61.18  E-value: 7.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  186 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQEPILFDC-TIAENIAYG 264
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLlTGREHLYLY 2036

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  265 DNSREVSHEEIVKAA----KEANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPQILLLDEATSALDTES 340
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  341 EKIVQEAL-DKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAEKGIYY 398
Cdd:TIGR01257 2106 RRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGDGY 2165
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 174-348 1.15e-09

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 58.57  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 174 YPNRPEVKILQGLNLKVEKG-----QTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAkTLNIQWLRA-QIGIVS 247
Cdd:cd03237     1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKAdYEGTVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 248 QepILFDCTiaeNIAYGDNSREVsheEIVKAAKeanihsfIDSLPDKyntRVgdkgTQLSGGQKQRIAIARALVRQPQIL 327
Cdd:cd03237    80 D--LLSSIT---KDFYTHPYFKT---EIAKPLQ-------IEQILDR---EV----PELSGGELQRVAIAACLSKDADIY 137

                         170       180
                  ....*....|....*....|.
gi 1495939436 328 LLDEATSALDTESEKIVQEAL 348
Cdd:cd03237   138 LLDEPSAYLDVEQRLMASKVI 158
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 190-383 1.29e-09

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 60.18  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 190 VEKGQTLALVGSSGCGKSTVVQLLErfydpldGEMLFDGKNAkTLNIQWlraQIGIVSQEPILFDCTIAENIAYGDnsRE 269
Cdd:PRK10636   24 INPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSY-TFPGNW---QLAWVNQETPALPQPALEYVIDGD--RE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 270 VSH-EEIVKAAKEAN-------IHSFIDSLpDKYNTR---------VGDKGTQL-------SGGQKQRIAIARALVRQPQ 325
Cdd:PRK10636   91 YRQlEAQLHDANERNdghaiatIHGKLDAI-DAWTIRsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSD 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 326 ILLLDEATSALDTESeKIVQEALDKAREGrTCIMIAHR---LSTIqnADKIAVIQNGKVVE 383
Cdd:PRK10636  170 LLLLDEPTNHLDLDA-VIWLEKWLKSYQG-TLILISHDrdfLDPI--VDKIIHIEQQSLFE 226
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 104-379 4.59e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.58  E-value: 4.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  104 VFLVFSAVVF-----GAMALGQTSSF----APDYAKAKISAAHLFLLFERVP---------SIDSYSEEGEKPETFGGSL 165
Cdd:TIGR00956  680 VFFFFVYILLtefnkGAKQKGEILVFrrgsLKRAKKAGETSASNKNDIEAGEvlgstdltdESDDVNDEKDMEKESGEDI 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  166 TV-KDVAFNYPNRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-ERFYDPL--DGEMLFDGknaKTLNIQWLR 240
Cdd:TIGR00956  760 FHwRNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGVitGGDRLVNG---RPLDSSFQR 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  241 AqIGIVSQEPI-LFDCTIAENI---AYGDNSREVSHEEivkaaKEANIHSFIDSLP-DKY-NTRVGDKGTQLSGGQKQRI 314
Cdd:TIGR00956  837 S-IGYVQQQDLhLPTSTVRESLrfsAYLRQPKSVSKSE-----KMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRL 910

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436  315 AIARALVRQPQILL-LDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTI--QNADKIAVIQNG 379
Cdd:TIGR00956  911 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 183-386 4.82e-09

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 56.85  E-value: 4.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVqlLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG---IVSQEPI-------- 251
Cdd:cd03271    11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIgrtprsnp 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 252 -----LFD------CTIAENIAYGDNSREVSH---------EEIVKAAKE-----ANIHSFIDSLPD---KYnTRVGDKG 303
Cdd:cd03271    89 atytgVFDeirelfCEVCKGKRYNRETLEVRYkgksiadvlDMTVEEALEffeniPKIARKLQTLCDvglGY-IKLGQPA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 304 TQLSGGQKQRIAIARALVRQ---PQILLLDEATSALDTESEKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIAVI--- 376
Cdd:cd03271   168 TTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWIIDLgpe 247

                         250
                  ....*....|...
gi 1495939436 377 ---QNGKVVEQGT 386
Cdd:cd03271   248 ggdGGGQVVASGT 260
PLN03073 PLN03073
ABC transporter F family; Provisional
 165-381 2.29e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.02  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLfdgKNAKTlniqwlraQIG 244
Cdd:PLN03073  509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKV--------RMA 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPIlfdctiaeniaygdNSREVSHEEIVKAAK------EANIHSFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIAR 318
Cdd:PLN03073  576 VFSQHHV--------------DGLDLSSNPLLYMMRcfpgvpEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAK 640

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGrtCIMIAHRLSTIQNA-DKIAVIQNGKV 381
Cdd:PLN03073  641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKV 702
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 175-385 2.61e-08

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: 53.81  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 175 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKST----VVQLLERFYDPlDGEMLFDGKNAKTLNIQWlRAQIGIVSQEp 250
Cdd:cd03233    15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 251 ilfDCTIAEniaygdnsreVSHEEIVKAAKEANIHSFIdslpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPQILLLD 330
Cdd:cd03233    92 ---DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWD 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 331 EATSALDTESE-KIVQEALDKAREGRTCIMIahrlSTIQNA-------DKIAVIQNGKVVEQG 385
Cdd:cd03233   144 NSTRGLDSSTAlEILKCIRTMADVLKTTTFV----SLYQASdeiydlfDKVLVLYEGRQIYYG 202
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
172-391 2.75e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 55.69  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 172 FNYPNRP------EVKILQG------LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnakTLNIQWL 239
Cdd:PRK11288  246 YGYRPRPlgevrlRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK---PIDIRSP 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 RAQI--GIV------SQEPILFDCTIAENIAYGDNSREVSHEEIVKAAKEA-NIHSFIDSLPDKynTRVGD-KGTQLSGG 309
Cdd:PRK11288  323 RDAIraGIMlcpedrKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGG 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 310 QKQRIAIARALVRQPQILLLDEATSALD--TESEkIVQEALDKAREGRTCIMIAHRLSTIQN-ADKIAVIQNGKVV---- 382
Cdd:PRK11288  401 NQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgela 479

                         250
                  ....*....|
gi 1495939436 383 -EQGTHQQLL 391
Cdd:PRK11288  480 rEQATERQAL 489
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 167-349 3.14e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 55.73  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLerfydpldgemlfdgknaktlnIQWLRAQIGIV 246
Cdd:PRK11147  322 MENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM----------------------LGQLQADSGRI 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SqepilfdCTIAENIAYGDNSREV-------------SHEEIVKAAKEANIHSFI-DSL--PDKYNTRVgdkgTQLSGGQ 310
Cdd:PRK11147  377 H-------CGTKLEVAYFDQHRAEldpektvmdnlaeGKQEVMVNGRPRHVLGYLqDFLfhPKRAMTPV----KALSGGE 445

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1495939436 311 KQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD 349
Cdd:PRK11147  446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 178-340 3.96e-08

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 55.12  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 178 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE-MLFDGknaktlniqwlrAQIGIVSQEPIL-FDC 255
Cdd:PRK11819   18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG------------IKVGYLPQEPQLdPEK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 256 TIAENI-------------------AYGDNSREVSH--------EEIVKAAKEANIHSFID------SLPDkyntrvGD- 301
Cdd:PRK11819   86 TVRENVeegvaevkaaldrfneiyaAYAEPDADFDAlaaeqgelQEIIDAADAWDLDSQLEiamdalRCPP------WDa 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1495939436 302 KGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTES 340
Cdd:PRK11819  160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 168-371 4.67e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.02  E-value: 4.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 168 KDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-----ERFYDPL--------DGEMLFDGKNaktl 234
Cdd:PRK10938  264 NNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSNDLtlfgrrrgSGETIWDIKK---- 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 235 niqwlraQIGIVSQEPIL---FDCTIAENIAYG--DN---SREVSHEEIVKAAKEANIHSFidslpdkyNTRVGDKGTQ- 305
Cdd:PRK10938  337 -------HIGYVSSSLHLdyrVSTSVRNVILSGffDSigiYQAVSDRQQKLAQQWLDILGI--------DKRTADAPFHs 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 306 LSGGQkQRIA-IARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIM------------IAHRLSTIQNAD 371
Cdd:PRK10938  402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDGD 480
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 165-370 6.18e-08

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 52.57  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFdgKNAKTLNIQ-----WL 239
Cdd:PRK13541    2 LSLHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAkpyctYI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 240 RAQIGIVSqepilfDCTIAENIAYGdnSREVSHEEIVKAAkeanIHSF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIAR 318
Cdd:PRK13541   76 GHNLGLKL------EMTVFENLKFW--SEIYNSAETLYAA----IHYFkLHDLLDE-------KCYSLSSGMQKIVAIAR 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALD-KAREGRTCIMIAHRLSTIQNA 370
Cdd:PRK13541  137 LIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 25-131 6.63e-08

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 53.67  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV 104
Cdd:cd18573   181 KVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDL 260

                          90       100
                  ....*....|....*....|....*....
gi 1495939436 105 --FLVFSAVVFGAMalGQTSSFAPDYAKA 131
Cdd:cd18573   261 tsFLMYAVYVGSSV--SGLSSFYSELMKG 287
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 171-385 6.84e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 54.73  E-value: 6.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  171 AFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL----ERFYDPLDGEMLFDGKNAKTLNIQwLRAQIGIV 246
Cdd:TIGR00956   65 LKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKH-YRGDVVYN 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  247 SQEPILF-DCTIAENIAY-----GDNSREVSHEEIVKAAKEANIHSFIDSLPDKYNTRVGD---KGtqLSGGQKQRIAIA 317
Cdd:TIGR00956  144 AETDVHFpHLTVGETLDFaarckTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIA 221

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436  318 RALVRQPQILLLDEATSALDTESekivqeALDKAREGRTCIMIAHRLSTI------QNA----DKIAVIQNGKVVEQG 385
Cdd:TIGR00956  222 EASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFG 293
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 279-390 7.43e-08

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: 54.63  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 279 AKEANIHSFIDSLPD---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PQILLLDEATSALDTESEK----IVQEAL 348
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1495939436 349 DKareGRTCIMIAHRLSTIQNADKIAVI------QNGKVVEQGTHQQL 390
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
PLN03140 PLN03140
ABC transporter G family member; Provisional
 180-365 9.62e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 54.47  E-value: 9.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  180 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLDGEMLFDG--KNAKTLniqwlrAQI-GIVSQEPILF- 253
Cdd:PLN03140   893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpKKQETF------ARIsGYCEQNDIHSp 966

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  254 DCTIAENIAYGDNSR---EVSHEEIVKAAKEANIHSFIDSLPDKYntrVGDKG-TQLSGGQKQRIAIARALVRQPQILLL 329
Cdd:PLN03140   967 QVTVRESLIYSAFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAI---VGLPGvTGLSTEQRKRLTIAVELVANPSIIFM 1043

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1495939436  330 DEATSALDTESEKIVQEAL-DKAREGRTCIMIAHRLS 365
Cdd:PLN03140  1044 DEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 287-385 1.19e-07

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: 51.17  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 287 FIDSLPDKYNT-----RVGDKGTQLSGGQKQRIAIARALVRQPQ--ILLLDEATSALDTESEKIVQEALDKAR-EGRTCI 358
Cdd:cd03238    64 FIDQLQFLIDVglgylTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVI 143

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1495939436 359 MIAHRLSTIQNADKI------AVIQNGKVVEQG 385
Cdd:cd03238   144 LIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 190-365 1.31e-07

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 52.37  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 190 VEKGQTLALVGSSGCGKSTVVQLLE--------RFYDPLDG----------------EMLFDGKNAKTLNIQWlraqigi 245
Cdd:cd03236    23 PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWdeildefrgselqnyfTKLLEGDVKVIVKPQY------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 246 VSQEPILFDCTIAENIAYGDNSREVshEEIVKAAKeanihsfIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPQ 325
Cdd:cd03236    96 VDLIPKAVKGKVGELLKKKDERGKL--DELVDQLE-------LRHVLDR-------NIDQLSGGELQRVAIAAALARDAD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1495939436 326 ILLLDEATSALDTESE----KIVQEAldkAREGRTCIMIAHRLS 365
Cdd:cd03236   160 FYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
180-367 1.64e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 53.27  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 180 VKILQGLNLKVE-----KGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlraqigiVSQEPilfd 254
Cdd:PRK13409  347 TKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----------------ISYKP---- 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 255 ctiaeniAYGDNSREVSHEEIVKAAKEANIHSFIDS-------LPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQIL 327
Cdd:PRK13409  407 -------QYIKPDYDGTVEDLLRSITDDLGSSYYKSeiikplqLERLLDKNVKD----LSGGELQRVAIAACLSRDADLY 475

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1495939436 328 LLDEATSALDTESEKIVQEALDKAREGR--TCIMIAHRLSTI 367
Cdd:PRK13409  476 LLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 177-392 2.10e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 52.70  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 177 RPEVKILQG-----LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQ-WLRAQIGIVSQEP 250
Cdd:PRK10762  257 RLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDR 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 251 ----ILFDCTIAENI---AYGDNSREVSHeeIVKAAKEANIHSFIDSLPDKYNTR---VGdkgtQLSGGQKQRIAIARAL 320
Cdd:PRK10762  337 krdgLVLGMSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMeqaIG----LLSGGNQQKVAIARGL 410

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1495939436 321 VRQPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIMIAHRLSTIQN-ADKIAVIQNGKV-----VEQGTHQQLLA 392
Cdd:PRK10762  411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
187-395 2.41e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.82  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 187 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE-MLFdGK--NAKTLNIqwlRAQIGIVSQEPILF-DCTIAENIA 262
Cdd:NF033858  286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLF-GQpvDAGDIAT---RRRVGYMSQAFSLYgELTVRQNLE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 263 -----YGdnsreVSHEEIVKAAKEAnIHSF-----IDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEA 332
Cdd:NF033858  362 lharlFH-----LPAAEIAARVAEM-LERFdladvADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEP 424

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 333 TSALDTESEKIVQEAL-DKAREGRTCIMIA-HRLSTIQNADKIAVIQNGKVVEQGTHQQLLAEKG 395
Cdd:NF033858  425 TSGVDPVARDMFWRLLiELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
305-392 2.74e-07

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 52.11  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTI-QNADKIAVIQNGKV 381
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237

                          90
                  ....*....|.
gi 1495939436 382 VEQGTHQQLLA 392
Cdd:PRK15093  238 VETAPSKELVT 248
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 169-367 6.15e-07

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: 51.32  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 169 DVAFNYPNRpeVKILQGLNLKVE-----KGQTLALVGSSGCGKSTVVQLLErfydpldGEMLFD-GKNAKTLNI----QW 238
Cdd:COG1245   339 ETLVEYPDL--TKSYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILA-------GVLKPDeGEVDEDLKIsykpQY 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 239 LRAQIGIVSQEpILFDcTIAENIaygDNSREvsHEEIVKAAKeanihsfIDSLPDKYntrVGDkgtqLSGGQKQRIAIAR 318
Cdd:COG1245   410 ISPDYDGTVEE-FLRS-ANTDDF---GSSYY--KTEIIKPLG-------LEKLLDKN---VKD----LSGGELQRVAIAA 468

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIMIAHRLSTI 367
Cdd:COG1245   469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
304-396 8.49e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 50.94  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 304 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIMIAHRLSTIQNA-DKIAVIQNGKV 381
Cdd:PRK09700  408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRL 487

                          90
                  ....*....|....*
gi 1495939436 382 VEQGTHQQLLAEKGI 396
Cdd:PRK09700  488 TQILTNRDDMSEEEI 502
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 186-381 1.42e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 50.43  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 186 LNLKVEKGQTLALVGSSGCGKStvvQLLERFY---DPLDGEMLFDGKNAKTLNIQwLRAQIGIV-----SQEPILF-DCT 256
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 257 IAENI---AYGDNSRevsheeIVKAAKEANIHsfidslpDKYNTRVGDKGTQ-------LSGGQKQRIAIARALVRQPQI 326
Cdd:PRK15439  358 LAWNVcalTHNRRGF------WIKPARENAVL-------ERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQL 424

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436 327 LLLDEATSALDTESEK-IVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQNGKV 381
Cdd:PRK15439  425 LIVDEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 25-100 1.88e-06

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 49.08  E-value: 1.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436  25 KVATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHME 100
Cdd:cd18572   176 QVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMS 251
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 26-117 2.35e-06

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 49.02  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  26 VATEVIENIRTVASLTRERkFELM-YGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNV 104
Cdd:cd18576   177 IVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDL 255

                          90
                  ....*....|....*
gi 1495939436 105 --FLVFSAVVFGAMA 117
Cdd:cd18576   256 vaFLLYTLFIAGSIG 270
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
300-395 2.36e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 300 GDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESE-KIVQEALDKAREGRTCIMIAHRLSTI-QNADKIAVIQ 377
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218

                          90
                  ....*....|....*...
gi 1495939436 378 NGKVVEQGTHQQLLAEKG 395
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 305-366 4.17e-06

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: 49.01  E-value: 4.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436 305 QLSGGQKQRIAIARALVRQPQILLLDEATSALD----TESEKIVQEAldkAREGRTCIMIAHRLST 366
Cdd:COG1245   212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 27-135 7.35e-06

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 47.16  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  27 ATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEYKNVFL 106
Cdd:cd07346   181 LQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVA 260

                          90       100
                  ....*....|....*....|....*....
gi 1495939436 107 VFSAVVFGAMALGQTSSFAPDYAKAKISA 135
Cdd:cd07346   261 FLAYLGMLFGPIQRLANLYNQLQQALASL 289
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 305-387 1.39e-05

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 45.04  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 305 QLSGGQKQRIAIARAL----VRQPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIMIAHRLSTIQNADKIAVIqnG 379
Cdd:cd03227    77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHI--K 154


                  ....*...
gi 1495939436 380 KVVEQGTH 387
Cdd:cd03227   155 KVITGVYK 162
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
190-364 1.59e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.11  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 190 VEKGQTLALVGSSGCGKSTVVQLL---------------------ERF-----YDPLdgEMLFDGKNAKTLNIQWlraqi 243
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRFrgtelQNYF--KKLYNGEIKVVHKPQY----- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 244 giVSQEPILFDCTIaeniaygdnsrevshEEIVKAAKEANIhsfIDSLPDKYN-TRVGDKG-TQLSGGQKQRIAIARALV 321
Cdd:PRK13409  169 --VDLIPKVFKGKV---------------RELLKKVDERGK---LDEVVERLGlENILDRDiSELSGGELQRVAIAAALL 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1495939436 322 RQPQILLLDEATSALDtesekiVQEALDKAR------EGRTCIMIAHRL 364
Cdd:PRK13409  229 RDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDL 271
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 26-131 2.43e-05

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 45.70  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  26 VATEVIENIRTVASLTRERKFELMYGEHLQVPY----RNSVKKAHIFGFCFALSQAMMFFTyagcFRFGAYLVVNGHMEY 101
Cdd:cd18780   183 VAEESISNIRTVRSFAKETKEVSRYSEKINESYllgkKLARASGGFNGFMGAAAQLAIVLV----LWYGGRLVIDGELTT 258

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1495939436 102 K--NVFLVFSAVVfgAMALGQTSSFAPDYAKA 131
Cdd:cd18780   259 GllTSFLLYTLTV--AMSFAFLSSLYGDFMQA 288
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 165-348 2.74e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 46.32  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFdgknAKTLniqwlraQIG 244
Cdd:PRK10636  313 LKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-------KLG 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 245 IVSQEPILFDctiaeniaygdNSREVSHEEIVKAAKEANIHSFIDSLP------DKyntrVGDKGTQLSGGQKQRIAIAR 318
Cdd:PRK10636  379 YFAQHQLEFL-----------RADESPLQHLARLAPQELEQKLRDYLGgfgfqgDK----VTEETRRFSGGEKARLVLAL 443

                         170       180       190
                  ....*....|....*....|....*....|
gi 1495939436 319 ALVRQPQILLLDEATSALDTESEKIVQEAL 348
Cdd:PRK10636  444 IVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
PLN03073 PLN03073
ABC transporter F family; Provisional
 305-337 4.67e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 45.62  E-value: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1495939436 305 QLSGGQKQRIAIARALVRQPQILLLDEATSALD 337
Cdd:PLN03073  344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
183-393 4.72e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 44.81  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 183 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIgivsqepilfdcTIAENIA 262
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQL------------TGIENIE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 263 YGDNSREVSHEEIVKAAKE----ANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPQILLLDEATSALDt 338
Cdd:PRK13546  108 FKMLCMGFKRKEIKAMTPKiiefSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 339 esEKIVQEALDKARE----GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQGTHQQLLAE 393
Cdd:PRK13546  176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 167-385 5.79e-05

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 45.27  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 167 VKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPldgemlfdgkNAKTLNIQWLRAQIGIV 246
Cdd:PRK13545   24 LKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMP----------NKGTVDIKGSAALIAIS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 247 SQepILFDCTIAENIAYGDNSREVSHEEIVKAAKE----ANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVR 322
Cdd:PRK13545   94 SG--LNGQLTGIENIELKGLMMGLTKEKIKEIIPEiiefADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1495939436 323 QPQILLLDEATSALDtesEKIVQEALDKARE----GRTCIMIAHRLSTIQN-ADKIAVIQNGKVVEQG 385
Cdd:PRK13545  161 NPDILVIDEALSVGD---QTFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYG 225
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 306-377 8.39e-05

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 42.94  E-value: 8.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436 306 LSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIMIAHRLSTIQN-ADKIAVIQ 377
Cdd:cd03222    72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 130-349 1.06e-04

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 44.54  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 130 KAKISAahlfllFERVPSidsySEEGEKPET----------FGGS-LTVKDVAFNYPNRPevkILQGLNLKVEKGQTLAL 198
Cdd:TIGR03719 287 KARLAR------YEELLS----QEFQKRNETaeiyippgprLGDKvIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGV 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 199 VGSSGCGKSTVVQLLERFYDPLDGEMLFdGKNAKtlniqwlraqIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIv 276
Cdd:TIGR03719 354 IGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNKTVWEEISGGLDIIKLGKREI- 421

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1495939436 277 kaAKEANIHSFIDSLPDKyNTRVGdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD 349
Cdd:TIGR03719 422 --PSRAYVGRFNFKGSDQ-QKKVG----QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
uvrA PRK00349
excinuclease ABC subunit UvrA;
298-397 1.35e-04

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 44.29  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 298 RVGDKGTQLSGGQKQRIAIARALVRQPQ---ILLLDEATSALDTES----EKIVQEALDKareGRTCIMIAHRLSTIQNA 370
Cdd:PRK00349  823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1495939436 371 DKIavI--------QNGKVVEQGTHQQLLAEKGIY 397
Cdd:PRK00349  900 DWI--IdlgpeggdGGGEIVATGTPEEVAKVEASY 932
GguA NF040905
sugar ABC transporter ATP-binding protein;
165-382 2.28e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 43.24  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 165 LTVKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKS-TVVQLLERFYDP-LDGEMLFDGKNAKTLNI-QWLRA 241
Cdd:NF040905  258 FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVsDAIDA 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 242 QIGIVSQEP-----ILFDcTIAENIAYGdNSREVSHEEIVKAAKEANIhsfIDSLPDKYNTR---VGDKGTQLSGGQKQR 313
Cdd:NF040905  338 GLAYVTEDRkgyglNLID-DIKRNITLA-NLGKVSRRGVIDENEEIKV---AEEYRKKMNIKtpsVFQKVGNLSGGNQQK 412

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495939436 314 IAIARALVRQPQILLLDEATSALDT----ESEKIVQEAldkAREGRTCIMIAHRL-STIQNADKIAVIQNGKVV 382
Cdd:NF040905  413 VVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVISSELpELLGMCDRIYVMNEGRIT 483
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 306-385 5.96e-04

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 41.09  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 306 LSGGQKQRIAIARAL------VrqpqILLLDEATSAL-DTESEKIVqEALDKARE-GRTCIMIAHRLSTIQNADKI---- 373
Cdd:cd03270   138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLhPRDNDRLI-ETLKRLRDlGNTVLVVEHDEDTIRAADHVidig 212

                          90
                  ....*....|....
gi 1495939436 374 --AVIQNGKVVEQG 385
Cdd:cd03270   213 pgAGVHGGEIVAQG 226
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 276-394 1.09e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 41.35  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  276 VKAAKEANIHSFIDSLPdkyntrVGDKGTQLSGGQKQRIAIARALV---RQPQILLLDEATSALDTESEKIVQEALDK-A 351
Cdd:PRK00635  1676 IQKPLQALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlV 1749

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1495939436  352 REGRTCIMIAHRLSTIQNADKIAVI------QNGKVVEQGTHQQLLAEK 394
Cdd:PRK00635  1750 SLGHSVIYIDHDPALLKQADYLIEMgpgsgkTGGKILFSGPPKDISASK 1798
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
304-397 1.64e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 40.78  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436 304 TQLSGGQKQRIAIARALVRQPQ---ILLLDEATSALDTESEKIVQEALDKARE-GRTCIMIAHRLSTIQNADKIavI--- 376
Cdd:COG0178   825 TTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWI--Idlg 902

                          90       100
                  ....*....|....*....|....*.
gi 1495939436 377 -----QNGKVVEQGTHQQLLAEKGIY 397
Cdd:COG0178   903 peggdGGGEIVAEGTPEEVAKVKASY 928
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 26-99 1.97e-03

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 39.99  E-value: 1.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1495939436  26 VATEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFG---FCFALSQAMMFftyAGCFRFGAYLVVNGHM 99
Cdd:cd18784   177 VAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGgyvWSNELTELALT---VSTLYYGGHLVITGQI 250
PRK01889 PRK01889
GTPase RsgA; Reviewed
 190-213 2.50e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 39.53  E-value: 2.50e-03
                          10        20
                  ....*....|....*....|....*
gi 1495939436 190 VEKGQTLALVGSSGCGKSTVV-QLL 213
Cdd:PRK01889  192 LSGGKTVALLGSSGVGKSTLVnALL 216
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 306-373 3.69e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.81  E-value: 3.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1495939436  306 LSGGQKQRIAIARAL---VRQPQILLLDEATSALDTES-EKIVQEALDKAREGRTCIMIAHRLSTIQNADKI 373
Cdd:PRK00635   810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 309-360 3.86e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 39.49  E-value: 3.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1495939436 309 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKaregRTCIMI 360
Cdd:PRK15064  159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE----RNSTMI 206
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
 29-99 4.26e-03

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 38.72  E-value: 4.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1495939436  29 EVIENIRTVASLTRE----RKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAgcfrFGAYLVVNGHM 99
Cdd:cd18566   185 ETLTGIHTIKAMAMEpqmlRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVA----FGALLVINGDL 255
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 28-132 5.52e-03

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 38.57  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495939436  28 TEVIENIRTVASLTRERKFELMYGEHLQVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMEyknV--- 104
Cdd:cd18551   179 ERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALT---Vgtl 255

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1495939436 105 --FLVFsavVFGAMA-LGQTSSFAPDYAKAK 132
Cdd:cd18551   256 vaFLLY---LFQLITpLSQLSSFFTQLQKAL 283
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
 305-340 5.93e-03

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 35.67  E-value: 5.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1495939436 305 QLSGGQKQR---IAIARALVRQ----------PQILLLDEATSALDTES 340
Cdd:pfam13558  32 GLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEEN 80
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 304-373 7.24e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.80  E-value: 7.24e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1495939436  304 TQLSGGQKQRIAIAraLV-----RQPQ-ILLLDEATSALDTESEKIVQEALDKAREGRTCIMIAHRLSTIQNADKI 373
Cdd:pfam02463 1076 DLLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
 
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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